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Conserved domains on  [gi|432857606|ref|XP_004068713|]
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5-aminolevulinate synthase, nonspecific, mitochondrial isoform X2 [Oryzias latipes]

Protein Classification

Preseq_ALAS and KBL_like domain-containing protein( domain architecture ID 11181659)

Preseq_ALAS and KBL_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 180-585 0e+00

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


The actual alignment was detected with superfamily member TIGR01821:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 402  Bit Score: 656.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  180 FQYDDFFEKKIEEKKSDHTYRVFKTVNRLATEFPMADDFtgSLEDKREVSVWCSNDYLGMSRHPQVVQSIMDTLQKHGSG 259
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWH--RPDGAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  260 AGGTRNISGTSKFHVELEQELADLHKKDAALLFTSCFVANDSTLFTLAKMLPGCEIYSDGGNHASMIQGIRNSGAKKFVF 339
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  340 RHNDVAHLRELLQKGDPSKPKIVAFETVHSMDGAVCPLEEMCDLAHEFGAITFVDEVHAVGLYGARGGGIGDRDGIMHKM 419
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  420 DIISGTLGKAFGCVGGYIASTSALVDTVRSYAAGFIFTTSLPPMLLAGARQSIQILKGEEgrTLRRKHQRNVKLLRQMLM 499
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  500 DSGLPVVHCPSHIIPIRVSNAEKNTEVCDIMMSRHNIYVQAINYPTVARGEELLRIAPTPHHTPEMMKYFVERLVQTWKE 579
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 432857606  580 VGLDLK 585
Cdd:TIGR01821 397 LGLPLS 402
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-124 1.08e-43

5-aminolevulinate synthase presequence; The N terminal presequence domain found in 5-aminolevulinate synthase exists as an amphipathic helix, with a positively charged surface provided by lysine residues and no stable helix at the N-terminus. The domain is essential for the import process by which ALAS is transported into the mitochondria: translocase of the outer membrane (Tom) and translocase of the inner membrane protein complexes appear responsible for recognition and import through the mitochondrial membrane. The protein Tom20 is anchored to the mitochondrial outer membrane, and its interaction with presequences is thought to be the recognition step which allows subsequent import.


:

Pssm-ID: 462658  Cd Length: 114  Bit Score: 151.88  E-value: 1.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606    2 EVIVRRCPFLASVPQAFFQQTKKSLVTYAQRCPIMMelaakpmapsmARALCSSSSHQQSGSNNVEAPKQE--EESKLPS 79
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-----------TRALSTSSANLQGEKEETPVAGPTakQAKALPL 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 432857606   80 GHPMPSQGQNVASKCPFLAAEMKQKNSAVFRQVAMEFQEDVQEVR 124
Cdd:pfam09029  70 GHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 180-585 0e+00

5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273820 [Multi-domain]  Cd Length: 402  Bit Score: 656.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  180 FQYDDFFEKKIEEKKSDHTYRVFKTVNRLATEFPMADDFtgSLEDKREVSVWCSNDYLGMSRHPQVVQSIMDTLQKHGSG 259
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWH--RPDGAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  260 AGGTRNISGTSKFHVELEQELADLHKKDAALLFTSCFVANDSTLFTLAKMLPGCEIYSDGGNHASMIQGIRNSGAKKFVF 339
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  340 RHNDVAHLRELLQKGDPSKPKIVAFETVHSMDGAVCPLEEMCDLAHEFGAITFVDEVHAVGLYGARGGGIGDRDGIMHKM 419
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  420 DIISGTLGKAFGCVGGYIASTSALVDTVRSYAAGFIFTTSLPPMLLAGARQSIQILKGEEgrTLRRKHQRNVKLLRQMLM 499
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  500 DSGLPVVHCPSHIIPIRVSNAEKNTEVCDIMMSRHNIYVQAINYPTVARGEELLRIAPTPHHTPEMMKYFVERLVQTWKE 579
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 432857606  580 VGLDLK 585
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 226-577 8.86e-179

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 510.18  E-value: 8.86e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 226 REVSVWCSNDYLGMSRHPQVVQSIMDTLQKHGSGAGGTRNISGTSKFHVELEQELADLHKKDAALLFTSCFVANDSTLFT 305
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 306 LakMLPGCEIYSDGGNHASMIQGIRNSGAKKFVFRHNDVAHLRELLQKGD-PSKPKIVAFETVHSMDGAVCPLEEMCDLA 384
Cdd:cd06454   81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 385 HEFGAITFVDEVHAVGLYGARGGGIGDRDGIMHKMDIISGTLGKAFGCVGGYIASTSALVDTVRSYAAGFIFTTSLPPML 464
Cdd:cd06454  159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 465 LAGARQSIQILKGEEGRtlRRKHQRNVKLLRQMLMDSGLPVVHCPSHIIPIRV-SNAEKNTEVCDiMMSRHNIYVQAINY 543
Cdd:cd06454  239 AAAALAALEVLQGGPER--RERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIgDDPAKAVAFSD-ALLERGIYVQAIRY 315

                        330       340       350
                 ....*....|....*....|....*....|....
gi 432857606 544 PTVARGEELLRIAPTPHHTPEMMKYFVERLVQTW 577
Cdd:cd06454  316 PTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 180-591 4.11e-174

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 500.54  E-value: 4.11e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 180 FQYDDFFEKKIEEKKSDHTYRVFKTVNRLATEFPMADDFTGslEDKREVSVWCSNDYLGMSRHPQVVQSIMDTLQKHGSG 259
Cdd:PRK13392   2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGP--DGPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 260 AGGTRNISGTSKFHVELEQELADLHKKDAALLFTSCFVANDSTLFTLAKMLPGCEIYSDGGNHASMIQGIRNSGAKKFVF 339
Cdd:PRK13392  80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 340 RHNDVAHLRELLQKGDPSKPKIVAFETVHSMDGAVCPLEEMCDLAHEFGAITFVDEVHAVGLYGARGGGIGDRDGIMHKM 419
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 420 DIISGTLGKAFGCVGGYIASTSALVDTVRSYAAGFIFTTSLPPMLLAGARQSIQILKgeEGRTLRRKHQRNVKLLRQMLM 499
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKLN 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 500 DSGLPVVHCPSHIIPIRVSNAEKNTEVCDIMMSRHNIYVQAINYPTVARGEELLRIAPTPHHTPEMMKYFVERLVQTWKE 579
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397

                        410
                 ....*....|..
gi 432857606 580 VGLDLKPHSSAE 591
Cdd:PRK13392 398 LELPRWREAAQA 409
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 182-579 4.13e-157

7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439926 [Multi-domain]  Cd Length: 385  Bit Score: 456.44  E-value: 4.13e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 182 YDDFFEKKIEEKKSDHTYRVFKTVNRLATEFPMADDftgsledkREVSVWCSNDYLGMSRHPQVVQSIMDTLQKHGSGAG 261
Cdd:COG0156    1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 262 GTRNISGTSKFHVELEQELADLHKKDAALLFTSCFVANDSTLFTLAKmlPGCEIYSDGGNHASMIQGIRNSGAKKFVFRH 341
Cdd:COG0156   73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 342 NDVAHLRELLQKGDPSKPKIVAFETVHSMDGAVCPLEEMCDLAHEFGAITFVDEVHAVGLYGARGGGIGDRDGIMHKMDI 421
Cdd:COG0156  151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 422 ISGTLGKAFGCVGGYIASTSALVDTVRSYAAGFIFTTSLPPMLLAGARQSIQILKGEEGRtlRRKHQRNVKLLRQMLMDS 501
Cdd:COG0156  231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPEL--RERLWENIAYFREGLKEL 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 432857606 502 GLPVVHCPSHIIPIRVSNAEKNTEVCDIMMSRhNIYVQAINYPTVARGEELLRIAPTPHHTPEMMKYFVERLVQTWKE 579
Cdd:COG0156  309 GFDLGPSESPIVPVIVGDAERALALADALLER-GIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
231-573 3.03e-72

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 236.43  E-value: 3.03e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  231 WCSNDYLGMsrhpqVVQSIMDTLQKHGsgAGGTRNISGTSKFHVELEQELADLH--------KKDAALLFTSCFVANDST 302
Cdd:pfam00155   6 LGSNEYLGD-----TLPAVAKAEKDAL--AGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGANIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  303 LFTLAKMlPGCEIYSDGGNHASMIQGIRNSGAKKFVFR-------HNDVAHLRELLQKgdpsKPKIVAFETVHSMDGAVC 375
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKE----KPKVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  376 PLEEMCDLA---HEFGAITFVDEVHAVGLYGARGGGIGDRDGIMHKMDIISGTLGKAFGCVG---GYIASTSALVDTVRS 449
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLRK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  450 YAAGFIFTTSLPPMLLAGARQSIQILkgEEGRTLRRKHQRNVKLLRQMLMDSGLPVVHCPSHIIPIRVSNAEKNTEVCDI 529
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDPLLVA--SELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQV 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 432857606  530 MMSRHNIYVQAINYPTVargEELLRIAPTpHHTPEMMKYFVERL 573
Cdd:pfam00155 312 LLEEVGVYVTPGSSPGV---PGWLRITVA-GGTEEELEELLEAI 351
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-124 1.08e-43

5-aminolevulinate synthase presequence; The N terminal presequence domain found in 5-aminolevulinate synthase exists as an amphipathic helix, with a positively charged surface provided by lysine residues and no stable helix at the N-terminus. The domain is essential for the import process by which ALAS is transported into the mitochondria: translocase of the outer membrane (Tom) and translocase of the inner membrane protein complexes appear responsible for recognition and import through the mitochondrial membrane. The protein Tom20 is anchored to the mitochondrial outer membrane, and its interaction with presequences is thought to be the recognition step which allows subsequent import.


Pssm-ID: 462658  Cd Length: 114  Bit Score: 151.88  E-value: 1.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606    2 EVIVRRCPFLASVPQAFFQQTKKSLVTYAQRCPIMMelaakpmapsmARALCSSSSHQQSGSNNVEAPKQE--EESKLPS 79
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-----------TRALSTSSANLQGEKEETPVAGPTakQAKALPL 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 432857606   80 GHPMPSQGQNVASKCPFLAAEMKQKNSAVFRQVAMEFQEDVQEVR 124
Cdd:pfam09029  70 GHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 180-585 0e+00

5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273820 [Multi-domain]  Cd Length: 402  Bit Score: 656.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  180 FQYDDFFEKKIEEKKSDHTYRVFKTVNRLATEFPMADDFtgSLEDKREVSVWCSNDYLGMSRHPQVVQSIMDTLQKHGSG 259
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWH--RPDGAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  260 AGGTRNISGTSKFHVELEQELADLHKKDAALLFTSCFVANDSTLFTLAKMLPGCEIYSDGGNHASMIQGIRNSGAKKFVF 339
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  340 RHNDVAHLRELLQKGDPSKPKIVAFETVHSMDGAVCPLEEMCDLAHEFGAITFVDEVHAVGLYGARGGGIGDRDGIMHKM 419
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  420 DIISGTLGKAFGCVGGYIASTSALVDTVRSYAAGFIFTTSLPPMLLAGARQSIQILKGEEgrTLRRKHQRNVKLLRQMLM 499
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  500 DSGLPVVHCPSHIIPIRVSNAEKNTEVCDIMMSRHNIYVQAINYPTVARGEELLRIAPTPHHTPEMMKYFVERLVQTWKE 579
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 432857606  580 VGLDLK 585
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 226-577 8.86e-179

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 510.18  E-value: 8.86e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 226 REVSVWCSNDYLGMSRHPQVVQSIMDTLQKHGSGAGGTRNISGTSKFHVELEQELADLHKKDAALLFTSCFVANDSTLFT 305
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 306 LakMLPGCEIYSDGGNHASMIQGIRNSGAKKFVFRHNDVAHLRELLQKGD-PSKPKIVAFETVHSMDGAVCPLEEMCDLA 384
Cdd:cd06454   81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 385 HEFGAITFVDEVHAVGLYGARGGGIGDRDGIMHKMDIISGTLGKAFGCVGGYIASTSALVDTVRSYAAGFIFTTSLPPML 464
Cdd:cd06454  159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 465 LAGARQSIQILKGEEGRtlRRKHQRNVKLLRQMLMDSGLPVVHCPSHIIPIRV-SNAEKNTEVCDiMMSRHNIYVQAINY 543
Cdd:cd06454  239 AAAALAALEVLQGGPER--RERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIgDDPAKAVAFSD-ALLERGIYVQAIRY 315

                        330       340       350
                 ....*....|....*....|....*....|....
gi 432857606 544 PTVARGEELLRIAPTPHHTPEMMKYFVERLVQTW 577
Cdd:cd06454  316 PTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 180-591 4.11e-174

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 500.54  E-value: 4.11e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 180 FQYDDFFEKKIEEKKSDHTYRVFKTVNRLATEFPMADDFTGslEDKREVSVWCSNDYLGMSRHPQVVQSIMDTLQKHGSG 259
Cdd:PRK13392   2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGP--DGPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 260 AGGTRNISGTSKFHVELEQELADLHKKDAALLFTSCFVANDSTLFTLAKMLPGCEIYSDGGNHASMIQGIRNSGAKKFVF 339
Cdd:PRK13392  80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 340 RHNDVAHLRELLQKGDPSKPKIVAFETVHSMDGAVCPLEEMCDLAHEFGAITFVDEVHAVGLYGARGGGIGDRDGIMHKM 419
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 420 DIISGTLGKAFGCVGGYIASTSALVDTVRSYAAGFIFTTSLPPMLLAGARQSIQILKgeEGRTLRRKHQRNVKLLRQMLM 499
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKLN 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 500 DSGLPVVHCPSHIIPIRVSNAEKNTEVCDIMMSRHNIYVQAINYPTVARGEELLRIAPTPHHTPEMMKYFVERLVQTWKE 579
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397

                        410
                 ....*....|..
gi 432857606 580 VGLDLKPHSSAE 591
Cdd:PRK13392 398 LELPRWREAAQA 409
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 182-579 4.13e-157

7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439926 [Multi-domain]  Cd Length: 385  Bit Score: 456.44  E-value: 4.13e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 182 YDDFFEKKIEEKKSDHTYRVFKTVNRLATEFPMADDftgsledkREVSVWCSNDYLGMSRHPQVVQSIMDTLQKHGSGAG 261
Cdd:COG0156    1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 262 GTRNISGTSKFHVELEQELADLHKKDAALLFTSCFVANDSTLFTLAKmlPGCEIYSDGGNHASMIQGIRNSGAKKFVFRH 341
Cdd:COG0156   73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 342 NDVAHLRELLQKGDPSKPKIVAFETVHSMDGAVCPLEEMCDLAHEFGAITFVDEVHAVGLYGARGGGIGDRDGIMHKMDI 421
Cdd:COG0156  151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 422 ISGTLGKAFGCVGGYIASTSALVDTVRSYAAGFIFTTSLPPMLLAGARQSIQILKGEEGRtlRRKHQRNVKLLRQMLMDS 501
Cdd:COG0156  231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPEL--RERLWENIAYFREGLKEL 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 432857606 502 GLPVVHCPSHIIPIRVSNAEKNTEVCDIMMSRhNIYVQAINYPTVARGEELLRIAPTPHHTPEMMKYFVERLVQTWKE 579
Cdd:COG0156  309 GFDLGPSESPIVPVIVGDAERALALADALLER-GIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 224-573 1.37e-94

8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273303 [Multi-domain]  Cd Length: 360  Bit Score: 294.95  E-value: 1.37e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  224 DKREVSVWCSNDYLGMSRHPQVVQSIMDTLQKHGSGAGGTRNISGTSKFHVELEQELADLHKKDAALLFTSCFVANDSTL 303
Cdd:TIGR00858  14 DGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  304 FTLAKmlPGCEIYSDGGNHASMIQGIRNSGAKKFVFRHNDVAHLRELLQKGDPSKPKIVAFETVHSMDGAVCPLEEMCDL 383
Cdd:TIGR00858  94 SALVG--KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVAL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  384 AHEFGAITFVDEVHAVGLYGARGGGIGDRDGIMHKMDIIS-GTLGKAFGCVGGYIASTSALVDTVRSYAAGFIFTTSLPP 462
Cdd:TIGR00858 172 AERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQvGTLSKALGSYGAYVAGSQALIDYLINRARTLIFSTALPP 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  463 MLLAGARQSIQILkgEEGRTLRRKHQRNVKLLRQMLMDSGLPVVHCPSHIIPIRVSNAEKNTEVCDiMMSRHNIYVQAIN 542
Cdd:TIGR00858 252 AVAAAALAALELI--QEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAE-ELQQQGIFVGAIR 328

                         330       340       350
                  ....*....|....*....|....*....|.
gi 432857606  543 YPTVARGEELLRIAPTPHHTPEMMKYFVERL 573
Cdd:TIGR00858 329 PPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 184-577 5.52e-94

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 294.37  E-value: 5.52e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 184 DFFEKKIEEKKSDHTYRVFKTVNRlatefpmADDFTGSLEDKREVSvWCSNDYLGMSRHPQVVQSIMDTLQKHGSGAGGT 263
Cdd:PRK05958   5 DRLEAALAQRRAAGLYRSLRPREG-------GAGRWLVVDGRRMLN-FASNDYLGLARHPRLIAAAQQAARRYGAGSGGS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 264 RNISGTSKFHVELEQELADLHKKDAALLFTSCFVANDSTLFTLAKmlPGCEIYSDGGNHASMIQGIRNSGAKKFVFRHND 343
Cdd:PRK05958  77 RLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAG--KGDLIVSDKLNHASLIDGARLSRARVRRYPHND 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 344 VAHLRELLQKgDPSKPKIVAFETVHSMDGAVCPLEEMCDLAHEFGAITFVDEVHAVGLYGARGG-GIGDRDGIMHKMDII 422
Cdd:PRK05958 155 VDALEALLAK-WRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRgLAAEAGLAGEPDVIL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 423 SGTLGKAFGCVGGYIASTSALVDTVRSYAAGFIFTTSLPPMLLAGARQSIQILKGEEGRtlRRKHQRNVKLLRQMLMDSG 502
Cdd:PRK05958 234 VGTLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPER--RERLAALIARLRAGLRALG 311

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 432857606 503 LPVVHCPSHIIPIRVSNAEKNTEVCDiMMSRHNIYVQAINYPTVARGEELLRIAPTPHHTPEMMKYFVERLVQTW 577
Cdd:PRK05958 312 FQLMDSQSAIQPLIVGDNERALALAA-ALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 184-582 4.42e-88

2-amino-3-ketobutyrate coenzyme A ligase; Provisional


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 279.39  E-value: 4.42e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 184 DFFEKKIEEKKSDHTYRVFKTVnrlatEFPMADDFTgsLEDKREVSVWCSNDYLGMSRHPQVVQSIMDTLQKHGSGAGGT 263
Cdd:PRK06939   7 AQLREELEEIKAEGLYKEERVI-----TSPQGADIT--VADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 264 RNISGTSKFHVELEQELADLHKKDAALLFTSCFVANDSTLFTLakMLPGCEIYSDGGNHASMIQGIRNSGAKKFVFRHND 343
Cdd:PRK06939  80 RFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETL--LGKEDAIISDALNHASIIDGVRLCKAKRYRYANND 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 344 VAHLRELLQ--KGDPSKPKIVAFETVHSMDGAVCPLEEMCDLAHEFGAITFVDEVHAVGLYGARGGGIGDRDGIMHKMDI 421
Cdd:PRK06939 158 MADLEAQLKeaKEAGARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDI 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 422 ISGTLGKAF-GCVGGYIASTSALVDTVRSYAAGFIFTTSLPPMLLAGARQSIQILkgEEGRTLRRKHQRNVKLLRQMLMD 500
Cdd:PRK06939 238 ITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELL--EESDELRDRLWENARYFREGMTA 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 501 SGLPVVHCPSHIIPIRVSNAEKNTEVCDIMMSRhNIYVQAINYPTVARGEELLRIAPTPHHTPEMMKYFVERLVQTWKEV 580
Cdd:PRK06939 316 AGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEE-GVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKEL 394


                 ..
gi 432857606 581 GL 582
Cdd:PRK06939 395 GV 396
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
231-573 3.03e-72

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 236.43  E-value: 3.03e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  231 WCSNDYLGMsrhpqVVQSIMDTLQKHGsgAGGTRNISGTSKFHVELEQELADLH--------KKDAALLFTSCFVANDST 302
Cdd:pfam00155   6 LGSNEYLGD-----TLPAVAKAEKDAL--AGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGANIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  303 LFTLAKMlPGCEIYSDGGNHASMIQGIRNSGAKKFVFR-------HNDVAHLRELLQKgdpsKPKIVAFETVHSMDGAVC 375
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKE----KPKVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  376 PLEEMCDLA---HEFGAITFVDEVHAVGLYGARGGGIGDRDGIMHKMDIISGTLGKAFGCVG---GYIASTSALVDTVRS 449
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLRK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  450 YAAGFIFTTSLPPMLLAGARQSIQILkgEEGRTLRRKHQRNVKLLRQMLMDSGLPVVHCPSHIIPIRVSNAEKNTEVCDI 529
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDPLLVA--SELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQV 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 432857606  530 MMSRHNIYVQAINYPTVargEELLRIAPTpHHTPEMMKYFVERL 573
Cdd:pfam00155 312 LLEEVGVYVTPGSSPGV---PGWLRITVA-GGTEEELEELLEAI 351
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 226-573 2.75e-47

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 172.94  E-value: 2.75e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 226 REVSVWCSNDYLGMSRHPQVVQSIMDTLQKHGSGAGGTRNISGTSKFHVELEQELADLHKKDAALLFTSCFVANDSTLFT 305
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVA 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 306 L---AKMLPGCE---------IYSDGGNHASMIQGIR----NSGAKKFVFRHNDVAHLRELLQKGDPSKpKIVAFETVHS 369
Cdd:PLN02955 182 IgsvASLLAASGkplknekvaIFSDALNHASIIDGVRlaerQGNVEVFVYRHCDMYHLNSLLSSCKMKR-KVVVTDSLFS 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 370 MDGAVCPLEEMCDLAHEFGAITFVDEVHAVGLYGARGGGIGDRDGIMHKMDIISGTLGKAFGCVGGYIASTSALVDTVRS 449
Cdd:PLN02955 261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 450 YAAGFIFTTSLPPMLLAGARQSIQILKGEEGRtlRRKHQRNVKLLRQMlmdSGLPVvhcPSHIIPIRVSNAEKNTEVcdi 529
Cdd:PLN02955 341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEKWR--RKAIWERVKEFKAL---SGVDI---SSPIISLVVGNQEKALKA--- 409

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 432857606 530 mmSRH----NIYVQAINYPTVARGEELLRIAPTPHHTPEMMKYFVERL 573
Cdd:PLN02955 410 --SRYllksGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
PLN02483 PLN02483
serine palmitoyltransferase
 233-591 2.98e-45

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 167.63  E-value: 2.98e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 233 SNDYLGM-SRHPQVVQSIMDTLQKHGSGAGGTRNISGTSKFHVELEQELADLHKKDAALLFTSCFVANDSTLFTLakMLP 311
Cdd:PLN02483 107 SYNYLGFaAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPAL--IGK 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 312 GCEIYSDGGNHASMIQGIRNSGAKKFVFRHNDVAHLRELLQK----GDPS-----KPKIVAFETVHSMDGAVCPLEEMCD 382
Cdd:PLN02483 185 GGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREqiaeGQPRthrpwKKIIVIVEGIYSMEGELCKLPEIVA 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 383 LAHEFGAITFVDEVHAVGLYGARGGGIGDRDGIMHK-MDIISGTLGKAFGCVGGYIASTSALVDTVRSYAAGFIFTTSLP 461
Cdd:PLN02483 265 VCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAdVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSMS 344

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 462 PMLLAGARQSIQILKGEEGRTL-RRKHQR---NVKLLRQMLMDSGLPVV-HCPSHIIPIRVSNAEKNTEVCDIMMSRhNI 536
Cdd:PLN02483 345 PPAVQQVISAIKVILGEDGTNRgAQKLAQireNSNFFRSELQKMGFEVLgDNDSPVMPIMLYNPAKIPAFSRECLKQ-NV 423

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 432857606 537 YVQAINYP----TVARGeellRIAPTPHHTPEMMKYFVERLVQTWKEVGLDLKPHSSAE 591
Cdd:PLN02483 424 AVVVVGFPatplLLARA----RICISASHSREDLIKALEVISEVGDLVGIKYFPAEPKK 478
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
233-586 4.53e-45

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 165.18  E-value: 4.53e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 233 SNDYLGMSRHPQVVQSIMDTLQKHGSG----AGGTRNISGTSKFhvelEQELADLHKKDAALLFTSCFVANDSTLFTLAK 308
Cdd:PRK07179  61 SNDYLNLSGHPDIIKAQIAALQEEGDSlvmsAVFLHDDSPKPQF----EKKLAAFTGFESCLLCQSGWAANVGLLQTIAD 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 309 mlPGCEIYSDGGNHASMIQGIRNSGAKKFVFRHNDVAHLRELLQKGDPSkpkIVAFETVHSMDGAVCPLEEMCDLAHEFG 388
Cdd:PRK07179 137 --PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG---IIVVDSVYSTTGTIAPLADIVDIAEEFG 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 389 AITFVDEVHAVGLYGARGGGIGDRDGIMHKMDIISGTLGKAFGCVGGYIASTSALVDTVR--SYAAgfIFTTSLPPMLLA 466
Cdd:PRK07179 212 CVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPfvSYPA--IFSSTLLPHEIA 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 467 GARQSIQILKGEEGRtlRRKHQRNVKLLRQMLMDSGLPvVHCPSHIIPIrVSNAEKNTEVCDIMMSRHNIYVQAINYPTV 546
Cdd:PRK07179 290 GLEATLEVIESADDR--RARLHANARFLREGLSELGYN-IRSESQIIAL-ETGSERNTEVLRDALEERNVFGAVFCAPAT 365

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 432857606 547 ARGEELLRIAPTPHHTPEMMKYFVERLVQTWKEVGLDLKP 586
Cdd:PRK07179 366 PKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWFWK 405
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-124 1.08e-43

5-aminolevulinate synthase presequence; The N terminal presequence domain found in 5-aminolevulinate synthase exists as an amphipathic helix, with a positively charged surface provided by lysine residues and no stable helix at the N-terminus. The domain is essential for the import process by which ALAS is transported into the mitochondria: translocase of the outer membrane (Tom) and translocase of the inner membrane protein complexes appear responsible for recognition and import through the mitochondrial membrane. The protein Tom20 is anchored to the mitochondrial outer membrane, and its interaction with presequences is thought to be the recognition step which allows subsequent import.


Pssm-ID: 462658  Cd Length: 114  Bit Score: 151.88  E-value: 1.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606    2 EVIVRRCPFLASVPQAFFQQTKKSLVTYAQRCPIMMelaakpmapsmARALCSSSSHQQSGSNNVEAPKQE--EESKLPS 79
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-----------TRALSTSSANLQGEKEETPVAGPTakQAKALPL 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 432857606   80 GHPMPSQGQNVASKCPFLAAEMKQKNSAVFRQVAMEFQEDVQEVR 124
Cdd:pfam09029  70 GHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 230-536 4.23e-32

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 128.48  E-value: 4.23e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 230 VWCSNDYLGMSRHPQVVQSIMDTLQKHGSGAGGTRNISGTSKFHVELEQELADLHKKDAALLFTSCFVANDSTLFTLAKM 309
Cdd:PLN03227   2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 310 lpGCEIYSDGGNHASMIQGIRNSGAKKFVFRHNDVAHLRELLQK----------GDPSKPKIVAFETVHSMDGAVCPLEE 379
Cdd:PLN03227  82 --GDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQvraqdvalkrKPTDQRRFLVVEGLYKNTGTLAPLKE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 380 MCDLAHEFGAITFVDEVHAVGLYG--ARGGGIGDRDGIMHKMDIISGTLGKAFGCVGGYIASTSALVDTVRSYAAGFIFT 457
Cdd:PLN03227 160 LVALKEEFHYRLILDESFSFGTLGksGRGSLEHAGLKPMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 458 TSLPPMLLAGARQSI-QILKGEEgrTLRRKHQrNVKLLRQMLMDSGLPVVHCP-----------SHIIPIRVSNAEKnTE 525
Cdd:PLN03227 240 ASAPPFLAKADATATaGELAGPQ--LLNRLHD-SIANLYSTLTNSSHPYALKLrnrlvitsdpiSPIIYLRLSDQEA-TR 315

                        330
                 ....*....|.
gi 432857606 526 VCDIMMSRHNI 536
Cdd:PLN03227 316 RTDETLILDQI 326
PLN02822 PLN02822
serine palmitoyltransferase
 224-507 2.63e-30

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 124.47  E-value: 2.63e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 224 DKREVSVWCSNDYLGMSRHPQVVQSIMDTLQKHGSGAGGTRNISGTSKFHVELEQELADLHKKDAALLFTscfvandSTL 303
Cdd:PLN02822 107 NGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYS-------YGL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 304 FTLAKMLPG-CE----IYSDGGNHASMIQGIRNSGAKKFVFRHNDVAHLRELLQK---GDPSKPKI---VAFETVHSMDG 372
Cdd:PLN02822 180 STIFSVIPAfCKkgdiIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKltaENKRKKKLrryIVVEAIYQNSG 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 373 AVCPLEEMCDLAHEFGAITFVDEVHAVGLYGAR-GGGIGDRDGIMHKMDIISGTLGKAFGCVGGYIASTSALVDTVRSYA 451
Cdd:PLN02822 260 QIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSgRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSS 339

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 432857606 452 AGFIFTTSLPPMLLAGARQSIQILkgEEGRTLRRKHQRNVKLLRQMLMD-SGL--------PVVH 507
Cdd:PLN02822 340 SGYVFSASLPPYLASAAITAIDVL--EDNPSVLAKLKENIALLHKGLSDiPGLsigsntlsPIVF 402
PRK07505 PRK07505
hypothetical protein; Provisional
 221-575 4.94e-27

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 113.54  E-value: 4.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 221 SLEDKREVSVWCSNDYLGMSRHPQVVQSIMDTLQKHGsgaggTRNISgTSKFHV------ELEQELADLHkkDA-ALLFT 293
Cdd:PRK07505  41 TLADGHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTG-----SLHLS-SSRTRVrsqilkDLEEALSELF--GAsVLTFT 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 294 SCFVANDSTLFTLAK-MLPGCE----IYsDGGNHASM--IQGIRNSGAKKFVFRHNDVAHLRELLQKGdpskpKIVAF-- 364
Cdd:PRK07505 113 SCSAAHLGILPLLASgHLTGGVpphmVF-DKNAHASLniLKGICADETEVETIDHNDLDALEDICKTN-----KTVAYva 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 365 ETVHSMdGAVCPLEEMCDLAHEFGAITFVDEVHAVGLYGARGGGIGDRDGImHKMD---IISGTLGKAFGCVGGYIA-ST 440
Cdd:PRK07505 187 DGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGYVRSELD-YRLNertIIAASLGKAFGASGGVIMlGD 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 441 SALVDTVRSYAAGFIFTTSLPPMLLAGARQSIQILKGEEGRTLRRKHQRNVKLLRQMLMD--SGLPVvhcpshiiPIR-- 516
Cdd:PRK07505 265 AEQIELILRYAGPLAFSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDSLIPTeqSGSFL--------PIRli 336

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 517 -VSNAEKNTEVCDIMMSRhNIYVQAINYPTVARGEELLRIAPTPHHTPEMMKYFVERLVQ 575
Cdd:PRK07505 337 yIGDEDTAIKAAKQLLDR-GFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKE 395
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 233-532 8.47e-23

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 100.63  E-value: 8.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 233 SNDYLGMSRHPQVVQSIMDTLQKHGS-------GAGGTRNISGTSKFHVELEQELADLHKKDAALLFTSCFVANDSTLFT 305
Cdd:PRK05937  11 TNDFLGFSRSDTLVHEVEKRYRLYCRqfphaqlGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 306 LAKMLPgcEIYSDGGNHASMIQGIRNSGAKKFVFRHNDVAHLRELLQKGDP-SKPKIVAFE-TVHSMDGAVCPLEEMCDL 383
Cdd:PRK05937  91 LSSVTD--YVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQrSFGRIFIFVcSVYSFKGTLAPLEQIIAL 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 384 AHEFGAITFVDEVHAVGLYGARGGGIGDRDGIMHKMDIISgTLGKAFGCVGGYIASTSALVDTVRSYAAGFIFTTSLPPM 463
Cdd:PRK05937 169 SKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPPH 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 464 LLAgarqSIQI------LKGEEGRTLRRK-----HQR-----------------NVKLLRQMLMDSGLPV-VHCPSHIIP 514
Cdd:PRK05937 248 LLI----SIQVaydflsQEGELARKQLFRlkeyfAQKfssaapgcvqpiflpgiSEQELYSKLVETGIRVgVVCFPTGPF 323

                        330       340
                 ....*....|....*....|
gi 432857606 515 IRVSNAEKNT--EVcDIMMS 532
Cdd:PRK05937 324 LRVNLHAFNTedEV-DILVS 342
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 272-435 8.33e-12

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 63.94  E-value: 8.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 272 FHVELEQELADL--HKKDAALLFTSCFVANDSTLFTLAKmlPGCEIYSDGGNHASMIQGIRNSGAKKFVF--------RH 341
Cdd:cd01494    1 KLEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALLG--PGDEVIVDANGHGSRYWVAAELAGAKPVPvpvddagyGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 342 NDVAHLRELLQKGdpsKPKIVAFETVHSMDGAVCPLEEMCDLAHEFGAITFVDEVHAVGLYGARGGGIGDrdgimHKMDI 421
Cdd:cd01494   79 LDVAILEELKAKP---NVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPE-----GGADV 150

                        170
                 ....*....|....
gi 432857606 422 ISGTLGKAFGCVGG 435
Cdd:cd01494  151 VTFSLHKNLGGEGG 164
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
343-400 4.36e-07

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 52.45  E-value: 4.36e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 432857606 343 DVAHLRELLQKgdpsKPKIVAFETVHSMDGAVCPLEEMCDLAHEFGAITFVDEVHAVG 400
Cdd:COG0520  143 DLEALEALLTP----RTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVP 196
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 273-394 5.10e-07

CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.


Pssm-ID: 99738 [Multi-domain]  Cd Length: 369  Bit Score: 52.20  E-value: 5.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 273 HVELEQELADLHKKDAALLFTSCFVANDSTLFTLAK----MLPGCEIYsdGGNHASMIQGIRNSGAK-KFVfrhnDVAHL 347
Cdd:cd00614   42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKagdhVVASDDLY--GGTYRLFERLLPKLGIEvTFV----DPDDP 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 432857606 348 RELLQKGDPsKPKIVAFETVHSMDGAVCPLEEMCDLAHEFGAITFVD 394
Cdd:cd00614  116 EALEAAIKP-ETKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVD 161
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 372-575 2.42e-05

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 46.95  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 372 GAVCPLEEM---CDLAHEFGAITFVDEVHAvGLYGARGGGIGDRDGIMHKMDIISGTLGKAFGCVG---GYIASTSALVd 445
Cdd:cd00609  146 GAVLSEEELeelAELAKKHGILIISDEAYA-ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYLIAPPEEL- 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606 446 tVRSYAAGFIFTTSLPPMLLAGArqSIQILKGEEG--RTLRRKHQRNVKLLRQMLMDSGLPVVHCPS---HIIpIRVSnA 520
Cdd:cd00609  224 -LERLKKLLPYTTSGPSTLSQAA--AAAALDDGEEhlEELRERYRRRRDALLEALKELGPLVVVKPSggfFLW-LDLP-E 298

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 432857606 521 EKNTEVCDIMMSRHNIYVQainyPTVARGEEL---LRIAPTphHTPEMMKYFVERLVQ 575
Cdd:cd00609  299 GDDEEFLERLLLEAGVVVR----PGSAFGEGGegfVRLSFA--TPEEELEEALERLAE 350
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 234-400 2.69e-05

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 46.86  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  234 NDYLGMSRHPQVVqsiMDTLQK---HGSGAGGtrniSGTSKFHVELEQELADLHKKDAALL---------FTSCfvandS 301
Cdd:pfam00266   3 LDSAATTQKPQEV---LDAIQEyytDYNGNVH----RGVHTLGKEATQAYEEAREKVAEFInapsndeiiFTSG-----T 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 432857606  302 T--LFTLAKML-----PGCEI-YSDGGNHASMI--QGIRN-SGAKKFVFRHNDVAHLR--ELLQKGDPsKPKIVAFETVH 368
Cdd:pfam00266  71 TeaINLVALSLgrslkPGDEIvITEMEHHANLVpwQELAKrTGARVRVLPLDEDGLLDldELEKLITP-KTKLVAITHVS 149

                         170       180       190
                  ....*....|....*....|....*....|..
gi 432857606  369 SMDGAVCPLEEMCDLAHEFGAITFVDEVHAVG 400
Cdd:pfam00266 150 NVTGTIQPVPEIGKLAHQYGALVLVDAAQAIG 181
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 343-400 3.79e-04

Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 43.22  E-value: 3.79e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 432857606 343 DVAHLRELLQKgdpsKPKIVAFETVHSMDGAVCPLEEMCDLAHEFGAITFVDEVHAVG 400
Cdd:cd06453  128 DLEALEKLLTE----RTKLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGAQSAG 181
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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