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Conserved domains on  [gi|268569720|ref|XP_002648321|]
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Hypothetical protein CBG24506 [Caenorhabditis briggsae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AcnA_Mitochon_Swivel cd01578
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ...
 43-191 4.15e-112

Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.


:

Pssm-ID: 238810 [Multi-domain]  Cd Length: 149  Bit Score: 317.87  E-value: 4.15e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  43 KVKGKCTTDHISAAGPWLKYRGHLDNISNNLFLTAVNAENGEMNKVKNQVTGEYGAVPATARKYKADGVRWVAVGDENYG 122
Cdd:cd01578    1 KAKGKCTTDHISAAGPWLKYRGHLDNISNNLLIGAINAENGKANSVKNQVTGEYGPVPDTARDYKAHGIKWVVIGDENYG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 268569720 123 EGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTFANPADYDKIDPSDEVSIVGLNSFAPG 191
Cdd:cd01578   81 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKIHPDDKVDILGLTDFAPG 149
 
Name Accession Description Interval E-value
AcnA_Mitochon_Swivel cd01578
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ...
 43-191 4.15e-112

Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.


Pssm-ID: 238810 [Multi-domain]  Cd Length: 149  Bit Score: 317.87  E-value: 4.15e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  43 KVKGKCTTDHISAAGPWLKYRGHLDNISNNLFLTAVNAENGEMNKVKNQVTGEYGAVPATARKYKADGVRWVAVGDENYG 122
Cdd:cd01578    1 KAKGKCTTDHISAAGPWLKYRGHLDNISNNLLIGAINAENGKANSVKNQVTGEYGPVPDTARDYKAHGIKWVVIGDENYG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 268569720 123 EGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTFANPADYDKIDPSDEVSIVGLNSFAPG 191
Cdd:cd01578   81 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKIHPDDKVDILGLTDFAPG 149
PRK07229 PRK07229
aconitate hydratase; Validated
 20-233 1.39e-91

aconitate hydratase; Validated


Pssm-ID: 235974 [Multi-domain]  Cd Length: 646  Bit Score: 282.04  E-value: 1.39e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  20 RLHLLQPFyecyrKDLTDMKILIKVKGKCTTDHISAAGP-WLKYRGHLDNISNNLFLTAVNAENGemnKVKNQvtgeyga 98
Cdd:PRK07229 458 PLPLLEPL-----PDLLEGKVLLKVGDNITTDHIMPAGAkWLPYRSNIPNISEFVFEGVDNTFPE---RAKEQ------- 522

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  99 vpatarkykaDGvrWVAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTFANPADYDKIDPSD 178
Cdd:PRK07229 523 ----------GG--GIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFADPADYDKIEEGD 590

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 268569720 179 EVSIVGLNSFAPGKPLTGVFKKQNgskVEVTLNHTFNEQQIEWFKAGSALNRMKE 233
Cdd:PRK07229 591 VLEIEDLREFLPGGPLTVVNVTKD---EEIEVRHTLSERQIEILLAGGALNLIKK 642
AcnA COG1048
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ...
 33-238 1.27e-82

Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle


Pssm-ID: 440669 [Multi-domain]  Cd Length: 891  Bit Score: 263.89  E-value: 1.27e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  33 KDLTDMKILIKVKGKCTTDHISAAGP-----------------------WLKYRGHLDNISNNLFLTAV--N--AENGEM 85
Cdd:COG1048  655 KDIKGARVLAKLGDSITTDHISPAGAikadspagryllehgvepkdfnsYGSRRGNHEVMMRGTFANIRikNllAPGTEG 734

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  86 NKVKNQVTGEYGAVPATARKYKADGVRWVAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTF 165
Cdd:COG1048  735 GYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQF 814

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268569720 166 ANPADYDK--IDPSDEVSIVGLNS-FAPGKPLTGVFKKQNGSKVEVTLNHTF-NEQQIEWFKAGSALNRMKEVFAKS 238
Cdd:COG1048  815 PEGESAESlgLTGDETFDIEGLDEgLAPGKTVTVTATRADGSTEEFPVLHRIdTPVEVEYYRAGGILQYVLRQLLAA 891
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 38-168 6.84e-60

Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.


Pssm-ID: 459908 [Multi-domain]  Cd Length: 131  Bit Score: 184.88  E-value: 6.84e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720   38 MKILIKVKGKCTTDHISAAGPWLKYRGHLDNISNNLFLTAVNAENGEMNKVKNQVTGEYGAVPATARKYKADGVRWVAVG 117
Cdd:pfam00694   1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 268569720  118 DENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTFANP 168
Cdd:pfam00694  81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
acon_putative TIGR01342
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins ...
 39-233 6.02e-29

aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins homologous (and likely functionally equivalent to) aconitase 1. Members are found, so far in the anaerobe Clostridium acetobutylicum, in the microaerophilic, early-branching bacterium Aquifex aeolicus, and in the halophilic archaeon Halobacterium sp. NRC-1. No member is experimentally characterized. [Energy metabolism, TCA cycle]


Pssm-ID: 130409 [Multi-domain]  Cd Length: 658  Bit Score: 114.31  E-value: 6.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720   39 KILIKVKGKCTTDHISAAGP-WLKYRGHLDNISNnLFLTAVNAENGEmnkvknqvtgeygavpaTARKYKADGVRWVAVG 117
Cdd:TIGR01342 474 ETALIMEDNITTDHIIPAGAdILKFRSNIEAISE-FTLHRIDDEFAE-----------------RAKAADEKGKAGIIIA 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  118 DENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTFANPADYDKIDPSDEVSIVG--LNSFAPGKPLT 195
Cdd:TIGR01342 536 GENYGQGSSREHAALAPMFLGVEAVIAKSFARIHHANLFNFGILPLEFDNEEDYAKFELGDDIEIPDdlAAALADGEDEF 615

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 268569720  196 gVFKKQNGSKVEVTLNHTfnEQQIEWFKAGSALNRMKE 233
Cdd:TIGR01342 616 -TINKNDDEEALATLDAS--EREKEILAAGGKLNLIKN 650
 
Name Accession Description Interval E-value
AcnA_Mitochon_Swivel cd01578
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ...
 43-191 4.15e-112

Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.


Pssm-ID: 238810 [Multi-domain]  Cd Length: 149  Bit Score: 317.87  E-value: 4.15e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  43 KVKGKCTTDHISAAGPWLKYRGHLDNISNNLFLTAVNAENGEMNKVKNQVTGEYGAVPATARKYKADGVRWVAVGDENYG 122
Cdd:cd01578    1 KAKGKCTTDHISAAGPWLKYRGHLDNISNNLLIGAINAENGKANSVKNQVTGEYGPVPDTARDYKAHGIKWVVIGDENYG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 268569720 123 EGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTFANPADYDKIDPSDEVSIVGLNSFAPG 191
Cdd:cd01578   81 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKIHPDDKVDILGLTDFAPG 149
PRK07229 PRK07229
aconitate hydratase; Validated
 20-233 1.39e-91

aconitate hydratase; Validated


Pssm-ID: 235974 [Multi-domain]  Cd Length: 646  Bit Score: 282.04  E-value: 1.39e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  20 RLHLLQPFyecyrKDLTDMKILIKVKGKCTTDHISAAGP-WLKYRGHLDNISNNLFLTAVNAENGemnKVKNQvtgeyga 98
Cdd:PRK07229 458 PLPLLEPL-----PDLLEGKVLLKVGDNITTDHIMPAGAkWLPYRSNIPNISEFVFEGVDNTFPE---RAKEQ------- 522

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  99 vpatarkykaDGvrWVAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTFANPADYDKIDPSD 178
Cdd:PRK07229 523 ----------GG--GIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFADPADYDKIEEGD 590

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 268569720 179 EVSIVGLNSFAPGKPLTGVFKKQNgskVEVTLNHTFNEQQIEWFKAGSALNRMKE 233
Cdd:PRK07229 591 VLEIEDLREFLPGGPLTVVNVTKD---EEIEVRHTLSERQIEILLAGGALNLIKK 642
AcnA COG1048
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ...
 33-238 1.27e-82

Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle


Pssm-ID: 440669 [Multi-domain]  Cd Length: 891  Bit Score: 263.89  E-value: 1.27e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  33 KDLTDMKILIKVKGKCTTDHISAAGP-----------------------WLKYRGHLDNISNNLFLTAV--N--AENGEM 85
Cdd:COG1048  655 KDIKGARVLAKLGDSITTDHISPAGAikadspagryllehgvepkdfnsYGSRRGNHEVMMRGTFANIRikNllAPGTEG 734

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  86 NKVKNQVTGEYGAVPATARKYKADGVRWVAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTF 165
Cdd:COG1048  735 GYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQF 814

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268569720 166 ANPADYDK--IDPSDEVSIVGLNS-FAPGKPLTGVFKKQNGSKVEVTLNHTF-NEQQIEWFKAGSALNRMKEVFAKS 238
Cdd:COG1048  815 PEGESAESlgLTGDETFDIEGLDEgLAPGKTVTVTATRADGSTEEFPVLHRIdTPVEVEYYRAGGILQYVLRQLLAA 891
Aconitase_C pfam00694
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ...
 38-168 6.84e-60

Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.


Pssm-ID: 459908 [Multi-domain]  Cd Length: 131  Bit Score: 184.88  E-value: 6.84e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720   38 MKILIKVKGKCTTDHISAAGPWLKYRGHLDNISNNLFLTAVNAENGEMNKVKNQVTGEYGAVPATARKYKADGVRWVAVG 117
Cdd:pfam00694   1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 268569720  118 DENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTFANP 168
Cdd:pfam00694  81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
AcnA_Bact_Swivel cd01579
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ...
 43-184 5.69e-35

Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism. This distinct subfamily is found only in bacteria and archea. Its exact characteristics are not known.


Pssm-ID: 238811 [Multi-domain]  Cd Length: 121  Bit Score: 121.01  E-value: 5.69e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  43 KVKGKCTTDHISAAGP-WLKYRGHLDNISNNLFltavnaengemnkvknqvtgeYGAVPATARKYKADGVRWVaVGDENY 121
Cdd:cd01579    1 KVGDNITTDHIMPAGAkVLPLRSNIPAISEFVF---------------------HRVDPTFAERAKAAGPGFI-VGGENY 58

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 268569720 122 GEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTFANPADYDKIDPSDEVSIVG 184
Cdd:cd01579   59 GQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFEQGDQLELPL 121
Aconitase_swivel cd00404
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ...
 43-184 4.91e-29

Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. The aconitase family contains the following proteins: - Iron-responsive element binding protein (IRE-BP). IRE-BP is a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.


Pssm-ID: 238236 [Multi-domain]  Cd Length: 88  Bit Score: 104.86  E-value: 4.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  43 KVKGKCTTDHISAAGPWlkyrghldnisnnlfltavnaengemnkvknqvtgeygavpatarkykadgvrwVAVGDENYG 122
Cdd:cd00404    1 KVAGNITTDHISPAGPG------------------------------------------------------VVIGDENYG 26

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 268569720 123 EGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTFANPADYDKIDPSDEVSIVG 184
Cdd:cd00404   27 TGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKLHTGDELDIYP 88
acon_putative TIGR01342
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins ...
 39-233 6.02e-29

aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins homologous (and likely functionally equivalent to) aconitase 1. Members are found, so far in the anaerobe Clostridium acetobutylicum, in the microaerophilic, early-branching bacterium Aquifex aeolicus, and in the halophilic archaeon Halobacterium sp. NRC-1. No member is experimentally characterized. [Energy metabolism, TCA cycle]


Pssm-ID: 130409 [Multi-domain]  Cd Length: 658  Bit Score: 114.31  E-value: 6.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720   39 KILIKVKGKCTTDHISAAGP-WLKYRGHLDNISNnLFLTAVNAENGEmnkvknqvtgeygavpaTARKYKADGVRWVAVG 117
Cdd:TIGR01342 474 ETALIMEDNITTDHIIPAGAdILKFRSNIEAISE-FTLHRIDDEFAE-----------------RAKAADEKGKAGIIIA 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  118 DENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTFANPADYDKIDPSDEVSIVG--LNSFAPGKPLT 195
Cdd:TIGR01342 536 GENYGQGSSREHAALAPMFLGVEAVIAKSFARIHHANLFNFGILPLEFDNEEDYAKFELGDDIEIPDdlAAALADGEDEF 615

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 268569720  196 gVFKKQNGSKVEVTLNHTfnEQQIEWFKAGSALNRMKE 233
Cdd:TIGR01342 616 -TINKNDDEEALATLDAS--EREKEILAAGGKLNLIKN 650
PRK09277 PRK09277
aconitate hydratase AcnA;
33-210 1.85e-27

aconitate hydratase AcnA;


Pssm-ID: 236445 [Multi-domain]  Cd Length: 888  Bit Score: 110.21  E-value: 1.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  33 KDLTDMKILIKVKGKCTTDHIS---------AAGPWLK-----------Y-----------RGHLDNIsnnlfltavnae 81
Cdd:PRK09277 653 RDIKGARVLALLGDSITTDHISpagaikadsPAGKYLLehgvepkdfnsYgsrrgnhevmmRGTFANI------------ 720

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  82 ngemnKVKNQV-------------TGEYGAVPATARKYKADGVRWVAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFA 148
Cdd:PRK09277 721 -----RIRNEMvpgveggytrhfpEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFE 795

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 268569720 149 RIHETNLKKQGMLPLTFANPADYD--KIDPSDEVSIVGLNSFAPGKPLTGVFKKQNGSKVEVTL 210
Cdd:PRK09277 796 RIHRSNLVGMGVLPLQFKPGESRKtlGLDGTETFDIEGLEDLKPGATVTVVITRADGEVVEFPV 859
acnA PRK12881
aconitate hydratase AcnA;
26-231 1.82e-23

aconitate hydratase AcnA;


Pssm-ID: 237246 [Multi-domain]  Cd Length: 889  Bit Score: 98.47  E-value: 1.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  26 PFYEC------YRKDLTDMKILIKVKGKCTTDHIS---------AAGPWLKYRG---------------HL--------- 66
Cdd:PRK12881 641 PFFDFsmgpaaSIATVKGARPLAVLGDSITTDHISpagaikadsPAGKYLKENGvpkadfnsygsrrgnHEvmmrgtfan 720

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  67 DNISNnlfLTAVNAENGEmnkVKNQVTGEYGAVPATARKYKADGVRWVAVGDENYGEGSSREHAALEPRHLGGRAIIVKS 146
Cdd:PRK12881 721 VRIKN---LMIPGKEGGL---TLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKAVIAES 794

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720 147 FARIHETNLKKQGMLPLTFA---NPADYdKIDPSDEVSIVGL-NSFAPGKPLTGVFKKQNGS--KVEVTLN-HTFNEqqI 219
Cdd:PRK12881 795 FERIHRSNLVGMGVLPLQFKggdSRQSL-GLTGGETFDIEGLpGEIKPRQDVTLVIHRADGSteRVPVLCRiDTPIE--V 871

                        250
                 ....*....|..
gi 268569720 220 EWFKAGSALNRM 231
Cdd:PRK12881 872 DYYKAGGILPYV 883
AcnA_IRP_Swivel cd01580
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ...
 49-184 7.00e-21

Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.


Pssm-ID: 238812 [Multi-domain]  Cd Length: 171  Bit Score: 85.79  E-value: 7.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  49 TTDHISAAG------PWLKY-------------------------RGHLDNISN-NLFltavnAENGEMNKVKNQVTGEY 96
Cdd:cd01580    7 TTDHISPAGsiakdsPAGKYlaergvkprdfnsygsrrgndevmmRGTFANIRLrNKL-----VPGTEGGTTHHPPTGEV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  97 GAVPATARKYKADGVRWVAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTFANP--ADYDKI 174
Cdd:cd01580   82 MSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGenADSLGL 161

                        170
                 ....*....|
gi 268569720 175 DPSDEVSIVG 184
Cdd:cd01580  162 TGEETYDIIG 171
PTZ00092 PTZ00092
aconitate hydratase-like protein; Provisional
 33-229 3.11e-18

aconitate hydratase-like protein; Provisional


Pssm-ID: 240263 [Multi-domain]  Cd Length: 898  Bit Score: 83.14  E-value: 3.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  33 KDLTDMKILIKVKGKCTTDHISAAGpwlkyrghldNISNN----LFLTAVNAE------------NGEM----------- 85
Cdd:PTZ00092 667 KSIENAYCLLNLGDSITTDHISPAG----------NIAKNspaaKYLMERGVErkdfntygarrgNDEVmvrgtfanirl 736

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  86 -NKVKNQV--------TGEYGAVPATARKYKADGVRWVAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLK 156
Cdd:PTZ00092 737 iNKLCGKVgpntvhvpTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSNLV 816

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268569720 157 KQGMLPLTFAN--PADYDKIDPSDEVSIvGLNS--FAPGKPLTgvFKKQNGSKVEVTLNHTfNEQQIEWFKAGSALN 229
Cdd:PTZ00092 817 GMGILPLQFLNgeNADSLGLTGKEQFSI-DLNSgeLKPGQDVT--VKTDTGKTFDTILRID-TEVEVEYFKHGGILQ 889
PLN00070 PLN00070
aconitate hydratase
 49-172 1.02e-15

aconitate hydratase


Pssm-ID: 215047 [Multi-domain]  Cd Length: 936  Bit Score: 76.00  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  49 TTDHISAAG------PWLKY-------------------------RGHLDNIS-NNLFLtavnaeNGEMN-KVKNQVTGE 95
Cdd:PLN00070 718 TTDHISPAGsihkdsPAAKYlmergvdrkdfnsygsrrgndeimaRGTFANIRiVNKLL------KGEVGpKTVHIPTGE 791

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268569720  96 YGAVPATARKYKADGVRWVAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTFANPADYD 172
Cdd:PLN00070 792 KLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDAD 868
IPMI_Swivel cd01577
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ...
 116-182 3.16e-14

Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.


Pssm-ID: 238809 [Multi-domain]  Cd Length: 91  Bit Score: 66.07  E-value: 3.16e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268569720 116 VGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTFANPADYD-KIDPSDEVSI 182
Cdd:cd01577   22 VAGKNFGCGSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEvEAKPGDEVEV 89
LeuD COG0066
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ...
 116-182 2.37e-12

3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439836 [Multi-domain]  Cd Length: 195  Bit Score: 63.65  E-value: 2.37e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 268569720 116 VGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTfANPADYDKI------DPSDEVSI 182
Cdd:COG0066   69 VAGRNFGCGSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIE-LPEEAVDALfaaieaNPGDELTV 140
leuD PRK00439
3-isopropylmalate dehydratase small subunit; Reviewed
 116-182 5.03e-12

3-isopropylmalate dehydratase small subunit; Reviewed


Pssm-ID: 234762 [Multi-domain]  Cd Length: 163  Bit Score: 62.15  E-value: 5.03e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268569720 116 VGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGmLPLtFANPADYDKIDPSDEVSI 182
Cdd:PRK00439  53 VAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIG-LPV-LECDEAVDKIEDGDEVEV 117
LEUD_arch TIGR02087
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ...
 97-196 6.11e-12

3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the 3-isopropylmalate dehydratase, small subunits which form TIGR00171. This subfamily includes the members of TIGR02084 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.


Pssm-ID: 273961 [Multi-domain]  Cd Length: 154  Bit Score: 61.67  E-value: 6.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720   97 GAVPATARKYKAdGVrwVAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGmLPLTFA-----NPADY 171
Cdd:TIGR02087  36 GIDPEFAKKVRP-GD--VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIG-LPLIEAktegiKDGDE 111

                          90       100
                  ....*....|....*....|....*
gi 268569720  172 DKIDPSDEVSIVGLNSFAPGKPLTG 196
Cdd:TIGR02087 112 VTVDLETGEIRVNGNEEYKGEPLPD 136
PRK14023 PRK14023
homoaconitate hydratase small subunit; Provisional
 116-182 3.30e-10

homoaconitate hydratase small subunit; Provisional


Pssm-ID: 184460 [Multi-domain]  Cd Length: 166  Bit Score: 57.12  E-value: 3.30e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268569720 116 VGDENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPltFANPADYDKIDPSDEVSI 182
Cdd:PRK14023  54 VAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPP--FESEEVVDALEDGDEVEL 118
leuD PRK01641
3-isopropylmalate dehydratase small subunit;
116-182 2.43e-08

3-isopropylmalate dehydratase small subunit;


Pssm-ID: 179314 [Multi-domain]  Cd Length: 200  Bit Score: 52.44  E-value: 2.43e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 268569720 116 VGDENYGEGSSREHA--ALEprHLGGRAIIVKSFARIHETNLKKQGMLPLTfANPADYDKI------DPSDEVSI 182
Cdd:PRK01641  72 LAGDNFGCGSSREHApwALA--DYGFRAVIAPSFADIFYNNCFKNGLLPIV-LPEEDVDELfklveaNPGAELTV 143
leuD TIGR00171
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ...
 119-163 2.78e-05

3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The candidate archaeal leuD proteins are not included in the seed alignment for this model and score below the trusted cutoff. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 129275 [Multi-domain]  Cd Length: 188  Bit Score: 43.65  E-value: 2.78e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 268569720  119 ENYGEGSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPL 163
Cdd:TIGR00171  77 ENFGCGSSREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPI 121
PLN00072 PLN00072
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
 114-150 5.41e-05

3-isopropylmalate isomerase/dehydratase small subunit; Provisional


Pssm-ID: 177701 [Multi-domain]  Cd Length: 246  Bit Score: 43.31  E-value: 5.41e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 268569720 114 VAVGDENYGEGSSREHAALEPRHLGGRAIIVKSFARI 150
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARI 168
PRK11413 PRK11413
putative hydratase; Provisional
 78-229 6.67e-05

putative hydratase; Provisional


Pssm-ID: 183125 [Multi-domain]  Cd Length: 751  Bit Score: 43.46  E-value: 6.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720  78 VNAENGEMNKVKNQVTGEYGAVPATARKykadgvrwVAVGDENY----GEGSSREHAALEPRHLGGRAIIVKSFA-RIHE 152
Cdd:PRK11413 598 LAGNVSELTEVFARIKQIAGQEHIDPLQ--------TEIGSMVYavkpGDGSAREQAASCQRVLGGLANIAEEYAtKRYR 669

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268569720 153 TNLKKQGMLPLTFANPADYDKidpSDEVSIVGLNSFAPGKP--LTGVFKKQNGSKVEVTL---NHTFNEQQIewFKAGSA 227
Cdd:PRK11413 670 SNVINWGMLPFQMAEEPTFEV---GDYIYIPGIRAALDNPGttFKGYVIHEDAPVTEITLymeSLTAEEREI--IKAGCL 744


                 ..
gi 268569720 228 LN 229
Cdd:PRK11413 745 IN 746
PRK14812 PRK14812
hypothetical protein; Provisional
 124-182 8.96e-04

hypothetical protein; Provisional


Pssm-ID: 173273 [Multi-domain]  Cd Length: 119  Bit Score: 38.16  E-value: 8.96e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 268569720 124 GSSREHAALEPRHLGGRAIIVKSFARIHETNLKKQGMLPLTfaNPAD----YDKIDPSDEVSI 182
Cdd:PRK14812   3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIV--QPREvrekLAQLKPTDQVTV 63
 
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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