2OQ2


Conserved Protein Domain Family
cysH

?
TIGR00434: cysH 
Click on image for an interactive view with Cn3D
phosophoadenylyl-sulfate reductase (thioredoxin)
This enzyme, involved in the assimilation of inorganic sulfate, is designated cysH in Bacteria and MET16 in Saccharomyces cerevisiae. Synonyms include phosphoadenosine phosphosulfate reductase, PAPS reductase, and PAPS reductase, thioredoxin-dependent. In a reaction requiring reduced thioredoxin and NADPH, it converts 3(prime)-phosphoadenylylsulfate (PAPS) to sulfite and adenosine 3(prime),5(prime) diphosphate (PAP). A related family of plant enzymes, scoring below the trusted cutoff, differs in having a thioredoxin-like C-terminal domain, not requiring thioredoxin, and in having a preference for 5(prime)-adenylylsulfate (APS) over PAPS. [Central intermediary metabolism, Sulfur metabolism]
Statistics
?
PSSM-Id: 129526
View PSSM: TIGR00434
Aligned: 6 rows
Threshold Bit Score: 337.53
Threshold Setting Gi: 165760900
Created: 7-Oct-2014
Updated: 23-Jan-2015
Structure
?
Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OQ2_A        30 PQEIIAWSIVTFP-HLFQTTAFGLTGLVTIDMLSKLSEKYYMPellFID---TLHHFPQTLTLKNEIEKKYYqpknQTIH 105
gi 2498275    22 AQQIITWAAQTFGpGLVMSTSFGIQAAVMLHLVTSIVPNIPVI---WID---TGYLPLETYQFADQLTGRLQ----LNLK 91
gi 7404350    23 ALSVLKWAYGHYGdQLVYACSFGIEGIVLIDLIYKVKKDAEIV---FLD---TGLHFKETYETIERVKERYPg---LNII 93
gi 505916151  25 eLDVLKWAYRTYGeKIVYACSFGAEGMVLLDLISKINKNAHII---FLD---TGLHFQETYELIETVKERYPg---FAIQ 95
gi 485681726  84 AEGRVAWALDNLPgEYVLSSSFGIQAAVSLHLVNQIRPDIPVI---LTD---TGYLFPETYRFIDELTDKLK----LNLK 153
gi 2507069    30 PQEIIAWSIVTFP-HLFQTTAFGLTGLVTIDMLSKLSEKYYMP---ELLfidTLHHFPQTLTLKNEIEKKYYqpknQTIH 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OQ2_A       106 VYKPDgcESEADFASKYGdFLWEK----DDDKYDYLAKVEPAHRAYKELHISAVFTGRRKSQGSARSQLSIIEIDElnGI 181
gi 2498275    92 VYQSP--LSPARMEALYG-KLWQQkdveSLNRYDQIRKVEPMQRALKELEAIAWLTGLRRDQTRHRQNLKPVDLQG--NQ 166
gi 7404350    94 LKKPD--LTLEEQAEEHGdKLWERe----PNQCCYLRKVVPLREALSGHP--AWLSGLRRDQGPSRANTNFLNKDEkfKS 165
gi 505916151  96 MLEPE--LSLTEQGTKYGgELWKH----NPNLCCQLRKIEPLKKHLSGMT--AWISGLRRDQSPTRKHIQYVNLDQkfEL 167
gi 485681726 154 VYRAT--ESAAWQEARYG-KLWEQgv-eGIEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAIQR--GV 227
gi 2507069   106 VYKPDgcESEADFASKYGdFLWEK----DDDKYDYLAKVEPAHRAYKELHISAVFTGRRKSQGSARSQLSIIEIDElnGI 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2OQ2_A       182 LKINPLINWTFEQVKQYIDANNVPYNELLDLGYRSIGDYHSTQPVKEG-EDERAGRWKGkAKTECGIHE 249
gi 2498275   167 YKVLPILDWNSKMVYEYLTAHDLPYHPFFDQGYVSVGDWHSSRPLMAHdEDERDTRFHG-LKQECGLHL 234
gi 7404350   166 VKVCPLIHWTWKDIWRYTSRNELDYNPLHDQGYPSIGCAPCTSPAFTA-EDLRSGRWNGmAKTECGLHE 233
gi 505916151 168 IKICPLIHWTWDDVWTYIRLHNLPYNKLHDQHYPSIGCEMCTLPSPDP-NDERAGRWAGrEKTECGLHQ 235
gi 485681726 228 FKVLPIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDTHTTRKWEPG-MAEEETRFFG-LKRECGLHE 294
gi 2507069   182 LKINPLINWTFEQVKQYIDANNVPYNELLDLGYRSIGDYHSTQPVKEG-EDERAGRWKGkAKTECGIHE 249
| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap