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Conserved domains on  [gi|1721624170|gb|QEC28863|]
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IscS subfamily cysteine desulfurase [Mannheimia haemolytica]

Protein Classification

IscS subfamily cysteine desulfurase( domain architecture ID 10014534)

IscS subfamily cysteine desulfurase is a pyridoxal-5'-phoshate dependent enzyme that catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine

EC:  2.8.1.7
PubMed:  12860127
SCOP:  4000672

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK14012 PRK14012
IscS subfamily cysteine desulfurase;
1-406 0e+00

IscS subfamily cysteine desulfurase;


:

Pssm-ID: 184450 [Multi-domain]  Cd Length: 404  Bit Score: 883.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   1 MKLPIYLDYAATTPMDERVAKKMMEYMTKDGIFGNPASRSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDN 80
Cdd:PRK14012    1 MKLPIYLDYSATTPVDPRVAEKMMPYLTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  81 LAIKGAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVI 160
Cdd:PRK14012   81 LAIKGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 161 QPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKPRVRLEAIIHGGGHERGMR 240
Cdd:PRK14012  161 QDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 241 SGTLPVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKDIEEVYVNGSMEegKRIGSNLNISFNFVEGESLMMSLR 320
Cdd:PRK14012  241 SGTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDLE--QRVPGNLNVSFNYVEGESLIMALK 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 321 DIAVSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEIDHTIEIVKKAIVKLRELSPLWEMFKEGVDLSK 400
Cdd:PRK14012  319 DLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNS 398

                  ....*.
gi 1721624170 401 IEWNHH 406
Cdd:PRK14012  399 IEWAHH 404
 
Name Accession Description Interval E-value
PRK14012 PRK14012
IscS subfamily cysteine desulfurase;
1-406 0e+00

IscS subfamily cysteine desulfurase;


Pssm-ID: 184450 [Multi-domain]  Cd Length: 404  Bit Score: 883.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   1 MKLPIYLDYAATTPMDERVAKKMMEYMTKDGIFGNPASRSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDN 80
Cdd:PRK14012    1 MKLPIYLDYSATTPVDPRVAEKMMPYLTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  81 LAIKGAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVI 160
Cdd:PRK14012   81 LAIKGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 161 QPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKPRVRLEAIIHGGGHERGMR 240
Cdd:PRK14012  161 QDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 241 SGTLPVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKDIEEVYVNGSMEegKRIGSNLNISFNFVEGESLMMSLR 320
Cdd:PRK14012  241 SGTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDLE--QRVPGNLNVSFNYVEGESLIMALK 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 321 DIAVSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEIDHTIEIVKKAIVKLRELSPLWEMFKEGVDLSK 400
Cdd:PRK14012  319 DLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNS 398

                  ....*.
gi 1721624170 401 IEWNHH 406
Cdd:PRK14012  399 IEWAHH 404
IscS TIGR02006
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ...
1-406 0e+00

cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases from a larger protein family designated (misleadingly, in this case) class V aminotransferases. IscS is one of at least 6 enzymes characteristic of the IscSUA-hscAB-fsx system of iron-sulfur cluster assembly. Scoring almost as well as proteobacterial sequences included in the model are mitochondrial cysteine desulfurases, apparently from an analogous system in eukaryotes. The sulfur, taken from cysteine, may be used in other systems as well, such as tRNA base modification and biosynthesis of other cofactors. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 131061 [Multi-domain]  Cd Length: 402  Bit Score: 771.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   1 MKLPIYLDYAATTPMDERVAKKMMEYMTKDgiFGNPASRSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDN 80
Cdd:TIGR02006   1 MKLPIYLDYAATTPVDPRVAEKMMPYLTEK--FGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  81 LAIKGAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVI 160
Cdd:TIGR02006  79 LAIKGIAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 161 QPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKPRVRLEAIIHGGGHERGMR 240
Cdd:TIGR02006 159 QDIAAIGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 241 SGTLPVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKDIEEVYVNGSMEEgkRIGSNLNISFNFVEGESLMMSLR 320
Cdd:TIGR02006 239 SGTLPTHQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKSIEEVYLNGDLEH--RVPGNLNVSFNYVEGESLIMALK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 321 DIAVSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEIDHTIEIVKKAIVKLRELSPLWEMFKEGVDLSK 400
Cdd:TIGR02006 317 DLAVSSGSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNS 396

                  ....*.
gi 1721624170 401 IEWNHH 406
Cdd:TIGR02006 397 IEWAAH 402
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
2-386 0e+00

Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];


Pssm-ID: 440721 [Multi-domain]  Cd Length: 381  Bit Score: 655.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   2 KLPIYLDYAATTPMDERVAKKMMEYMTKDgiFGNPASrSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDNL 81
Cdd:COG1104     1 MMMIYLDNAATTPVDPEVLEAMLPYLTEY--FGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  82 AIKGAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQ 161
Cdd:COG1104    78 AIKGAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 162 PIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVcrKPRVRLEAIIHGGGHERGMRS 241
Cdd:COG1104   158 PIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYV--RKGVRLEPLIHGGGQERGLRS 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 242 GTLPVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKD-IEEVYVNGSMEEgkRIGSNLNISFNFVEGESLMMSL- 319
Cdd:COG1104   236 GTENVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAaIPGVVINGDPEN--RLPNTLNFSFPGVEGEALLLALd 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721624170 320 -RDIAVSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEIDHTIEIVKKAIVKLRELS 386
Cdd:COG1104   314 lAGIAVSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
5-369 8.33e-104

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: 311.49  E-value: 8.33e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   5 IYLDYAATTPMDERVAKKMMEYMTKdgIFGNPASRSHKFGWEAEEAVDVARNQIADLIGADSR-EIVFTSGATESDNLAI 83
Cdd:pfam00266   1 IYLDSAATTQKPQEVLDAIQEYYTD--YNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNdEIIFTSGTTEAINLVA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  84 KGAAHFYQtKGKHIITVKTEHKAVLDTCRQL-EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQP 162
Cdd:pfam00266  79 LSLGRSLK-PGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 163 IKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKPRVRLEAIIHGGG-------H 235
Cdd:pfam00266 158 VPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 236 ERGM-------RSGTLPVHQIVGMGEAYR-IAKEEMATEMARLTVLRDRLYNGFKDIEEVYVNGSmeegKRIGSNLNISF 307
Cdd:pfam00266 238 ESTFadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGP----ERRASIISFNF 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721624170 308 NFVEGESLMMSLRD--IAVSSGSACTsaslEPSYVLRAIgrddelaHSSIRFTLGRWTTEEEID 369
Cdd:pfam00266 314 KGVHPHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVD 366
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
5-373 1.07e-74

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: 236.98  E-value: 1.07e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   5 IYLDYAATTPMDERVAKKMMEYMTKDGifGNPASRSHKFGWEAEEAVDVARNQIADLIGA-DSREIVFTSGATESDNLAI 83
Cdd:cd06453     1 VYLDNAATSQKPQPVIDAIVDYYRHYN--ANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  84 KGAAhFYQTKGKHIITVKTEHKAVLDTCRQL-EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQP 162
Cdd:cd06453    79 YGLG-RANKPGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 163 IKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVcrKPRVrLEAI--IHGGG------ 234
Cdd:cd06453   158 VKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYG--KEEL-LEEMppYGGGGemieev 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 235 -------HERGMR--SGTLPVHQIVGMGEA--Y--RIAKEEMATEMARLTvlrDRLYNGFKDIEEVYVNGSMEegKRIGS 301
Cdd:cd06453   235 sfeettyADLPHKfeAGTPNIAGAIGLGAAidYleKIGMEAIAAHEHELT---AYALERLSEIPGVRVYGDAE--DRAGV 309
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721624170 302 nlnISFNfVEGE-----SLMMSLRDIAVSSGSACTsaslEPsyVLRAIGrddelAHSSIRFTLGRWTTEEEIDHTIE 373
Cdd:cd06453   310 ---VSFN-LEGIhphdvATILDQYGIAVRAGHHCA----QP--LMRRLG-----VPGTVRASFGLYNTEEEIDALVE 371
f2_encap_cargo1 NF041166
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ...
54-235 2.16e-20

family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide. Proteins of this family are cysteine desulfurases with an additional N-terminal encapsulation targeting sequence (~200 aa) that is necessary and sufficient for compartmentalization.


Pssm-ID: 469077 [Multi-domain]  Cd Length: 623  Bit Score: 93.38  E-value: 2.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  54 ARNQIADLIGADS-REIVFTSGATESDNLAIK--GAAHFYQtkGKHIITVKTEHKAVLDTCRQL-EREG--FEVTYLDpe 127
Cdd:NF041166  294 AREKVRRFIGAPSvDEIIFVRGTTEAINLVAKswGRQNIGA--GDEIIVSHLEHHANIVPWQQLaQETGakLRVIPVD-- 369
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 128 EDG--ILD-LAKLkaaIRPDTILVSVMHVNNEMGVIQPIKEIGAICRAK--KIIfhVDATQSVGKIEVNVQDLNVDLMSF 202
Cdd:NF041166  370 DSGqiLLDeYAKL---LNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAgaKVL--VDGAQSVSHMPVDVQALDADFFVF 444
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1721624170 203 SSHKLYGPKGIGGLYvcRKPRVrLEAI--IHGGGH 235
Cdd:NF041166  445 SGHKVFGPTGIGVVY--GKRDL-LEAMppWQGGGN 476
 
Name Accession Description Interval E-value
PRK14012 PRK14012
IscS subfamily cysteine desulfurase;
1-406 0e+00

IscS subfamily cysteine desulfurase;


Pssm-ID: 184450 [Multi-domain]  Cd Length: 404  Bit Score: 883.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   1 MKLPIYLDYAATTPMDERVAKKMMEYMTKDGIFGNPASRSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDN 80
Cdd:PRK14012    1 MKLPIYLDYSATTPVDPRVAEKMMPYLTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  81 LAIKGAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVI 160
Cdd:PRK14012   81 LAIKGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 161 QPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKPRVRLEAIIHGGGHERGMR 240
Cdd:PRK14012  161 QDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 241 SGTLPVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKDIEEVYVNGSMEegKRIGSNLNISFNFVEGESLMMSLR 320
Cdd:PRK14012  241 SGTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDLE--QRVPGNLNVSFNYVEGESLIMALK 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 321 DIAVSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEIDHTIEIVKKAIVKLRELSPLWEMFKEGVDLSK 400
Cdd:PRK14012  319 DLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNS 398

                  ....*.
gi 1721624170 401 IEWNHH 406
Cdd:PRK14012  399 IEWAHH 404
IscS TIGR02006
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ...
1-406 0e+00

cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases from a larger protein family designated (misleadingly, in this case) class V aminotransferases. IscS is one of at least 6 enzymes characteristic of the IscSUA-hscAB-fsx system of iron-sulfur cluster assembly. Scoring almost as well as proteobacterial sequences included in the model are mitochondrial cysteine desulfurases, apparently from an analogous system in eukaryotes. The sulfur, taken from cysteine, may be used in other systems as well, such as tRNA base modification and biosynthesis of other cofactors. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 131061 [Multi-domain]  Cd Length: 402  Bit Score: 771.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   1 MKLPIYLDYAATTPMDERVAKKMMEYMTKDgiFGNPASRSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDN 80
Cdd:TIGR02006   1 MKLPIYLDYAATTPVDPRVAEKMMPYLTEK--FGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  81 LAIKGAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVI 160
Cdd:TIGR02006  79 LAIKGIAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 161 QPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKPRVRLEAIIHGGGHERGMR 240
Cdd:TIGR02006 159 QDIAAIGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 241 SGTLPVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKDIEEVYVNGSMEEgkRIGSNLNISFNFVEGESLMMSLR 320
Cdd:TIGR02006 239 SGTLPTHQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKSIEEVYLNGDLEH--RVPGNLNVSFNYVEGESLIMALK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 321 DIAVSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEIDHTIEIVKKAIVKLRELSPLWEMFKEGVDLSK 400
Cdd:TIGR02006 317 DLAVSSGSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNS 396

                  ....*.
gi 1721624170 401 IEWNHH 406
Cdd:TIGR02006 397 IEWAAH 402
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
2-386 0e+00

Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];


Pssm-ID: 440721 [Multi-domain]  Cd Length: 381  Bit Score: 655.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   2 KLPIYLDYAATTPMDERVAKKMMEYMTKDgiFGNPASrSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDNL 81
Cdd:COG1104     1 MMMIYLDNAATTPVDPEVLEAMLPYLTEY--FGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  82 AIKGAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQ 161
Cdd:COG1104    78 AIKGAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 162 PIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVcrKPRVRLEAIIHGGGHERGMRS 241
Cdd:COG1104   158 PIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYV--RKGVRLEPLIHGGGQERGLRS 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 242 GTLPVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKD-IEEVYVNGSMEEgkRIGSNLNISFNFVEGESLMMSL- 319
Cdd:COG1104   236 GTENVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAaIPGVVINGDPEN--RLPNTLNFSFPGVEGEALLLALd 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721624170 320 -RDIAVSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEIDHTIEIVKKAIVKLRELS 386
Cdd:COG1104   314 lAGIAVSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
PLN02651 PLN02651
cysteine desulfurase
5-369 0e+00

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 568.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   5 IYLDYAATTPMDERVAKKMMEYMTKDgiFGNPASRSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDNLAIK 84
Cdd:PLN02651    1 LYLDMQATTPIDPRVLDAMLPFLIEH--FGNPHSRTHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  85 GAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQPIK 164
Cdd:PLN02651   79 GVMHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 165 EIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKPRVRLEAIIHGGGHERGMRSGTL 244
Cdd:PLN02651  159 EIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQERGRRSGTE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 245 PVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKD-IEEVYVNGSMEEGKRIGSNLNISFNFVEGESLMMSLRDIA 323
Cdd:PLN02651  239 NTPLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAkLGGVRVNGPRDPEKRYPGTLNLSFAYVEGESLLMGLKEVA 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1721624170 324 VSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEID 369
Cdd:PLN02651  319 VSSGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEVD 364
PRK02948 PRK02948
IscS subfamily cysteine desulfurase;
5-397 1.24e-110

IscS subfamily cysteine desulfurase;


Pssm-ID: 179511 [Multi-domain]  Cd Length: 381  Bit Score: 329.77  E-value: 1.24e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   5 IYLDYAATTPMDERVAKKMMEYMTKdgIFGNpASRSHKFGWEAEEAVDVARNQIADLIGADSREIVFTSGATESDNLAIK 84
Cdd:PRK02948    2 IYLDYAATTPMSKEALQTYQKAASQ--YFGN-ESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  85 GAAHFYQTKGKHIITVKTEHKAVLDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQPIK 164
Cdd:PRK02948   79 SLLNALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 165 EIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVcrKPRVRLEAIIHGGGHERGMRSGTL 244
Cdd:PRK02948  159 EIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYI--NPQVRWKPVFPGTTHEKGFRPGTV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 245 PVHQIVGMGEAYRIAKEEMATEMARLTVLRDRLYNGFKDIE-EVYVNGSMEEgkRIGSNLNISFNFVEGESLMMSL--RD 321
Cdd:PRK02948  237 NVPGIAAFLTAAENILKNMQEESLRFKELRSYFLEQIQTLPlPIEVEGHSTS--CLPHIIGVTIKGIEGQYTMLECnrRG 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721624170 322 IAVSSGSACTSASLEPSYVLRAIGRDDELAHSSIRFTLGRWTTEEEIDHTIEIvkkaivklreLSPLWEMFKEGVD 397
Cdd:PRK02948  315 IAISTGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTTIHA----------LETIGNQFYRGVK 380
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
5-369 8.33e-104

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: 311.49  E-value: 8.33e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   5 IYLDYAATTPMDERVAKKMMEYMTKdgIFGNPASRSHKFGWEAEEAVDVARNQIADLIGADSR-EIVFTSGATESDNLAI 83
Cdd:pfam00266   1 IYLDSAATTQKPQEVLDAIQEYYTD--YNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNdEIIFTSGTTEAINLVA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  84 KGAAHFYQtKGKHIITVKTEHKAVLDTCRQL-EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQP 162
Cdd:pfam00266  79 LSLGRSLK-PGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 163 IKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKPRVRLEAIIHGGG-------H 235
Cdd:pfam00266 158 VPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 236 ERGM-------RSGTLPVHQIVGMGEAYR-IAKEEMATEMARLTVLRDRLYNGFKDIEEVYVNGSmeegKRIGSNLNISF 307
Cdd:pfam00266 238 ESTFadapwkfEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGP----ERRASIISFNF 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721624170 308 NFVEGESLMMSLRD--IAVSSGSACTsaslEPSYVLRAIgrddelaHSSIRFTLGRWTTEEEID 369
Cdd:pfam00266 314 KGVHPHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVD 366
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
5-379 4.56e-77

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 243.89  E-value: 4.56e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   5 IYLDYAATTPMDERVAKKMMEYMTKDGifGNPASRSHKFGWEAEEAVDVARNQIADLIGADSR-EIVFTSGATESDNLAI 83
Cdd:COG0520    17 VYLDNAATGQKPRPVIDAIRDYYEPYN--ANVHRGAHELSAEATDAYEAAREKVARFIGAASPdEIIFTRGTTEAINLVA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  84 KGAAHFyqTKGKHIITVKTEHKAVLDTCRQL-EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQP 162
Cdd:COG0520    95 YGLGRL--KPGDEILITEMEHHSNIVPWQELaERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVNP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 163 IKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVCRKprvRLEAII--HGGGH----- 235
Cdd:COG0520   173 VKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRE---LLEALPpfLGGGGmiewv 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 236 ----------ERGMRSGTLPVHQIVGMGEA--Y--RIAKEEMAtemARLTVLRDRLYNGFKDIEEVYVNGSMEEGKRIGS 301
Cdd:COG0520   250 sfdgttyadlPRRFEAGTPNIAGAIGLGAAidYleAIGMEAIE---ARERELTAYALEGLAAIPGVRILGPADPEDRSGI 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 302 nlnISFNfVEGE-----SLMMSLRDIAVSSGSACTsaslEPsyVLRAIGrddelAHSSIRFTLGRWTTEEEIDHTIEIVK 376
Cdd:COG0520   327 ---VSFN-VDGVhphdvAALLDDEGIAVRAGHHCA----QP--LMRRLG-----VPGTVRASFHLYNTEEEIDRLVEALK 391

                  ...
gi 1721624170 377 KAI 379
Cdd:COG0520   392 KLA 394
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
5-373 1.07e-74

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: 236.98  E-value: 1.07e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   5 IYLDYAATTPMDERVAKKMMEYMTKDGifGNPASRSHKFGWEAEEAVDVARNQIADLIGA-DSREIVFTSGATESDNLAI 83
Cdd:cd06453     1 VYLDNAATSQKPQPVIDAIVDYYRHYN--ANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  84 KGAAhFYQTKGKHIITVKTEHKAVLDTCRQL-EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQP 162
Cdd:cd06453    79 YGLG-RANKPGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 163 IKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYVcrKPRVrLEAI--IHGGG------ 234
Cdd:cd06453   158 VKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYG--KEEL-LEEMppYGGGGemieev 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 235 -------HERGMR--SGTLPVHQIVGMGEA--Y--RIAKEEMATEMARLTvlrDRLYNGFKDIEEVYVNGSMEegKRIGS 301
Cdd:cd06453   235 sfeettyADLPHKfeAGTPNIAGAIGLGAAidYleKIGMEAIAAHEHELT---AYALERLSEIPGVRVYGDAE--DRAGV 309
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721624170 302 nlnISFNfVEGE-----SLMMSLRDIAVSSGSACTsaslEPsyVLRAIGrddelAHSSIRFTLGRWTTEEEIDHTIE 373
Cdd:cd06453   310 ---VSFN-LEGIhphdvATILDQYGIAVRAGHHCA----QP--LMRRLG-----VPGTVRASFGLYNTEEEIDALVE 371
PLN02855 PLN02855
Bifunctional selenocysteine lyase/cysteine desulfurase
5-385 7.29e-37

Bifunctional selenocysteine lyase/cysteine desulfurase


Pssm-ID: 215460 [Multi-domain]  Cd Length: 424  Bit Score: 138.73  E-value: 7.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   5 IYLDYAATTPMDERVAKKMMEYMTkdGIFGNPASRSHKFGWEAEEAVDVARNQIADLIGA-DSREIVFTSGATESDNLAI 83
Cdd:PLN02855   34 VYLDNAATSQKPAAVLDALQDYYE--EYNSNVHRGIHALSAKATDAYELARKKVAAFINAsTSREIVFTRNATEAINLVA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  84 K--GAAHFYQtkGKHIITVKTEHKAVLdTCRQL--EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGV 159
Cdd:PLN02855  112 YtwGLANLKP--GDEVILSVAEHHSNI-VPWQLvaQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGS 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 160 IQPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYvcRKPRVrLEAI--IHGGGH-- 235
Cdd:PLN02855  189 ILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLW--GKSDL-LESMppFLGGGEmi 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 236 -----------ERGMR--SGTLPVHQIVGMGEA--Y-------RIAKEEMAtemarltvLRDRLYNGFKDIEEVYVNGSM 293
Cdd:PLN02855  266 sdvfldhstyaPPPSRfeAGTPAIGEAIGLGAAidYlseigmdRIHEYEVE--------LGTYLYEKLSSVPGVRIYGPK 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 294 EEGKRIGSNLnISFNfVEG------ESLMMSLRDIAVSSGSACTsaslEPSYvlRAIGrddelAHSSIRFTLGRWTTEEE 367
Cdd:PLN02855  338 PSEGVGRAAL-CAFN-VEGihptdlSTFLDQQHGVAIRSGHHCA----QPLH--RYLG-----VNASARASLYFYNTKEE 404
                         410
                  ....*....|....*...
gi 1721624170 368 IDHTIEIVKKAIVKLREL 385
Cdd:PLN02855  405 VDAFIHALKDTIAFFSSF 422
PRK09295 PRK09295
cysteine desulfurase SufS;
5-218 3.78e-31

cysteine desulfurase SufS;


Pssm-ID: 181766 [Multi-domain]  Cd Length: 406  Bit Score: 122.94  E-value: 3.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   5 IYLDYAATTPMDERVAKKMMEY------MTKDGIfgnpasrsHKFGWEAEEAVDVARNQIADLIGADSRE-IVFTSGATE 77
Cdd:PRK09295   25 AYLDSAASAQKPSQVIDAEAEFyrhgyaAVHRGI--------HTLSAQATEKMENVRKQAALFINARSAEeLVFVRGTTE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  78 SDNLAIKGAAHFYQTKGKHIITVKTEHKAVLDTCRQL-EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNE 156
Cdd:PRK09295   97 GINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLcARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNV 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721624170 157 MGVIQPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYV 218
Cdd:PRK09295  177 LGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYV 238
PRK10874 PRK10874
cysteine desulfurase CsdA;
5-234 7.00e-23

cysteine desulfurase CsdA;


Pssm-ID: 182799 [Multi-domain]  Cd Length: 401  Bit Score: 99.34  E-value: 7.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   5 IYLDYAATTPMDERVAKKMMEYMTKDGifGNPASRSHKFGWEAEEAVDVARNQIADLIGA-DSREIVFTSGATESDNLAI 83
Cdd:PRK10874   21 VYLDSAATALKPQAVIEATQQFYSLSA--GNVHRSQFAAAQRLTARYEAAREQVAQLLNApDAKNIVWTRGTTESINLVA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  84 KGAAHFYQTKGKHIITVKTEHKAVLDTCRQL-EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQP 162
Cdd:PRK10874   99 QSYARPRLQPGDEIIVSEAEHHANLVPWLMVaQQTGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGCPD 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721624170 163 IKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSFSSHKLYGPKGIGGLYvcRKPRvRLEAII--HGGG 234
Cdd:PRK10874  179 LARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLY--GKSE-LLEAMSpwQGGG 249
f2_encap_cargo1 NF041166
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ...
54-235 2.16e-20

family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide. Proteins of this family are cysteine desulfurases with an additional N-terminal encapsulation targeting sequence (~200 aa) that is necessary and sufficient for compartmentalization.


Pssm-ID: 469077 [Multi-domain]  Cd Length: 623  Bit Score: 93.38  E-value: 2.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  54 ARNQIADLIGADS-REIVFTSGATESDNLAIK--GAAHFYQtkGKHIITVKTEHKAVLDTCRQL-EREG--FEVTYLDpe 127
Cdd:NF041166  294 AREKVRRFIGAPSvDEIIFVRGTTEAINLVAKswGRQNIGA--GDEIIVSHLEHHANIVPWQQLaQETGakLRVIPVD-- 369
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 128 EDG--ILD-LAKLkaaIRPDTILVSVMHVNNEMGVIQPIKEIGAICRAK--KIIfhVDATQSVGKIEVNVQDLNVDLMSF 202
Cdd:NF041166  370 DSGqiLLDeYAKL---LNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAgaKVL--VDGAQSVSHMPVDVQALDADFFVF 444
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1721624170 203 SSHKLYGPKGIGGLYvcRKPRVrLEAI--IHGGGH 235
Cdd:NF041166  445 SGHKVFGPTGIGVVY--GKRDL-LEAMppWQGGGN 476
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
45-218 5.77e-14

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: 69.33  E-value: 5.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  45 WEAEEAVdvarnqiADLIGADSREIVFTSGATESDNLAIKGAAhfyqTKGKHIITVKTEHKAVldTCRQLEREGFEVTYL 124
Cdd:cd01494     3 EELEEKL-------ARLLQPGNDKAVFVPSGTGANEAALLALL----GPGDEVIVDANGHGSR--YWVAAELAGAKPVPV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 125 --DPEEDGILDLAKL-KAAIRPDTILVSVMHVNNEMGVIQPIKEIGAICRAKKIIFHVDATQSVG---KIEVNVQDLNVD 198
Cdd:cd01494    70 pvDDAGYGGLDVAILeELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGaspAPGVLIPEGGAD 149
                         170       180
                  ....*....|....*....|
gi 1721624170 199 LMSFSSHKLYGPKGIGGLYV 218
Cdd:cd01494   150 VVTFSLHKNLGGEGGGVVIV 169
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
115-282 1.99e-13

Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439845 [Multi-domain]  Cd Length: 376  Bit Score: 70.89  E-value: 1.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 115 EREGFEVTYLDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEM--GVIQPIKEIGAICRAKKIIFHVDATQSVGKIEVNV 192
Cdd:COG0075    94 ERYGAEVVVLEVPWGEAVDPEEVEEALAADPDIKAVAVVHNETstGVLNPLEEIGALAKEHGALLIVDAVSSLGGVPLDM 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 193 QDLNVDLMSFSSHK-LYGPKGIGglYVCRKPRVrLEAIihgggHERGMRS------------------GTLPVHQIVGMG 253
Cdd:COG0075   174 DEWGIDVVVSGSQKcLMLPPGLA--FVAVSERA-LEAI-----EARKLPSyyldlklwlkywekgqtpYTPPVSLLYALR 245
                         170       180       190
                  ....*....|....*....|....*....|
gi 1721624170 254 EAYRIAKEE-MATEMARLTVLRDRLYNGFK 282
Cdd:COG0075   246 EALDLILEEgLENRFARHRRLAEALRAGLE 275
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
13-218 2.40e-11

DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.


Pssm-ID: 99743 [Multi-domain]  Cd Length: 345  Bit Score: 64.53  E-value: 2.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  13 TPMDERVAKKMMEYMTKdGIFGNPASRSHKFgweAE-EAVDVarNQIADLIGADSREI--VFTSGATESDNLAIKGAAHF 89
Cdd:cd06450     7 TTMDPPALLLEMLTSAK-NAIDFTWDESPAA---TEmEAEVV--NWLAKLFGLPSEDAdgVFTSGGSESNLLALLAARDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  90 YQTKGKH----------IITVKTEHKAVLDTCRQLEREgfeVTYLDPEEDGILDLAKLKAAIRPD------TILVSVMHV 153
Cdd:cd06450    81 ARKRLKAgggrgidklvIVCSDQAHVSVEKAAAYLDVK---VRLVPVDEDGRMDPEALEAAIDEDkaeglnPIMVVATAG 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721624170 154 NNEMGVIQPIKEIGAICRAKKIIFHVDAT------------QSVGKIEvnvqdlNVDLMSFSSHKLYG-PKGIGGLYV 218
Cdd:cd06450   158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAyggfllpfpeprHLDFGIE------RVDSISVDPHKYGLvPLGCSAVLV 229
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
113-282 1.90e-10

Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.


Pssm-ID: 99744 [Multi-domain]  Cd Length: 356  Bit Score: 61.92  E-value: 1.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 113 QLEREGFEVTYLDPEEDGILDLAKLKAAIRPDTI-LVSVMHVNNEMGVIQPIKEIGAICRAKKIIFHVDATQSVGKIEVN 191
Cdd:cd06451    92 MAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIkAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFR 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 192 VQDLNVDLMSFSSHK-LYGPKGIGglYVCRKPRVrLEAIIHGGGH---------------ERGMRSGTLPVHQIVGMGEA 255
Cdd:cd06451   172 MDEWGVDVAYTGSQKaLGAPPGLG--PIAFSERA-LERIKKKTKPkgfyfdlllllkywgEGYSYPHTPPVNLLYALREA 248
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1721624170 256 YRIAKEE-------MATEMARltVLRDRLYN-GFK 282
Cdd:cd06451   249 LDLILEEglenrwaRHRRLAK--ALREGLEAlGLK 281
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
56-228 5.07e-09

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 439846 [Multi-domain]  Cd Length: 460  Bit Score: 57.92  E-value: 5.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  56 NQIADLIGADSREI-VFTSGATESdNL-AIKGA-----AHFYQTKGKH------IITVKTEH----KA--VLDtcrqLER 116
Cdd:COG0076   114 RWLADLLGLPEGAGgVFTSGGTEA-NLlALLAArdralARRVRAEGLPgaprprIVVSEEAHssvdKAarLLG----LGR 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 117 EGfeVTYLDPEEDGILDLAKLKAAIRPD------TILV-----SVMHvnnemGVIQPIKEIGAICRAKKIIFHVDA---- 181
Cdd:COG0076   189 DA--LRKVPVDEDGRMDPDALEAAIDEDraaglnPIAVvatagTTNT-----GAIDPLAEIADIAREHGLWLHVDAaygg 261
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1721624170 182 --------TQSVGKIEvnvqdlNVDLMSFSSHK-LYGPKGIGGLYVcRKPRVRLEA 228
Cdd:COG0076   262 falpspelRHLLDGIE------RADSITVDPHKwLYVPYGCGAVLV-RDPELLREA 310
PRK13479 PRK13479
2-aminoethylphosphonate--pyruvate transaminase; Provisional
114-214 7.11e-08

2-aminoethylphosphonate--pyruvate transaminase; Provisional


Pssm-ID: 184076 [Multi-domain]  Cd Length: 368  Bit Score: 53.76  E-value: 7.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 114 LEREGFEVTYLDPEEDGILDLAKLKAAIR--PDTILVSVMHVNNEMGVIQPIKEIGAICRA--KKIIfhVDATQSVGKIE 189
Cdd:PRK13479   99 AEYLGIAHVVLDTGEDEPPDAAEVEAALAadPRITHVALVHCETTTGILNPLDEIAAVAKRhgKRLI--VDAMSSFGAIP 176
                          90       100
                  ....*....|....*....|....*.
gi 1721624170 190 VNVQDLNVDLMSFSSHK-LYGPKGIG 214
Cdd:PRK13479  177 IDIAELGIDALISSANKcIEGVPGFG 202
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
58-295 8.74e-08

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 53.37  E-value: 8.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  58 IADLIGADSreIVFTSGATESDNLAIkgAAHFyqTKGKHIITVKTEHkAVLDTCRQL-EREGFEVTYLDPEEDGILDLAK 136
Cdd:pfam01212  41 VAELFGKEA--ALFVPSGTAANQLAL--MAHC--QRGDEVICGEPAH-IHFDETGGHaELGGVQPRPLDGDEAGNMDLED 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 137 LKAAIRPDTI-------LVSVMHVNNEMG--VIQP--IKEIGAICRAKKIIFHVDATQ---SVGKIEVNVQDL--NVDLM 200
Cdd:pfam01212 114 LEAAIREVGAdifpptgLISLENTHNSAGgqVVSLenLREIAALAREHGIPVHLDGARfanAAVALGVIVKEItsYADSV 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 201 SFSSHK-LYGPkgIGGLYVCRKPRVRlEAI----IHGGgherGMR-SGTLPVHQIVGMGEAYRIAKEemATEMARltvlr 274
Cdd:pfam01212 194 TMCLSKgLGAP--VGSVLAGSDDFIA-KAIrqrkYLGG----GLRqAGVLAAAGLRALEEGVARLAR--DHATAR----- 259
                         250       260
                  ....*....|....*....|....*.
gi 1721624170 275 dRLYNGFKDI-----EEVYVNGSMEE 295
Cdd:pfam01212 260 -RLAEGLELLrlaipRRVYTNTHMVY 284
PRK05939 PRK05939
cystathionine gamma-synthase family protein;
93-182 6.85e-07

cystathionine gamma-synthase family protein;


Pssm-ID: 235650 [Multi-domain]  Cd Length: 397  Bit Score: 50.84  E-value: 6.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  93 KGKHIIT---VKTEHKAVLDTCRQLereGFEVTYLDPEedgilDLAKLKAAIRPDTILVSVMHVNNEMGVIQPIKEIGAI 169
Cdd:PRK05939   85 AGDHLVSsqfLFGNTNSLFGTLRGL---GVEVTMVDAT-----DVQNVAAAIRPNTRMVFVETIANPGTQVADLAGIGAL 156
                          90
                  ....*....|...
gi 1721624170 170 CRAKKIIFHVDAT 182
Cdd:PRK05939  157 CRERGLLYVVDNT 169
PRK00451 PRK00451
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
91-177 8.11e-06

aminomethyl-transferring glycine dehydrogenase subunit GcvPA;


Pssm-ID: 234769 [Multi-domain]  Cd Length: 447  Bit Score: 47.83  E-value: 8.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  91 QTKGKHIITVKT---EHKAVLDTcrQLEREGFEVTYLDPEeDGILDLAKLKAAIRPDTILVSVMHvNNEMGVIQPIKEIG 167
Cdd:PRK00451  151 ITKRKKVLVSGAvhpEYREVLKT--YLKGQGIEVVEVPYE-DGVTDLEALEAAVDDDTAAVVVQY-PNFFGVIEDLEEIA 226
                          90
                  ....*....|
gi 1721624170 168 AICRAKKIIF 177
Cdd:PRK00451  227 EIAHAGGALF 236
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
55-377 1.67e-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: 46.57  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  55 RNQIADLIG------ADSREIVFTSGATEsdnlAIKGAAHFYQTKGKHIITVK---TEHKAVldtcrqLEREGFEVTY-- 123
Cdd:cd00609    42 REAIAEWLGrrggvdVPPEEIVVTNGAQE----ALSLLLRALLNPGDEVLVPDptyPGYEAA------ARLAGAEVVPvp 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 124 LDPEEDGILDLAKLKAAIRPDTILVSVMHVNNEMGVIQP---IKEIGAICRAKKII--------------FHVDATQSVG 186
Cdd:cd00609   112 LDEEGGFLLDLELLEAAKTPKTKLLYLNNPNNPTGAVLSeeeLEELAELAKKHGILiisdeayaelvydgEPPPALALLD 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 187 KIEvNVqdlnVDLMSFSshKLYGPKG--IGGLYVCRKPRVRLEAIIHgggherGMRSGTLPVHQIVGMGEAYRIAKEEMA 264
Cdd:cd00609   192 AYE-RV----IVLRSFS--KTFGLPGlrIGYLIAPPEELLERLKKLL------PYTTSGPSTLSQAAAAAALDDGEEHLE 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 265 TEMARLTVLRDRLYNGFKDIEEVYVNGSMeegkriGSNLnisfnfvegesLMMSLRDIavSSGSACTSASLEPSYVLRAI 344
Cdd:cd00609   259 ELRERYRRRRDALLEALKELGPLVVVKPS------GGFF-----------LWLDLPEG--DDEEFLERLLLEAGVVVRPG 319
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1721624170 345 GRDDELAHSSIRFTLGrwTTEEEIDHTIEIVKK 377
Cdd:cd00609   320 SAFGEGGEGFVRLSFA--TPEEELEEALERLAE 350
SepCysS cd06452
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ...
58-213 4.81e-05

Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.


Pssm-ID: 99745  Cd Length: 361  Bit Score: 45.07  E-value: 4.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  58 IADLIGADsrEIVFTSGATEsdnlAIKGAAHFYQTKGKHIITVK----TEHKAVldtcrqlEREGFEVT----------Y 123
Cdd:cd06452    53 LAEFLGMD--EARVTPGARE----GKFAVMHSLCEKGDWVVVDGlahyTSYVAA-------ERAGLNVRevpntghpeyH 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 124 LDPEEDG-ILDLAKLKAAIRPDTILVSvmHVNNEMGVIQPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMSF 202
Cdd:cd06452   120 ITPEGYAeVIEEVKDEFGKPPALALLT--HVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVG 197
                         170
                  ....*....|....
gi 1721624170 203 SSHKLY---GPKGI 213
Cdd:cd06452   198 SGHKSMaasAPIGV 211
GDC-P cd00613
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ...
58-259 1.73e-04

Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalysed by this protein is: Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2. Alpha-beta-type dimers associate to form an alpha(2)beta(2) tetramer, where the alpha- and beta-subunits are structurally similar and appear to have arisen by gene duplication and subsequent divergence with a loss of one active site. The members of this CD are widely dispersed among all three forms of cellular life.


Pssm-ID: 99737 [Multi-domain]  Cd Length: 398  Bit Score: 43.37  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  58 IADLIGADSREIVFTSGATESDNLAIKGAAHFYQTKGKHII--TVKTEHKAVLDTCrqLEREGFEVTYLDPEEDGILDLA 135
Cdd:cd00613    73 LCELTGMDVANASLQDEATAAAEAAGLAAIRAYHKRNKVLVpdSAHPTNPAVARTR--GEPLGIEVVEVPSDEGGTVDLE 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 136 KLKAAIRPDTILVSVMHVNNEmGVI-QPIKEIGAICRAKKIIFHVDATQsvgkieVNVQ------DLNVDLMSFSSHKLY 208
Cdd:cd00613   151 ALKEEVSEEVAALMVQYPNTL-GVFeDLIKEIADIAHSAGALVYVDGDN------LNLTglkppgEYGADIVVGNLQKTG 223
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721624170 209 GPKGIGGLYV----CRKPRVRLeaiihggghergmrsgtLPVHqIVGMGE------AYRIA 259
Cdd:cd00613   224 VPHGGGGPGAgffaVKKELVRF-----------------LPGR-LVGVTKdaegnrAFRLA 266
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
12-180 1.17e-03

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 40.78  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  12 TTPMDErvakkMMEYMTKdgifgnpASRSHKfGWEAEEAVDVARNQIADLIGADsrEIVFTSGATESDNLAIKGAAHFYQ 91
Cdd:cd06502     8 TGPTPE-----MLEAMAA-------ANVGDD-VYGEDPTTAKLEARAAELFGKE--AALFVPSGTAANQLALAAHTQPGG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  92 T----KGKHIITvktehkavlDTCRQLEREGFEVTYLDPEEDGILDLAKLKAAIRPD-------TILVSVMHVNNEMGVI 160
Cdd:cd06502    73 SvichETAHIYT---------DEAGAPEFLSGVKLLPVPGENGKLTPEDLEAAIRPRddihfppPSLVSLENTTEGGTVY 143
                         170       180
                  ....*....|....*....|..
gi 1721624170 161 QP--IKEIGAICRAKKIIFHVD 180
Cdd:cd06502   144 PLdeLKAISALAKENGLPLHLD 165
PRK09331 PRK09331
Sep-tRNA:Cys-tRNA synthetase; Provisional
58-213 1.78e-03

Sep-tRNA:Cys-tRNA synthetase; Provisional


Pssm-ID: 236469  Cd Length: 387  Bit Score: 40.30  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  58 IADLIGADsrEIVFTSGATESdnlaiKGA-AHFYQTKGKHIITVK----TEHKAVldtcrqlEREGFEVTYLDPEE--DG 130
Cdd:PRK09331   72 LAEFLGMD--EARVTHGAREG-----KFAvMHSLCKKGDYVVLDGlahyTSYVAA-------ERAGLNVREVPKTGypEY 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170 131 ILDLAKLKAAIR---------PDTILVSvmHVNNEMGVIQPIKEIGAICRAKKIIFHVDATQSVGKIEVNVQDLNVDLMS 201
Cdd:PRK09331  138 KITPEAYAEKIEevkeetgkpPALALLT--HVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIV 215
                         170
                  ....*....|....*
gi 1721624170 202 FSSHKLY---GPKGI 213
Cdd:PRK09331  216 GSGHKSMaasAPSGV 230
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
126-180 1.91e-03

Threonine aldolase [Amino acid transport and metabolism];


Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 40.05  E-value: 1.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721624170 126 PEEDGILDLAKLKAAIRPDTI------LVSVMHVNnEMGVIQP---IKEIGAICRAKKIIFHVD 180
Cdd:COG2008   105 PGEDGKLTPEDLEAAIRPGDVhfpqpgLVSLENTT-EGGTVYPleeLRAIAAVAREHGLPLHLD 167
PLN02724 PLN02724
Molybdenum cofactor sulfurase
5-108 2.58e-03

Molybdenum cofactor sulfurase


Pssm-ID: 215384 [Multi-domain]  Cd Length: 805  Bit Score: 40.24  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170   5 IYLDYAATTPMDErvakKMMEYMTKD---GIFGNPASRSHKfGWEAEEAVDVARNQIADLIGADSRE--IVFTSGATESd 79
Cdd:PLN02724   36 VYLDHAGATLYSE----SQLEAALADfssNVYGNPHSQSDS-SMRSSDTIESARQQVLEYFNAPPSDyaCVFTSGATAA- 109
                          90       100
                  ....*....|....*....|....*....
gi 1721624170  80 nLAIKGAAhFYQTKGKHIITVKTEHKAVL 108
Cdd:PLN02724  110 -LKLVGET-FPWSSESHFCYTLENHNSVL 136
PRK07324 PRK07324
transaminase; Validated
65-181 2.71e-03

transaminase; Validated


Pssm-ID: 235989  Cd Length: 373  Bit Score: 39.54  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721624170  65 DSREIVFTSGATESDNLAIKGAAHfyqtKGKHIItvktehkAVLDTCRQL----EREGFEVTYLD-PEEDGIL-DLAKLK 138
Cdd:PRK07324   79 KPENILQTNGATGANFLVLYALVE----PGDHVI-------SVYPTYQQLydipESLGAEVDYWQlKEENGWLpDLDELR 147
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1721624170 139 AAIRPDTILVSVMHVNNEMGVIQP---IKEIGAICRAkkiifhVDA 181
Cdd:PRK07324  148 RLVRPNTKLICINNANNPTGALMDrayLEEIVEIARS------VDA 187
GcvP1 COG0403
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ...
103-181 3.21e-03

Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain is part of the Pathway/BioSystem: Glycine cleavage


Pssm-ID: 440172 [Multi-domain]  Cd Length: 442  Bit Score: 39.63  E-value: 3.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721624170 103 EHKAVLDTcrQLEREGFEVTYLdPEEDGILDLAKLKAAIRPDTILVSVMHVNNEmGVIQPIKEIGAICRAKKIIFHVDA 181
Cdd:COG0403   167 QTRAVLKT--YAEPLGIEVVEV-PDEDGVTDLEALKALLDDDVAGVLVQYPNFF-GVIEDLRAIAEAAHAAGALVIVAA 241
 
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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