|
Name |
Accession |
Description |
Interval |
E-value |
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
1-383 |
3.51e-142 |
|
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: 409.05 E-value: 3.51e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 1 MIYLDNNATTTIDPLVVDAMTQQWARGPFNPSSQHQLGQQASQQLDLALLEMGRCLNSDfttPGgpRLIWTSGGTESNNL 80
Cdd:COG1104 3 MIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGAD---PE--EIIFTSGGTEANNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 81 ALAGLGDDPAAP---LIVSRIEHPSVLRFAQLAEKSGRQVSYLNICSDGSVDLNHLQELLDAQHSLspvVAVMSANNETG 157
Cdd:COG1104 78 AIKGAARAYRKKgkhIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTAL---VSVMHANNETG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 158 VIQPIEQLASLCRAAGALVHVDATQSIGKEPLDLATLPIDSLCFSAHKFHGPVGVGALWLGAGVNIRPHLIGGEQQLLSR 237
Cdd:COG1104 155 TIQPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGVRLEPLIHGGGQERGLR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 238 PGTIPVPLAAGTAKALSLAVGNLSEHRATMVRLRDLLEQRLAAAIPPLVIHGVDAKRLPNTTCVSFPGTDRQSMLMALDM 317
Cdd:COG1104 235 SGTENVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALDL 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712519945 318 AGVCCSSGSACSSGSSPPSHVLLAMGCDDALVSSAIRFGVSRFSTTGDIDTAAERICLVHKRLTSR 383
Cdd:COG1104 315 AGIAVSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKL 380
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
2-380 |
3.36e-103 |
|
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related families of cysteine desulfurase involved in iron-sulfur (FeS) cluster biosynthesis. NifS is part of the NIF system, usually associated with other nif genes involved in nitrogenase expression and nitrogen fixation. The protein family is given a fairly broad interpretation here. It includes a clade nearly always found in extended nitrogen fixation genomic regions, plus a second clade more closely related to the first than to IscS and also part of NifS-like/NifU-like systems. This model does not extend to a more distantly clade found in the epsilon proteobacteria such as Helicobacter pylori, also named NifS in the literature, built instead in TIGR03403.
Pssm-ID: 132443 [Multi-domain] Cd Length: 379 Bit Score: 309.54 E-value: 3.36e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 2 IYLDNNATTTIDPLVVDAMTqqwargPF------NPSSQHQLGQQASQQLDLALLEMGRCLNSDFTtpggpRLIWTSGGT 75
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAML------PYfteyfgNPSSMHSFGGEVGKAVEEAREQVAKLLGAEPD-----EIIFTSGGT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 76 ESNNLALagLGDDPAAP----LIVSRIEHPSVLRFAQLAEKSGRQVSYLNICSDGSVDLNHLQELLDAQHSLspvVAVMS 151
Cdd:TIGR03402 70 ESDNTAI--KSALAAQPekrhIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTAL---VSVMW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 152 ANNETGVIQPIEQLASLCRAAGALVHVDATQSIGKEPLDLATLPIDSLCFSAHKFHGPVGVGALWLGAGVNIRPHLIGGE 231
Cdd:TIGR03402 145 ANNETGTIFPIEEIGEIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKGTRFRPLLRGGH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 232 QQLLSRPGTIPVPLAAGTAKALSLAVGNLSEHRATMVRLRDLLEQRLAAAIPPLVIHGVDAKRLPNTTCVSFPGTDRQSM 311
Cdd:TIGR03402 225 QERGRRAGTENVPGIVGLGKAAELATEHLEEENTRVRALRDRLEAGLLARIPDARLNGDPTKRLPNTVNISFEYIEGEAI 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712519945 312 LMALDMAGVCCSSGSACSSGSSPPSHVLLAMGCDDALVSSAIRFGVSRFSTTGDIDTAAERICLVHKRL 380
Cdd:TIGR03402 305 LLLLDMEGICASSGSACTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIARL 373
|
|
| nifS_epsilon |
TIGR03403 |
cysteine desulfurase, NifS family, epsilon proteobacteria type; Members of this family are the ... |
2-382 |
5.08e-84 |
|
cysteine desulfurase, NifS family, epsilon proteobacteria type; Members of this family are the NifS-like cysteine desulfurase of the epsilon division of the Proteobacteria, similar to the NifS protein of nitrogen-fixing bacteria. Like NifS, and unlike IscS, this protein is found as part of a system of just two proteins, a cysteine desulfurase and a scaffold, for iron-sulfur cluster biosynthesis. This protein is called NifS by Olsen, et al. (), so we use this designation.
Pssm-ID: 132444 Cd Length: 382 Bit Score: 260.56 E-value: 5.08e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 2 IYLDNNATTTIDPLVVDAMTQQWARGPFNPSSQHQLGQQASQQLDLALLEMGRCLNSDfttpGGPRLIWTSGGTESNNLA 81
Cdd:TIGR03403 1 VYLDNNATTMLDPKVKELMDPFFCDIYGNPNSLHQFGTATHPAIAEALDKLYKGINAR----DLDDIIITSCATESNNWV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 82 LAGLGDDPAAP-----LIVSRIEHPSVLRFAQLAEKSGRQVSYLNICSDGSVDLNHLQELLDAQHSLspvVAVMSANNET 156
Cdd:TIGR03403 77 LKGVYFDEILKggknhIITTEVEHPAVRATCAFLESLGVEVTYLPINEQGTITAEQVREAITEKTAL---VSVMWANNET 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 157 GVIQPIEQLASLCRAAGALVHVDATQSIGKEPLDLATLPIDSLCFSAHKFHGPVGVGALWLGAGVNIRPHLIGGEQQLLS 236
Cdd:TIGR03403 154 GMIFPIKEIGEICKERGVLFHTDAVQAIGKIPVDVQKAGVDFLSFSAHKFHGPKGVGGLYIRKGVELTPLFHGGEHMGGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 237 RPGTIPVPLAAGTAKALSLAVGNLSEHRATMVRLRDLLEQRLaAAIPPLVIHGVDAKRLPNTTCVSFPGTDRQSMLMALD 316
Cdd:TIGR03403 234 RSGTLNVPYIVAMGEAMRLANEYLDFEKSHVRRLRDRLEDAL-LELPDVFVVGDREHRVPNTILISIKGVEGEAMLWDLN 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712519945 317 MAGVCCSSGSACSSGSSPPSHVLLAMGCDDALVSSAIRFGVSRFSTTGDIDTAAERICLVHKRLTS 382
Cdd:TIGR03403 313 KAGIAASTGSACASEDLEANPVMVAIGADKELAHTAIRLSLSRFTTEEEIDYTIEVFKKAVQRLRA 378
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
2-367 |
9.18e-81 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 251.50 E-value: 9.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 2 IYLDNNATTTIDPLVVDAMTqqwargPF------NPSSQ-HQLGQQASQQLDLALLEMGRCLNSDfttpgGPRLIWTSGG 74
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAML------PFliehfgNPHSRtHLYGWESEDAVEKARAQVAALIGAD-----PKEIIFTSGA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 75 TESNNLALAGLGD---DPAAPLIVSRIEHPSVLRFAQLAEKSGRQVSYLNICSDGSVDLnhlQELLDAQHSLSPVVAVMS 151
Cdd:PLN02651 70 TESNNLAIKGVMHfykDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDL---DELAAAIRPDTALVSVMA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 152 ANNETGVIQPIEQLASLCRAAGALVHVDATQSIGKEPLDLATLPIDSLCFSAHKFHGPVGVGALWL--GAGVNIRPHLIG 229
Cdd:PLN02651 147 VNNEIGVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVrrRPRVRLEPLMSG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 230 GEQQLLSRPGTIPVPLAAGTAKALSLAVGNLSEHRATMVRLRDLLEQRLAAAIPPLVIHGV--DAKRLPNTTCVSFPGTD 307
Cdd:PLN02651 227 GGQERGRRSGTENTPLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKLGGVRVNGPrdPEKRYPGTLNLSFAYVE 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 308 RQSMLMALdmAGVCCSSGSACSSGSSPPSHVLLAMGCDDALVSSAIRFGVSRFSTTGDID 367
Cdd:PLN02651 307 GESLLMGL--KEVAVSSGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEVD 364
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
2-374 |
1.94e-78 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 246.78 E-value: 1.94e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 2 IYLDNNATTTIDPLVVDAMTQQWAR-GPF-NPSSQ-HQLGQQASQQLDLALLEMGRCLNSDfttpggPR-LIWTSGGTES 77
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKMMPYLTMdGTFgNPASRsHRFGWQAEEAVDIARNQIADLIGAD------PReIVFTSGATES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 78 NNLALAGLGD---DPAAPLIVSRIEHPSVLRFAQLAEKSGRQVSYLNICSDGSVDLNHLQELLDAQHSLspvVAVMSANN 154
Cdd:PRK14012 79 DNLAIKGAAHfyqKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTIL---VSIMHVNN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 155 ETGVIQPIEQLASLCRAAGALVHVDATQSIGKEPLDLATLPIDSLCFSAHKFHGPVGVGALWLGAGVNIR--PHLIGGEQ 232
Cdd:PRK14012 156 EIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRleAQMHGGGH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 233 QLLSRPGTIPVPLAAGTAKALSLAVGNLSEHRATMVRLRDLLEQRLaAAIPPLVIHGVDAKRLPNTTCVSFPGTDRQSML 312
Cdd:PRK14012 236 ERGMRSGTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGI-KDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLI 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712519945 313 MAL-DMAgvcCSSGSACSSGSSPPSHVLLAMGCDDALVSSAIRFGVSRFSTTGDIDTAAERIC 374
Cdd:PRK14012 315 MALkDLA---VSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVR 374
|
|
| DNA_S_dndA |
TIGR03235 |
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a ... |
3-355 |
8.95e-75 |
|
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a larger family of cysteine desulfurases. It is encoded, typically, divergently from a conserved, sparsely distributed operon for sulfur modification of DNA. This modification system is designated dnd, after the phenotype of DNA degradation during electrophoresis. The system is sporadically distributed in bacteria, much like some restriction enzyme operons. DndB is described as a putative ATPase. [DNA metabolism, Restriction/modification]
Pssm-ID: 163191 [Multi-domain] Cd Length: 353 Bit Score: 235.85 E-value: 8.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 3 YLDNNATTTIDPLVVDAMtQQWARGPF-NPSSQ-HQLGQQASQQLDLALLEMGRCLNSDfttpgGPRLIWTSGGTESNNL 80
Cdd:TIGR03235 1 YLDHNATTPIDPAVAEAM-LPWLLEEFgNPSSRtHEFGHNAKKAVERARKQVAEALGAD-----TEEVIFTSGATESNNL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 81 ALAGLG----DDPAAPLIVSRIEHPSVLRFAQLAEKSGRQVSYLNICSDGSVDLNHLQELLDAQHSLspvVAVMSANNET 156
Cdd:TIGR03235 75 AILGLArageQKGKKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTLL---VSIMHVNNET 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 157 GVIQPIEQLASLCRAAGALVHVDATQSIGKEPLDLATLPIDSLCFSAHKFHGPVGVGALWLGAG----VNIRPHLIGGEQ 232
Cdd:TIGR03235 152 GSIQPIREIAEVLEAHEAFFHVDAAQVVGKITVDLSADRIDLISCSGHKIYGPKGIGALVIRKRgkpkAPLKPIMFGGGQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 233 QLLSRPGTIPVPLAAGTAKALSLAVGNlseHRATMVRLRDLLEQRLAA-AIPPLVIHGVDAKRLPNTTCVSFPGTDRQSM 311
Cdd:TIGR03235 232 ERGLRPGTLPVHLIVGMGEAAEIARRN---AQAWEVKLRAMRNQLRDAlQTLGVKLNGDPAETIPHILNFSIDGVNSEAL 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1712519945 312 LMALDmAGVCCSSGSACSSGSSPPSHVLLAMGCDDALVSSAIRF 355
Cdd:TIGR03235 309 IVNLR-ADAAVSTGSACSSSKYEPSHVLQAMGLDTDRARGAIRF 351
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
2-320 |
6.38e-64 |
|
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: 208.26 E-value: 6.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 2 IYLDNNATTTIDPLVVDAMTQQWARGPFNP-SSQHQLGQQASQQLDLALLEMGRCLNSDFTtpggPRLIWTSGGTESNNL 80
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINAPSN----DEIIFTSGTTEAINL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 81 ALAGLGD--DPAAPLIVSRIEHPSVLRFAQ-LAEKSGRQVSYLNICSDGSVDLNHLQELLDAQHSLspvVAVMSANNETG 157
Cdd:pfam00266 77 VALSLGRslKPGDEIVITEMEHHANLVPWQeLAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKL---VAITHVSNVTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 158 VIQPIEQLASLCRAAGALVHVDATQSIGKEPLDLATLPIDSLCFSAHKFHGPVGVGALWL--GAGVNIRPHLIGG----- 230
Cdd:pfam00266 154 TIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGrrDLLEKMPPLLGGGgmiet 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 231 ---------EQQLLSRPGTIPVPLAAGTAKALS-LAVGNLSEHRATMVRLRDLLEQRLaAAIPPLVIHGvdAKRLPNTTC 300
Cdd:pfam00266 234 vslqestfaDAPWKFEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERL-LSLPGIRLYG--PERRASIIS 310
|
330 340
....*....|....*....|
gi 1712519945 301 VSFPGTDRQSMLMALDMAGV 320
Cdd:pfam00266 311 FNFKGVHPHDVATLLDESGI 330
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
1-368 |
2.81e-46 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 162.59 E-value: 2.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 1 MIYLDNNATTtidPLVVDAMT--QQWARGPF-NPSSQHQLGQQASQQLDLALLEMGRCLNsdfttpGGPRLIW-TSGGTE 76
Cdd:PRK02948 1 MIYLDYAATT---PMSKEALQtyQKAASQYFgNESSLHDIGGTASSLLQVCRKTFAEMIG------GEEQGIYfTSGGTE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 77 SNNLA----LAGLGDDpAAPLIVSRIEHPSVLRFAQLAEKSGRQVSYLNICSDGSVDLNHLQELLDAQHSLspvVAVMSA 152
Cdd:PRK02948 72 SNYLAiqslLNALPQN-KKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVL---ASIQHA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 153 NNETGVIQPIEQLASLCRAAGALVHVDATQSIGKEPLDLATLPIDSLCFSAHKFHGPVGVGALWLGAGVNIRPHLIGGEQ 232
Cdd:PRK02948 148 NSEIGTIQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQVRWKPVFPGTTH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 233 QLLSRPGTIPVP-LAAGTAKALSLaVGNLSEHRATMVRLRDLLEQRLAAAIPPLVIHGVDAKRLPNTTCVSFPGTDRQSM 311
Cdd:PRK02948 228 EKGFRPGTVNVPgIAAFLTAAENI-LKNMQEESLRFKELRSYFLEQIQTLPLPIEVEGHSTSCLPHIIGVTIKGIEGQYT 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1712519945 312 LMALDMAGVCCSSGSACSSGSSPPSHVLLAMGCDDALVSSAIRFGVSRFSTTGDIDT 368
Cdd:PRK02948 307 MLECNRRGIAISTGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDT 363
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
2-320 |
1.89e-45 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 160.69 E-value: 1.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 2 IYLDNNATTTIDPLVVDAMTQQWARGPFNPS-SQHQLGQQASQQLDLALLEMGRCLNSDfttpgGPR-LIWTSGGTESNN 79
Cdd:COG0520 17 VYLDNAATGQKPRPVIDAIRDYYEPYNANVHrGAHELSAEATDAYEAAREKVARFIGAA-----SPDeIIFTRGTTEAIN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 80 LALAGL-----GDDpaapLIVSRIEHPSVLR-FAQLAEKSGRQVSYLNICSDGSVDLNHLQELLDAQHSLspvVAVMSAN 153
Cdd:COG0520 92 LVAYGLgrlkpGDE----ILITEMEHHSNIVpWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKL---VAVTHVS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 154 NETGVIQPIEQLASLCRAAGALVHVDATQSIGKEPLDLATLPIDSLCFSAHKFHGPVGVGALWLGAGV--NIRPHLIGGE 231
Cdd:COG0520 165 NVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELleALPPFLGGGG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 232 ---------QQLLSRP-----GTIPVPLAAGTAKALSL--AVGnLSEHRATMVRLRDLLEQRLaAAIPPLVIHG--VDAK 293
Cdd:COG0520 245 miewvsfdgTTYADLPrrfeaGTPNIAGAIGLGAAIDYleAIG-MEAIEARERELTAYALEGL-AAIPGVRILGpaDPED 322
|
330 340
....*....|....*....|....*....
gi 1712519945 294 RLPnttCVSF--PGTDRQSMLMALDMAGV 320
Cdd:COG0520 323 RSG---IVSFnvDGVHPHDVAALLDDEGI 348
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
2-371 |
3.12e-40 |
|
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: 146.07 E-value: 3.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 2 IYLDNNATTTIDPLVVDAMTQQWARGPFNPS-SQHQLGQQASQQLDLALLEMGRCLNSDFTTpggpRLIWTSGGTESNNL 80
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHrGVHELSARATDAYEAAREKVARFINAPSPD----EIIFTRNTTEAINL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 81 ALAGLGDDPAA--PLIVSRIEHPSVLR-FAQLAEKSGRQVSYLNICSDGSVDLNHLQELLDAQHSLspvVAVMSANNETG 157
Cdd:cd06453 77 VAYGLGRANKPgdEIVTSVMEHHSNIVpWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKL---VAVTHVSNVLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 158 VIQPIEQLASLCRAAGALVHVDATQSIGKEPLDLATLPIDSLCFSAHKFHGPVGVGALWLGAGV--NIRPHLIGGE---- 231
Cdd:cd06453 154 TINPVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELleEMPPYGGGGEmiee 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 232 --------QQLLSR--PGTIPVPLAAGTAKALS--LAVG--NLSEHRAtmvRLRDLLEQRLaAAIPPLVIHGVDAKRLPn 297
Cdd:cd06453 234 vsfeettyADLPHKfeAGTPNIAGAIGLGAAIDylEKIGmeAIAAHEH---ELTAYALERL-SEIPGVRVYGDAEDRAG- 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712519945 298 ttCVSF--PGTDRQSMLMALDMAGVccssgsacssGSSPPSHVllAMGCDDAL-VSSAIRFGVSRFSTTGDIDTAAE 371
Cdd:cd06453 309 --VVSFnlEGIHPHDVATILDQYGI----------AVRAGHHC--AQPLMRRLgVPGTVRASFGLYNTEEEIDALVE 371
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
2-320 |
6.61e-24 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 102.04 E-value: 6.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 2 IYLDNnATTTIDPLVVDAMTQQWARGPFNP--SSQHQLGQQASQQLDLALLEMGRCLNSdfttPGGPRLIWTSGGTESNN 79
Cdd:PRK10874 21 VYLDS-AATALKPQAVIEATQQFYSLSAGNvhRSQFAAAQRLTARYEAAREQVAQLLNA----PDAKNIVWTRGTTESIN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 80 LALAG-------LGDDpaapLIVSRIEHPSVL-RFAQLAEKSGRQVSYLNICSDGSVDLNHLQELLDAQhslSPVVAVMS 151
Cdd:PRK10874 96 LVAQSyarprlqPGDE----IIVSEAEHHANLvPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELITPR---TRILALGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 152 ANNETGVIQPIEQLASLCRAAGALVHVDATQSIGKEPLDLATLPIDSLCFSAHKFHGPVGVGAL------------WLGA 219
Cdd:PRK10874 169 MSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLygkselleamspWQGG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 220 GVNIRPHLIGGeqqllSRPGTIPVPLAAGT---------AKALS-LAVGNLSEHRATMVRLRDLLEQRLaAAIPplvihG 289
Cdd:PRK10874 249 GKMLTEVSFDG-----FTPQSAPWRFEAGTpnvagviglSAALEwLADIDINQAESWSRSLATLAEDAL-AKLP-----G 317
|
330 340 350
....*....|....*....|....*....|.
gi 1712519945 290 VDAKRLPnttcvsfpgtdrQSMLMALDMAGV 320
Cdd:PRK10874 318 FRSFRCQ------------DSSLLAFDFAGV 336
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
1-231 |
8.29e-24 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 101.75 E-value: 8.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 1 MIYLDNNATTTIDPLVVDAMTQQWA-------RGpfnpssQHQLGQQASQQLDLALLEMGRCLNSdfttPGGPRLIWTSG 73
Cdd:PLN02855 33 LVYLDNAATSQKPAAVLDALQDYYEeynsnvhRG------IHALSAKATDAYELARKKVAAFINA----STSREIVFTRN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 74 GTESNNL-----ALAGLGddPAAPLIVSRIEHPSVLRFAQL-AEKSGRQVSYLNICSDGSVDLNHLQELLDAQHSLspvV 147
Cdd:PLN02855 103 ATEAINLvaytwGLANLK--PGDEVILSVAEHHSNIVPWQLvAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKL---V 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 148 AVMSANNETGVIQPIEQLASLCRAAGALVHVDATQSIGKEPLDLATLPIDSLCFSAHKFHGPVGVGALWLGAGV--NIRP 225
Cdd:PLN02855 178 ATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLleSMPP 257
|
....*.
gi 1712519945 226 HLIGGE 231
Cdd:PLN02855 258 FLGGGE 263
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
2-367 |
6.97e-21 |
|
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family (pfam00266). The most closely related characterized proteins are active as cysteine desulfurases, selenocysteine lyases, or both; some are involved in FeS cofactor biosynthesis and are designated NifS. An active site Cys residue present in those sequences, in motifs resembling GHHC or GSAC, is not found in this family. The function of members of this family is unknown, but seems unlike to be as an aminotransferase. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273906 [Multi-domain] Cd Length: 397 Bit Score: 93.28 E-value: 6.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 2 IYLDNNATTTIDPLVVDAMTQQWARGPFNPSSQHQLGQQASQQLDLALLEMGRCLNSDfttpgGPRLIWTSGGTESNNLA 81
Cdd:TIGR01976 19 VFFDNPAGTQIPQSVADAVSAALTRSNANRGGAYESSRRADQVVDDAREAVADLLNAD-----PPEVVFGANATSLTFLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 82 LAGLGDD--PAAPLIVSRIEHPSVLR-FAQLAEKSGRQVSYLNI-CSDGSVDLNHLQELLDAQHSLspvVAVMSANNETG 157
Cdd:TIGR01976 94 SRAISRRwgPGDEVIVTRLDHEANISpWLQAAERAGAKVKWARVdEATGELHPDDLASLLSPRTRL---VAVTAASNTLG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 158 VIQPIEQLASLCRAAGALVHVDATQSIGKEPLDLATLPIDSLCFSAHKFHGPvGVGALWlgagvnIRPHLIGGEQQLLSR 237
Cdd:TIGR01976 171 SIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGP-HMGILW------GRPELLMNLPPYKLT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 238 P-----------GTIPVPLAAGTAKAL----SLAVGNLSEHRATMV-----------RLRDLLEQRLaAAIPPLVIHGVD 291
Cdd:TIGR01976 244 FsydtgperfelGTPQYELLAGVVAAVdylaGLGESANGSRRERLVasfqaidayenRLAEYLLVGL-SDLPGVTLYGVA 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712519945 292 --AKRLPnTTCVSFPGTDRQSMLMALDMAGVccssgsACSSGSSPPSHVLLAMGCDDalVSSAIRFGVSRFSTTGDID 367
Cdd:TIGR01976 323 rlAARVP-TVSFTVHGLPPQRVVRRLADQGI------DAWAGHFYAVRLLRRLGLND--EGGVVRVGLAHYNTAEEVD 391
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
1-216 |
2.39e-16 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 79.80 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 1 MIYLDNNATTTIDPLVVDAMTQ----QWA---RGPfnpssqHQLGQQASQQLdlallEMGRCLNSDFTTPGGPR-LIWTS 72
Cdd:PRK09295 24 LAYLDSAASAQKPSQVIDAEAEfyrhGYAavhRGI------HTLSAQATEKM-----ENVRKQAALFINARSAEeLVFVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 73 GGTESNNLALAGLGDDPAAP---LIVSRIEH-PSVLRFAQLAEKSGRQVSYLNICSDGSVDLNHLQELLDAQHSLspvVA 148
Cdd:PRK09295 93 GTTEGINLVANSWGNSNVRAgdnIIISEMEHhANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALFDERTRL---LA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712519945 149 VMSANNETGVIQPIEQLASLCRAAGALVHVDATQSIGKEPLDLATLPIDSLCFSAHKFHGPVGVGALW 216
Cdd:PRK09295 170 ITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILY 237
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
49-216 |
1.20e-12 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 65.48 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 49 LLEMGRCLnSDFTTPGGPRLIWTSGGTESNNLALAGLGDdPAAPLIVSRIEHPSVLRFAqlAEKSGRQVSYLNicSDGSV 128
Cdd:cd01494 2 LEELEEKL-ARLLQPGNDKAVFVPSGTGANEAALLALLG-PGDEVIVDANGHGSRYWVA--AELAGAKPVPVP--VDDAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 129 D-LNHLQELLDAQHSLSPVVAVMSAN-NETGVIQPIEQLASLCRAAGALVHVDATQSIGKEPLDLATLP---IDSLCFSA 203
Cdd:cd01494 76 YgGLDVAILEELKAKPNVALIVITPNtTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPeggADVVTFSL 155
|
170
....*....|...
gi 1712519945 204 HKFHGPVGVGALW 216
Cdd:cd01494 156 HKNLGGEGGGVVI 168
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
71-216 |
1.06e-11 |
|
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: 66.01 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 71 TSGGTESNNLALA--------------GLGDDPAAPLIVSRIEHPSVLRFAQLAEKSGRQVSYLNICSDGSVDLNHLQEL 136
Cdd:COG0076 131 TSGGTEANLLALLaardralarrvraeGLPGAPRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 137 LDAQHS--LSPVVAVMSANN-ETGVIQPIEQLASLCRAAGALVHVDA-------TQSIGKEPLD---LAtlpiDSLCFSA 203
Cdd:COG0076 211 IDEDRAagLNPIAVVATAGTtNTGAIDPLAEIADIAREHGLWLHVDAayggfalPSPELRHLLDgieRA----DSITVDP 286
|
170
....*....|....
gi 1712519945 204 HK-FHGPVGVGALW 216
Cdd:COG0076 287 HKwLYVPYGCGAVL 300
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
105-304 |
2.63e-11 |
|
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: 64.34 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 105 RFAQLAEKSGRQVSYLNICSDGSVDLNHLQELLDAQHSLSPVVAVMsanNET--GVIQPIEQLASLCRAAGALVHVDATQ 182
Cdd:COG0075 88 RWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPDIKAVAVVH---NETstGVLNPLEEIGALAKEHGALLIVDAVS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 183 SIGKEPLDLATLPIDSLCFSAHK-FHGPVGVGALWLG-------AGVNIRP-----HLIGGEQQLLSRPGTIPVPLAAGT 249
Cdd:COG0075 165 SLGGVPLDMDEWGIDVVVSGSQKcLMLPPGLAFVAVSeraleaiEARKLPSyyldlKLWLKYWEKGQTPYTPPVSLLYAL 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712519945 250 AKALSLAvgnLSE--------HRatmvRLRDLLEQRLAAAipPLVIHGVDAKRLPNTTCVSFP 304
Cdd:COG0075 245 REALDLI---LEEglenrfarHR----RLAEALRAGLEAL--GLELFAEEEYRSPTVTAVRVP 298
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
52-281 |
2.50e-10 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 61.17 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 52 MGRCLNSDFTTPGGprlIWTSGGTESNNLALAGLGDDPAAPLIVSRIEHPSVLRFAQLAeksGRQVSY--LNICSDGSVD 129
Cdd:pfam00155 52 LGRSPVLKLDREAA---VVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLA---GGEVVRypLYDSNDFHLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 130 LNHLQELLDAQHSlspVVAVMSANNETGVIQPIEQL---ASLCRAAGALVHVD--------ATQSIGKEPLDLATLPIDS 198
Cdd:pfam00155 126 FDALEAALKEKPK---VVLHTSPHNPTGTVATLEELeklLDLAKEHNILLLVDeayagfvfGSPDAVATRALLAEGPNLL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 199 LCFSAHKFHGPVGvgalWLGAGVNIRPHLIGGeQQLLSRPGTIPVPLAAGTAKALS---LAVGNLSEHRATMVRLRDLLE 275
Cdd:pfam00155 203 VVGSFSKAFGLAG----WRVGYILGNAAVISQ-LRKLARPFYSSTHLQAAAAAALSdplLVASELEEMRQRIKERRDYLR 277
|
....*.
gi 1712519945 276 QRLAAA 281
Cdd:pfam00155 278 DGLQAA 283
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
52-219 |
1.07e-09 |
|
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: 59.14 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 52 MGRCLNSDFTTPGGprlIWTSGGTESNNLAL------------AGLGDDPAAPLIV-SRIEHPSVLRFAQLAEKSGRQVS 118
Cdd:cd06450 47 LAKLFGLPSEDADG---VFTSGGSESNLLALlaardrarkrlkAGGGRGIDKLVIVcSDQAHVSVEKAAAYLDVKVRLVP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 119 YlniCSDGSVDLNHLQELL--DAQHSLSPVVAVMSA-NNETGVIQPIEQLASLCRAAGALVHVDATQS----IGKEPLD- 190
Cdd:cd06450 124 V---DEDGRMDPEALEAAIdeDKAEGLNPIMVVATAgTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGgfllPFPEPRHl 200
|
170 180 190
....*....|....*....|....*....|.
gi 1712519945 191 LATLP-IDSLCFSAHK-FHGPVGVGALWLGA 219
Cdd:cd06450 201 DFGIErVDSISVDPHKyGLVPLGCSAVLVRA 231
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
105-205 |
1.77e-09 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 58.77 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 105 RFAQLAEKSGRQVSYLNICSDGSVDLNHLQELLDAQHSLSPVVAVMSANNeTGVIQPIEQLASLCRAAGALVHVDATQSI 184
Cdd:PRK13479 94 RIAQIAEYLGIAHVVLDTGEDEPPDAAEVEAALAADPRITHVALVHCETT-TGILNPLDEIAAVAKRHGKRLIVDAMSSF 172
|
90 100
....*....|....*....|.
gi 1712519945 185 GKEPLDLATLPIDSLCFSAHK 205
Cdd:PRK13479 173 GAIPIDIAELGIDALISSANK 193
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
60-213 |
4.83e-08 |
|
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: 54.22 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 60 FTTPGGPRLIWTSGGTESNNLALAGLgDDPAAPLIVSRIEHPSvLRFAQLAEKSGRQVSYLNICSDGSVDLNHLQELLDa 139
Cdd:cd06451 45 FQTENGLTFLLSGSGTGAMEAALSNL-LEPGDKVLVGVNGVFG-DRWADMAERYGADVDVVEKPWGEAVSPEEIAEALE- 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712519945 140 QHSlspVVAVMSANNE--TGVIQPIEQLASLCRAAGALVHVDATQSIGKEPLDLATLPIDsLCFSAHK--FHGPVGVG 213
Cdd:cd06451 122 QHD---IKAVTLTHNEtsTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRMDEWGVD-VAYTGSQkaLGAPPGLG 195
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
71-288 |
1.70e-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: 46.18 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 71 TSGGTESNNLALAGLGDdPAAPLIVSRIEHPSVLRFAQLAeksGRQVSYLNICSDGSVDLNHLQELLDAQHSLSpVVAVM 150
Cdd:cd00609 65 TNGAQEALSLLLRALLN-PGDEVLVPDPTYPGYEAAARLA---GAEVVPVPLDEEGGFLLDLELLEAAKTPKTK-LLYLN 139
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 151 SANNETGVIQP---IEQLASLCRAAGALVHVD-ATQSIGKEPLDLATLPIDSL------CFSAHKFHGPVGvgalW-LGA 219
Cdd:cd00609 140 NPNNPTGAVLSeeeLEELAELAKKHGILIISDeAYAELVYDGEPPPALALLDAyervivLRSFSKTFGLPG----LrIGY 215
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170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 220 GVNIRPHLIGGEQQLLS-RPGTIPVPLAAGTAKALSLAVGNLSEHRATMVRLRDLLEQRLAAAIPPLVIH 288
Cdd:cd00609 216 LIAPPEELLERLKKLLPyTTSGPSTLSQAAAAAALDDGEEHLEELRERYRRRRDALLEALKELGPLVVVK 285
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| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
71-212 |
9.30e-05 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 44.26 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 71 TSGGTESNnlaLAG--LGDD--PAAPLIVSRIEHPSVLRFAQLAEKSGRQVSYLNicsDGSVDLNHLQELLDAQHSLSPV 146
Cdd:PRK02769 90 TNGGTEGN---LYGcyLARElfPDGTLYYSKDTHYSVSKIARLLRIKSRVITSLP---NGEIDYDDLISKIKENKNQPPI 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712519945 147 VAVMSANNETGVIQPIEQLASLCRAAGA---LVHVDATQS-------IGKEPLDLATlPIDSLCFSAHKFHG---PVGV 212
Cdd:PRK02769 164 IFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSgmilpfvNNPPPFSFAD-GIDSIAISGHKFIGspmPCGI 241
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| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
99-213 |
1.98e-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: 42.99 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712519945 99 EHPSVLRFAqlAEKSGRQVSYLNICSDGSVDLNHLQELLDAQhslspVVAVMSAN-NETGVI-QPIEQLASLCRAAGALV 176
Cdd:cd00613 120 TNPAVARTR--GEPLGIEVVEVPSDEGGTVDLEALKEEVSEE-----VAALMVQYpNTLGVFeDLIKEIADIAHSAGALV 192
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1712519945 177 HVDAtqsigkEPLDLATL--P----IDSLCFSAHKFHGPVGVG 213
Cdd:cd00613 193 YVDG------DNLNLTGLkpPgeygADIVVGNLQKTGVPHGGG 229
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