|
Name |
Accession |
Description |
Interval |
E-value |
| am_tr_V_EF2568 |
TIGR01977 |
cysteine desulfurase family protein; This model describes a subfamily of probable pyridoxal ... |
2-376 |
0e+00 |
|
cysteine desulfurase family protein; This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family. Related families contain members active as cysteine desulfurases, selenocysteine lyases, or both. The members of this family form a distinct clade and all are shorter at the N-terminus. The function of this subfamily is unknown. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 131032 [Multi-domain] Cd Length: 376 Bit Score: 526.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 2 IYLDNAATTYPKPERVYNAVLDCMKNYCANPGRAGHKLAMRAAREIYDTRENIAKLFNVSNPMNIVFTSNATDSLNLAIK 81
Cdd:TIGR01977 1 IYFDNAATTYPKPDEVYEAMADFYKNYGGSPGRGRYRLALRASREVEETRQLLAKLFNAPSSAHVVFTNNATTALNIALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 82 GVLQEGDHVITTSMEHNSVIRPIKAL-EKRGIENTVVKCDYEGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLIDIKKVG 160
Cdd:TIGR01977 81 GLLKEGDHVITTPMEHNSVARPLECLkEQIGVEITIVKCDNEGLISPERIKRAIKTNTKLIVVSHASNVTGTILPIEEIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 161 EIAKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKCLFGPQGTGILYVREGLNLNILKEGGTGSKSEEIVQPELFP 240
Cdd:TIGR01977 161 ELAQENGIFFILDAAQTAGVIPIDMTELAIDMLAFTGHKGLLGPQGTGGLYIREGIKLKPLKSGGTGSHSALIDQPSELP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 241 DKYESGTHNTPGIAGLNQGILFIFERGINNIRQHEEELCQYMIDKLEEVPDIKIYGPKDSKKRASVIALNIGDMDSGEVT 320
Cdd:TIGR01977 241 DRFESGTLNTPGIAGLNAGIKFIEKIGIANIAKKECMLTEKLLNGLREINKVKIYGPADPANRVGVVSFTVEGIDSEEVA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489529510 321 FLLDSDYNIATRSGIHCSPLAHTTLGTLKQGAVRFSIGYFNTKDEIDKAVEALKKI 376
Cdd:TIGR01977 321 DILDEKFDIATRTGLHCAPLAHKTIGTFATGTIRLSLGYFNTEEEIEKLLEALSEI 376
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
2-373 |
3.06e-161 |
|
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: 456.93 E-value: 3.06e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 2 IYLDNAATTYPKPERVYnAVLDCMKNYCANPGRAGHKLAMRAAREIYDTRENIAKLFNVSNPMNIVFTSNATDSLNLAIK 81
Cdd:cd06453 1 VYLDNAATSQKPQPVID-AIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 82 GVL---QEGDHVITTSMEHNSVIRPIKAL-EKRGIENTVVKCDYEGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLIDIK 157
Cdd:cd06453 80 GLGranKPGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 158 KVGEIAKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKcLFGPQGTGILYVREGLNLNILKEGGTGSKSEEI---- 233
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHK-MLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVsfee 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 234 VQPELFPDKYESGTHNTPGIAGLNQGILFIFERGINNIRQHEEELCQYMIDKLEEVPDIKIYGpkDSKKRASVIALNIGD 313
Cdd:cd06453 239 TTYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYG--DAEDRAGVVSFNLEG 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 314 MDSGEVTFLLDsDYNIATRSGIHCSPLAHTTLGtlKQGAVRFSIGYFNTKDEIDKAVEAL 373
Cdd:cd06453 317 IHPHDVATILD-QYGIAVRAGHHCAQPLMRRLG--VPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
2-379 |
1.61e-134 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 389.88 E-value: 1.61e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 2 IYLDNAATTyPKPERVYNAVLDCMKNYCANPGRAGHKLAMRAAREIYDTRENIAKLFNVSNPMNIVFTSNATDSLNLAIK 81
Cdd:COG0520 17 VYLDNAATG-QKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAASPDEIIFTRGTTEAINLVAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 82 GV--LQEGDHVITTSMEHNSVIRPIKALEKR-GIENTVVKCDYEGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLIDIKK 158
Cdd:COG0520 96 GLgrLKPGDEILITEMEHHSNIVPWQELAERtGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVNPVKE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 159 VGEIAKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKcLFGPQGTGILYVREGLnLNILK----EGGTGSK-SEEI 233
Cdd:COG0520 176 IAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHK-LYGPTGIGVLYGKREL-LEALPpflgGGGMIEWvSFDG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 234 VQPELFPDKYESGTHNTPGIAGLNQGILFIFERGINNIRQHEEELCQYMIDKLEEVPDIKIYGPKDSKKRASVIALNIGD 313
Cdd:COG0520 254 TTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVRILGPADPEDRSGIVSFNVDG 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489529510 314 MDSGEVTFLLDsDYNIATRSGIHCSPLAHTTLGTlkQGAVRFSIGYFNTKDEIDKAVEALKKISKN 379
Cdd:COG0520 334 VHPHDVAALLD-DEGIAVRAGHHCAQPLMRRLGV--PGTVRASFHLYNTEEEIDRLVEALKKLAEL 396
|
|
| Sec_lyase_SclA |
NF040779 |
selenocysteine lyase SclA; In bacteria, selenocysteine lyase activity (EC 4.4.1.16) usually is ... |
2-376 |
1.69e-130 |
|
selenocysteine lyase SclA; In bacteria, selenocysteine lyase activity (EC 4.4.1.16) usually is seen as a secondary activity of a cysteine desulfurase (EC 2.8.1.7). However, SclA, as studied in Enterococcus faecalis, acts primary on selenocysteine, binding cysteine just as well but acting on cysteine with much lower catalytic efficiency.
Pssm-ID: 468734 [Multi-domain] Cd Length: 378 Bit Score: 379.03 E-value: 1.69e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 2 IYLDNAATTYPKPERVYNAVLDCMK-NYCANPGRAGHklAMRAAREIYDTRENIAKLFNVSNPMNIVFTSNATDSLNLAI 80
Cdd:NF040779 1 VYLNHAATSNHKFEATIQALCAYLQeNNNLNTNRGLQ--GLDELGLAFETRQALADFFHAPDPAHVIFTANATTSLNMVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 81 KGVLQEGDHVITTSMEHNSVIRPIKALE-KRGIENTVVKCDYEGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLIDIKKV 159
Cdd:NF040779 79 NGLLKPGDHVLTTSVEHNAVARPLHLLEtEQNVSVTYLPCEKDGQLDPEQIEAAIRPETKVLVMTHASNVLGTILPVKEC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 160 GEIAKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKCLFGPQGTGILyvreGLNLNILKE------GGTGSKSEEI 233
Cdd:NF040779 159 FKIAKKHGIITVLDSAQTAGFLPIDMEEMSIDVLAFTGHKSLMGLAGIGGF----ALAKNIEKKidpwltGGTGSASLSL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 234 VQPELFPDKYESGTHNTPGIAGLNQGILFIFERGINNIRQHEEELCQYMIDKLEEVPdIKIYGPKDSKKRASVIALNIGD 313
Cdd:NF040779 235 EQPDFLPDKFEPGTPNTLGILSLKSSVKAIQELGLEKIQAHERALTARFLTGLKELP-VTILGTKDAAQSVPVVSITAPG 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489529510 314 MDSGEVTFLLDSDYNIATRSGIHCSPLAHTTLGTLKQGAVRFSIGYFNTKDEIDKAVEALKKI 376
Cdd:NF040779 314 IDSGELAQQLFDRYGIITRSGLHCAPLAHQTAGTLKTGAVRFSFGWNTTAEEIDYTLSALKEI 376
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
2-368 |
1.29e-109 |
|
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: 325.36 E-value: 1.29e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 2 IYLDNAATTyPKPERVYNAVLDCMKNYCANPGRAGHKLAMRAAREIYDTRENIAKLFNVSNPMNIVFTSNATDSLNLAIK 81
Cdd:pfam00266 1 IYLDSAATT-QKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 82 GV---LQEGDHVITTSMEHNSVIRPIKALEKR-GIENTVVKCDYEGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLIDIK 157
Cdd:pfam00266 80 SLgrsLKPGDEIVITEMEHHANLVPWQELAKRtGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 158 KVGEIAKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKcLFGPQGTGILYVREGLnLNILK--EGGTGSKS----E 231
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTGIGVLYGRRDL-LEKMPplLGGGGMIEtvslQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 232 EIVQPELfPDKYESGTHNTPGIAGLNQGILFIFERGINNIRQHEEELCQYMIDKLEEVPDIKIYGPkdsKKRASVIALNI 311
Cdd:pfam00266 238 ESTFADA-PWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGP---ERRASIISFNF 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 489529510 312 GDMDSGEVTFLLDsDYNIATRSGIHCSPLAHTTLGtlKQGAVRFSIGYFNTKDEIDK 368
Cdd:pfam00266 314 KGVHPHDVATLLD-ESGIAVRSGHHCAQPLMVRLG--LGGTVRASFYIYNTQEDVDR 367
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
1-376 |
1.34e-95 |
|
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: 290.03 E-value: 1.34e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 1 MIYLDNAATTYPKPErVYNAVLDCMKNYCANPGrAGHKLAMRAAREIYDTRENIAKLFNVSnPMNIVFTSNATDSLNLAI 80
Cdd:COG1104 3 MIYLDNAATTPVDPE-VLEAMLPYLTEYFGNPS-SLHSFGREARAALEEAREQVAALLGAD-PEEIIFTSGGTEANNLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 81 KGVL----QEGDHVITTSMEHNSVIRPIKALEKRGIENTVVKCDYEGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLIDI 156
Cdd:COG1104 80 KGAArayrKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 157 KKVGEIAKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKcLFGPQGTGILYVREGLNLNILKEGGtgskSEEivqp 236
Cdd:COG1104 160 AEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHK-IYGPKGVGALYVRKGVRLEPLIHGG----GQE---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 237 elfpDKYESGTHNTPGIAGLNQgILFIFERGINNIRQHEEELCQYMIDKL-EEVPDIKIYGPKDskKRASVIaLNIG--D 313
Cdd:COG1104 231 ----RGLRSGTENVPGIVGLGK-AAELAAEELEEEAARLRALRDRLEEGLlAAIPGVVINGDPE--NRLPNT-LNFSfpG 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489529510 314 MDSGEVTFLLDsDYNIATRSGIHCS-----P----LAhttLG---TLKQGAVRFSIGYFNTKDEIDKAVEALKKI 376
Cdd:COG1104 303 VEGEALLLALD-LAGIAVSSGSACSsgslePshvlLA---MGldeELAHGSIRFSLGRFTTEEEIDRAIEALKEI 373
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
2-376 |
6.93e-76 |
|
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: 239.44 E-value: 6.93e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 2 IYLDNAATTYPKPErVYNAVLDCMKNYCANPGrAGHKLAMRAAREIYDTRENIAKLFNVSnPMNIVFTSNATDSLNLAIK 81
Cdd:TIGR03402 1 IYLDNNATTRVDPE-VLEAMLPYFTEYFGNPS-SMHSFGGEVGKAVEEAREQVAKLLGAE-PDEIIFTSGGTESDNTAIK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 82 GVLQ---EGDHVITTSMEHNSVIRPIKALEKRGIENTVVKCDYEGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLIDIKK 158
Cdd:TIGR03402 78 SALAaqpEKRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 159 VGEIAKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKcLFGPQGTGILYVREGLNLNILKEGGTGSKseeivqpel 238
Cdd:TIGR03402 158 IGEIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHK-LHGPKGVGALYIRKGTRFRPLLRGGHQER--------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 239 fpdKYESGTHNTPGIAGLNQGIlfifERGINNIRQHEEELcQYMIDKLEE-----VPDIKIYGPKDskKRASViALNIG- 312
Cdd:TIGR03402 228 ---GRRAGTENVPGIVGLGKAA----ELATEHLEEENTRV-RALRDRLEAgllarIPDARLNGDPT--KRLPN-TVNISf 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489529510 313 DMDSGEVTFLLDSDYNIATRSGIHCSP-------------LAHTTLgtlkQGAVRFSIGYFNTKDEIDKAVEALKKI 376
Cdd:TIGR03402 297 EYIEGEAILLLLDMEGICASSGSACTSgslepshvlramgVPHTAA----HGSIRFSLSRYNTEEDIDYVLEVLPPI 369
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
1-374 |
2.53e-70 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 226.55 E-value: 2.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 1 MIYLDNAATTYpKPERVYNAVLDCMKNYCANPGRAGHKLAMRAAREIYDTRENIAKLFNVSNPMNIVFTSNATDSLNLAI 80
Cdd:PLN02855 33 LVYLDNAATSQ-KPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINASTSREIVFTRNATEAINLVA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 81 K--GV--LQEGDHVITTSMEHNSVIRPIKAL-EKRGIENTVVKCDYEGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLID 155
Cdd:PLN02855 112 YtwGLanLKPGDEVILSVAEHHSNIVPWQLVaQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGSILP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 156 IKKVGEIAKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHK-ClfGPQGTGILYVREGLnLNIL---KEGGtgskse 231
Cdd:PLN02855 192 VEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKmC--GPTGIGFLWGKSDL-LESMppfLGGG------ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 232 EIVQpELF---------PDKYESGthnTPGIA---GLNQGILFIFERGINNIRQHEEELCQYMIDKLEEVPDIKIYGPK- 298
Cdd:PLN02855 263 EMIS-DVFldhstyappPSRFEAG---TPAIGeaiGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRIYGPKp 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489529510 299 -DSKKRASVIALNIGDMDSGEVTFLLDSDYNIATRSGIHCSPLAHTTLGTlkQGAVRFSIGYFNTKDEIDKAVEALK 374
Cdd:PLN02855 339 sEGVGRAALCAFNVEGIHPTDLSTFLDQQHGVAIRSGHHCAQPLHRYLGV--NASARASLYFYNTKEEVDAFIHALK 413
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
1-378 |
2.99e-65 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 212.69 E-value: 2.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 1 MIYLDNAATTyPKPERVYNAVLDCMKNYCANPGRAGHKLAMRAAREIYDTRENIAKLFNVSNPMNIVFTSNATDSLNLAI 80
Cdd:PRK09295 24 LAYLDSAASA-QKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINARSAEELVFVRGTTEGINLVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 81 ----KGVLQEGDHVITTSMEHNSVIRPIKALEKR-GIENTVVKCDYEGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLID 155
Cdd:PRK09295 103 nswgNSNVRAGDNIIISEMEHHANIVPWQMLCARvGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGTENP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 156 IKKVGEIAKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKcLFGPQGTGILYVREGLnLNILK--EGG-----TGS 228
Cdd:PRK09295 183 LAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHK-LYGPTGIGILYVKEAL-LQEMPpwEGGgsmiaTVS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 229 KSEEIVQPELfPDKYESGTHNTPGIAGLNQGILFIFERGINNIRQHEEELCQYMIDKLEEVPDIKIYGPkdsKKRASVIA 308
Cdd:PRK09295 261 LTEGTTWAKA-PWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESVPDLTLYGP---QNRLGVIA 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489529510 309 LNIGDMDSGEVTFLLDsDYNIATRSGIHCS-PL-AHTTLGTLkqgaVRFSIGYFNTKDEIDKAVEALKKISK 378
Cdd:PRK09295 337 FNLGKHHAYDVGSFLD-NYGIAVRTGHHCAmPLmAYYNVPAM----CRASLAMYNTHEEVDRLVAGLQRIHR 403
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
2-367 |
2.79e-58 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 193.33 E-value: 2.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 2 IYLDNAATTyPKPERVYNAVLDCMKNYCANPGRAGHKLAMRAAREIYDTRENIAKLFNvSNPMNIVFTSNATDSLNLAIK 81
Cdd:PLN02651 1 LYLDMQATT-PIDPRVLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIG-ADPKEIIFTSGATESNNLAIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 82 GVLQ----EGDHVITTSMEHNSVIRPIKALEKRGIENTVVKCDYEGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLIDIK 157
Cdd:PLN02651 79 GVMHfykdKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 158 KVGEIAKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKcLFGPQGTGILYVR--EGLNLNILKEGGtGSKSeeivq 235
Cdd:PLN02651 159 EIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHK-IYGPKGVGALYVRrrPRVRLEPLMSGG-GQER----- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 236 pelfpdKYESGTHNTPGIAGLNQGILfIFERGINNIRQHEEELCQYMIDKLEE-VPDIKIYGPKDSKKR-ASVIALNIGD 313
Cdd:PLN02651 232 ------GRRSGTENTPLVVGLGAACE-LAMKEMDYDEKHMKALRERLLNGLRAkLGGVRVNGPRDPEKRyPGTLNLSFAY 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489529510 314 MDSGEvtfLLDSDYNIATRSGIHC-----SP------------LAHTTLgtlkqgavRFSIGYFNTKDEID 367
Cdd:PLN02651 305 VEGES---LLMGLKEVAVSSGSACtsaslEPsyvlralgvpeeMAHGSL--------RLGVGRFTTEEEVD 364
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
2-375 |
2.85e-56 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 189.38 E-value: 2.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 2 IYLDNAATTyPKPERVYNAVLDC--MKNYCANPGRAGHKLAMRAAREIYDTRENIAKLFNvSNPMNIVFTSNATDSLNLA 79
Cdd:PRK14012 5 IYLDYSATT-PVDPRVAEKMMPYltMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLIG-ADPREIVFTSGATESDNLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 80 IKGVLQ----EGDHVITTSMEHNSVIRPIKALEKRGIENTVVKCDYEGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLID 155
Cdd:PRK14012 83 IKGAAHfyqkKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 156 IKKVGEIAKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKcLFGPQGTGILYVREG--LNLNILKEGGTGSKSeei 233
Cdd:PRK14012 163 IAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHK-IYGPKGIGALYVRRKprVRLEAQMHGGGHERG--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 234 vqpelfpdkYESGTHNTPGIAGLnqGILF-IFERGINNIRQHEEELCQYMIDKLEEVPDIKIYGpkDSKKRASVIaLNIG 312
Cdd:PRK14012 239 ---------MRSGTLPTHQIVGM--GEAArIAKEEMATENERIRALRDRLWNGIKDIEEVYLNG--DLEQRVPGN-LNVS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 313 -DMDSGEVtfLLDSDYNIATRSGIHCSP-----------------LAHTtlgtlkqgAVRFSIGYFNTKDEIDKAVEALK 374
Cdd:PRK14012 305 fNYVEGES--LIMALKDLAVSSGSACTSaslepsyvlralglndeLAHS--------SIRFSLGRFTTEEEIDYAIELVR 374
|
.
gi 489529510 375 K 375
Cdd:PRK14012 375 K 375
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
2-373 |
7.33e-50 |
|
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: 172.24 E-value: 7.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 2 IYLDNAATTYpKPERVYNAVLDCMKNYCANPGRAGHKlAMRAAREIYDTRENIAKLFNVSNPmNIVFTSNATD---SLNL 78
Cdd:TIGR01976 19 VFFDNPAGTQ-IPQSVADAVSAALTRSNANRGGAYES-SRRADQVVDDAREAVADLLNADPP-EVVFGANATSltfLLSR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 79 AIKGVLQEGDHVITTSMEHNSVIRP-IKALEKRGIENTVVKCD-YEGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLIDI 156
Cdd:TIGR01976 96 AISRRWGPGDEVIVTRLDHEANISPwLQAAERAGAKVKWARVDeATGELHPDDLASLLSPRTRLVAVTAASNTLGSIVDL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 157 KKVGEIAKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKcLFGPQgTGILYVREGLNLNILkeggtGSKSEEIvqP 236
Cdd:TIGR01976 176 AAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYK-FFGPH-MGILWGRPELLMNLP-----PYKLTFS--Y 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 237 ELFPDKYESGTHNTPGIAGLNQGILFIFERGINN--------------IRQHEEELCQYMIDKLEEVPDIKIYGPKDSKK 302
Cdd:TIGR01976 247 DTGPERFELGTPQYELLAGVVAAVDYLAGLGESAngsrrerlvasfqaIDAYENRLAEYLLVGLSDLPGVTLYGVARLAA 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489529510 303 RASVIALNIGDMDSGEVTFLLdSDYNIATRSGIHCSPLAHTTLG-TLKQGAVRFSIGYFNTKDEIDKAVEAL 373
Cdd:TIGR01976 327 RVPTVSFTVHGLPPQRVVRRL-ADQGIDAWAGHFYAVRLLRRLGlNDEGGVVRVGLAHYNTAEEVDRLLEAL 397
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
1-380 |
3.64e-47 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 164.90 E-value: 3.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 1 MIYLDNAATTyPKPERVYNAVLDCMKNYCANpGRAGHKLAMRAAREIYDTRENIAKLFNvSNPMNIVFTSNATDSLNLAI 80
Cdd:PRK02948 1 MIYLDYAATT-PMSKEALQTYQKAASQYFGN-ESSLHDIGGTASSLLQVCRKTFAEMIG-GEEQGIYFTSGGTESNYLAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 81 KGVLQ----EGDHVITTSMEHNSVIRPIKALEKRGIENTVVKCDYEGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLIDI 156
Cdd:PRK02948 78 QSLLNalpqNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 157 KKVGEIAKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKcLFGPQGTGILYVREGLNLNILKEGGTGSKSeeivqp 236
Cdd:PRK02948 158 AEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHK-IYGPKGVGAVYINPQVRWKPVFPGTTHEKG------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 237 elfpdkYESGTHNTPGIAGLNQGILFIFERgINNIRQHEEELCQYMIDKLEEVP-DIKIYGPKDSkKRASVIALNIGDMD 315
Cdd:PRK02948 231 ------FRPGTVNVPGIAAFLTAAENILKN-MQEESLRFKELRSYFLEQIQTLPlPIEVEGHSTS-CLPHIIGVTIKGIE 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489529510 316 sGEVTFLLDSDYNIATRSGIHCSPLAHTTLGTLK------QGA---VRFSIGYFNTKDEIDKAVEALKKISKNK 380
Cdd:PRK02948 303 -GQYTMLECNRRGIAISTGSACQVGKQEPSKTMLaigktyEEAkqfVRFSFGQQTTKDQIDTTIHALETIGNQF 375
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
2-375 |
1.05e-41 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 150.96 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 2 IYLDNAATTYpKPERVYNAVLDCMKNYCANPGRAGHKLAMRAAREIYDTRENIAKLFNVSNPMNIVFTSNATDSLNLAIK 81
Cdd:PRK10874 21 VYLDSAATAL-KPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNAPDAKNIVWTRGTTESINLVAQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 82 GV----LQEGDHVITTSMEHNSVIRP-IKALEKRGIenTVVK--CDYEGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLI 154
Cdd:PRK10874 100 SYarprLQPGDEIIVSEAEHHANLVPwLMVAQQTGA--KVVKlpLGADRLPDVDLLPELITPRTRILALGQMSNVTGGCP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 155 DIKKVGEIAKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKcLFGPQGTGILYVREGLnLNILKEGGTGSK----- 229
Cdd:PRK10874 178 DLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHK-LYGPTGIGVLYGKSEL-LEAMSPWQGGGKmltev 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 230 SEEIVQPELFPDKYESGTHNTPGIAGLNQGILFIFERGINNIRQHEEELCQYMIDKLEEVPDIKIYGPKDSkkraSVIAL 309
Cdd:PRK10874 256 SFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLPGFRSFRCQDS----SLLAF 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489529510 310 NIGDMDSGEVTFLLdSDYNIATRSGIHCS-PLAhTTLGTlkQGAVRFSIGYFNTKDEIDKAVEALKK 375
Cdd:PRK10874 332 DFAGVHHSDLVTLL-AEYGIALRAGQHCAqPLL-AALGV--TGTLRASFAPYNTQSDVDALVNAVDR 394
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
2-376 |
4.58e-32 |
|
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: 127.28 E-value: 4.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 2 IYLDNAATTYpKPervyNAVLDCMKNYCA----NPGRAGHKLAMRA--AREiyDTRENIAKLFNVSNPMNIVFTSNATDS 75
Cdd:NF041166 247 VWFDNAATTQ-KP----QAVIDRLSYFYEhensNIHRAAHELAARAtdAYE--GAREKVRRFIGAPSVDEIIFVRGTTEA 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 76 LNLAIK--GV--LQEGDHVITTSMEHNSVIRPIKAL-EKRGIENTVVKCDYEGFLDYEDLEKSIKSNTKLIVTTHASNVC 150
Cdd:NF041166 320 INLVAKswGRqnIGAGDEIIVSHLEHHANIVPWQQLaQETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSNAL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 151 GTLIDIKKVGEIAKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKcLFGPQGTGILYVREGLnLNILK--EGG--- 225
Cdd:NF041166 400 GTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHK-VFGPTGIGVVYGKRDL-LEAMPpwQGGgnm 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 226 ----TgskSEEIV-QPElfPDKYESGTHNtpgIA---GLNQGILFIfER-GINNIRQHEEELCQYMIDKLEEVPDIKIYG 296
Cdd:NF041166 478 iadvT---FEKTVyQPA--PNRFEAGTGN---IAdavGLGAALDYV-ERiGIENIARYEHDLLEYATAGLAEVPGLRLIG 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 297 PKDSKkrASVIALNIGDMDSGEVTFLLDSDyNIATRSGIHCsplAHTTL------GTlkqgaVRFSIGYFNTKDEIDKAV 370
Cdd:NF041166 549 TAADK--ASVLSFVLDGYSTEEVGKALNQE-GIAVRSGHHC---AQPILrrfgveAT-----VRPSLAFYNTCEEVDALV 617
|
....*.
gi 489529510 371 EALKKI 376
Cdd:NF041166 618 AVLRRL 623
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
45-376 |
2.01e-22 |
|
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: 97.08 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 45 REIYD-TRENIAKLFNVSNPMnIVFTSNATDSLNLAIKGVLQEGDHVIttsmehnsVI-------RPIKALEKRGIENTV 116
Cdd:COG0075 32 VELMDeVRELLKKVFGTENDV-VILTGSGTGAMEAALANLVSPGDKVL--------VLvngafgeRWAEIAERYGAEVVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 117 VKCDY-EGFlDYEDLEKSIKSNT--KLIVTTHA--SnvCGTLIDIKKVGEIAKKHNILFLVDASQTAGVYDIDVNECNID 191
Cdd:COG0075 103 LEVPWgEAV-DPEEVEEALAADPdiKAVAVVHNetS--TGVLNPLEEIGALAKEHGALLIVDAVSSLGGVPLDMDEWGID 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 192 MLAMPGHKCLFGPQGTGILYVRE------------GLNLNILKEGGTGSKSEeivqpelFPdkyesGTHNTPGIAGLNQG 259
Cdd:COG0075 180 VVVSGSQKCLMLPPGLAFVAVSEraleaiearklpSYYLDLKLWLKYWEKGQ-------TP-----YTPPVSLLYALREA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 260 ILFIFERGINNIRQHEEELCQYMIDKLEEVPdIKIYGPKDSkkRA-SVIALNIGD-MDSGEVTFLLDSDYNIATRSGihc 337
Cdd:COG0075 248 LDLILEEGLENRFARHRRLAEALRAGLEALG-LELFAEEEY--RSpTVTAVRVPEgVDAAALRKRLKERYGIEIAGG--- 321
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489529510 338 splahttLGTLKQGAVRFS-IGYfNTKDEIDKAVEALKKI 376
Cdd:COG0075 322 -------LGPLKGKIFRIGhMGY-VNPEDVLRTLAALEEA 353
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
47-213 |
8.16e-19 |
|
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: 82.82 E-value: 8.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 47 IYDTRENIAKLFNVSNPmNIVFTSNATDSLNLAIKGVLQEGDHVITTSMEHNSVIRPIKALEKRGIENTVVKCDYEGFLD 126
Cdd:cd01494 2 LEELEEKLARLLQPGND-KAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYWVAAELAGAKPVPVPVDDAGYGGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 127 YEDLEKSIKS-NTKLIVTTHASNVCGTLIDIKKVGEIAKKHNILFLVDASQTAG-----VYDIDVNECniDMLAMPGHKc 200
Cdd:cd01494 81 VAILEELKAKpNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGaspapGVLIPEGGA--DVVTFSLHK- 157
|
170
....*....|...
gi 489529510 201 LFGPQGTGILYVR 213
Cdd:cd01494 158 NLGGEGGGVVIVK 170
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
49-288 |
3.17e-17 |
|
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: 81.95 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 49 DTRENIAKLFNVSNPMNIVFTSNATDSLNLAIKGVLQEGDHVITTSMEHNSViRPIKALEKRGIENTVVKCDYEGFLDYE 128
Cdd:cd06451 36 EILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVGVNGVFGD-RWADMAERYGADVDVVEKPWGEAVSPE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 129 DLEKSIKSNTKLIVT-THASNVCGTLIDIKKVGEIAKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKCLFGPQGT 207
Cdd:cd06451 115 EIAEALEQHDIKAVTlTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 208 GILYV-REGLNLNILKEGGTGS--KSEEIVQpelFPDKYESgTHNTPGIA---GLNQGILFIFERGINN-IRQHeEELCQ 280
Cdd:cd06451 195 GPIAFsERALERIKKKTKPKGFyfDLLLLLK---YWGEGYS-YPHTPPVNllyALREALDLILEEGLENrWARH-RRLAK 269
|
....*...
gi 489529510 281 YMIDKLEE 288
Cdd:cd06451 270 ALREGLEA 277
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
51-375 |
1.62e-15 |
|
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: 77.00 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 51 RENIAKLFNVSN-----PMNIVFTSNATDSLNLAIKGVLQEGDHVITTS---MEHNSVIRpikaleKRGIENTVVKCDYE 122
Cdd:cd00609 42 REAIAEWLGRRGgvdvpPEEIVVTNGAQEALSLLLRALLNPGDEVLVPDptyPGYEAAAR------LAGAEVVPVPLDEE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 123 G--FLDYEDLEKSIKSNTKLIVTTHASNVCGTLID---IKKVGEIAKKHNILFLVDasqtagvydidvnECNIDmLAMPG 197
Cdd:cd00609 116 GgfLLDLELLEAAKTPKTKLLYLNNPNNPTGAVLSeeeLEELAELAKKHGILIISD-------------EAYAE-LVYDG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 198 HK---CLFGPQGTGILYVReglnlnilkeggTGSKS---------------EEIVqpELFPDKYESGTHNTPGIAglnQG 259
Cdd:cd00609 182 EPppaLALLDAYERVIVLR------------SFSKTfglpglrigyliappEELL--ERLKKLLPYTTSGPSTLS---QA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 260 ILFIFERG----INNIRQHEEELCQYMIDKLEEVPDIKIYGPKDskkrASVIALNIGDMDSGE-VTFLLDsDYNIATRSG 334
Cdd:cd00609 245 AAAAALDDgeehLEELRERYRRRRDALLEALKELGPLVVVKPSG----GFFLWLDLPEGDDEEfLERLLL-EAGVVVRPG 319
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 489529510 335 ihcsplahTTLGTLKQGAVRFSIGyfNTKDEIDKAVEALKK 375
Cdd:cd00609 320 --------SAFGEGGEGFVRLSFA--TPEEELEEALERLAE 350
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
51-173 |
3.69e-12 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 66.88 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 51 RENIAKLFNVSNPMNIVFTSNATDSLNLAIKGVLQEGDHVIT---TSMEHNSVIRPIKAlekrgienTVvkcDY------ 121
Cdd:PRK07324 68 KEAVASLYQNVKPENILQTNGATGANFLVLYALVEPGDHVISvypTYQQLYDIPESLGA--------EV---DYwqlkee 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 489529510 122 EGFL-DYEDLEKSIKSNTKLIVTTHASNVCGTLID---IKKVGEIAKKHNILFLVD 173
Cdd:PRK07324 137 NGWLpDLDELRRLVRPNTKLICINNANNPTGALMDrayLEEIVEIARSVDAYVLSD 192
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
52-179 |
6.00e-11 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 63.16 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 52 ENIAKLFNVSNpmnIVFTSNATDSLNLAIKGV-LQEGDHVITTSMEH----NSVI----RPIkalekrgientVVKCDYE 122
Cdd:COG0399 37 EEFAAYLGVKH---AVAVSSGTAALHLALRALgIGPGDEVITPAFTFvataNAILyvgaTPV-----------FVDIDPD 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489529510 123 GF-LDYEDLEKSIKSNTKLIVTTHasnVCGTLIDIKKVGEIAKKHNILFLVDASQTAG 179
Cdd:COG0399 103 TYnIDPEALEAAITPRTKAIIPVH---LYGQPADMDAIMAIAKKHGLKVIEDAAQALG 157
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
51-373 |
1.59e-10 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 61.94 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 51 RENIAKLFNVSNPM------NIVFTSNATDSLNLAIKGVLQEGDHVITTSMEHNSVIRPIKAlekRGIENTVVKCDYE-- 122
Cdd:pfam00155 45 REALAKFLGRSPVLkldreaAVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARL---AGGEVVRYPLYDSnd 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 123 GFLDYEDLEKSIKSNTKLIVTTHASNVCGTLI---DIKKVGEIAKKHNILFLVDASQTAGVYDIDVNECNIDmLAMPGHK 199
Cdd:pfam00155 122 FHLDFDALEAALKEKPKVVLHTSPHNPTGTVAtleELEKLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRA-LLAEGPN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 200 CL--------FGPQG--TGILYVREGLnLNILKEGGTGSKSEEIVQPELfpdkyesgthntpgIAGLNQGILFIFErgIN 269
Cdd:pfam00155 201 LLvvgsfskaFGLAGwrVGYILGNAAV-ISQLRKLARPFYSSTHLQAAA--------------AAALSDPLLVASE--LE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 270 NIRQHEEELCQYMIDKLEEVpDIKIYGPKdskkrASVIALNIGDMDSGEVTFlldsdYNIATRSGIHCSPLAHTTLgtlk 349
Cdd:pfam00155 264 EMRQRIKERRDYLRDGLQAA-GLSVLPSQ-----AGFFLLTGLDPETAKELA-----QVLLEEVGVYVTPGSSPGV---- 328
|
330 340
....*....|....*....|....
gi 489529510 350 QGAVRFSIGYFnTKDEIDKAVEAL 373
Cdd:pfam00155 329 PGWLRITVAGG-TEEELEELLEAI 351
|
|
| Cys_Met_Meta_PP |
pfam01053 |
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and ... |
52-181 |
1.63e-10 |
|
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and methionine metabolism. The following are members: Cystathionine gamma-lyase, Cystathionine gamma-synthase, Cystathionine beta-lyase, Methionine gamma-lyase, OAH/OAS sulfhydrylase, O-succinylhomoserine sulfhydrylase All of these members participate is slightly different reactions. All these enzymes use PLP (pyridoxal-5'-phosphate) as a cofactor.
Pssm-ID: 395837 [Multi-domain] Cd Length: 376 Bit Score: 61.87 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 52 ENIAKLFNVSNpmnIVFTSNATDSLNLAIKGVLQEGDHVITTSMEHNSVIRPIKALEKR-GIENTVVKCDyegflDYEDL 130
Cdd:pfam01053 54 ERIAALEGGAA---ALAFSSGMAAITAAILALLKAGDHIVATDDLYGGTYRLFNKVLPRfGIEVTFVDTS-----DPEDL 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489529510 131 EKSIKSNTKLIVTTHASNVCGTLIDIKKVGEIAKKHNILFLVDASQTAGVY 181
Cdd:pfam01053 126 EAAIKPNTKAVYLETPTNPLLKVVDIEAIAKLAKKHGILVVVDNTFASPYL 176
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
2-375 |
3.45e-10 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 61.81 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 2 IYLDNAATTYPKPERVYNAVLDCMKNYCANPgRAGHKLAMRAAREIYDTRENIAKLFNVS-NPMNIVFTSNATDSLNLAI 80
Cdd:PLN02724 36 VYLDHAGATLYSESQLEAALADFSSNVYGNP-HSQSDSSMRSSDTIESARQQVLEYFNAPpSDYACVFTSGATAALKLVG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 81 KGV-LQEGDHVITTSMEHNSV--IRPIkALEKRGIENTVvkcdyegflDYEDLEKSIKSNTKLIVTTHAS---------- 147
Cdd:PLN02724 115 ETFpWSSESHFCYTLENHNSVlgIREY-ALEKGAAAIAV---------DIEEAANQPTNSQGSVVVKSRGlqrrntsklq 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 148 ------------------NVCGTLIDIKKVGEI--------AKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKcL 201
Cdd:PLN02724 185 kreddgeaynlfafpsecNFSGAKFPLDLVKLIkdnqhsnfSKSGRWMVLLDAAKGCGTSPPDLSRYPADFVVVSFYK-I 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 202 FG-PQGTGILYVREGLNlNILKE----GGTGSKS----EEIVQPELFPDKYESGTHNTPGIAGLNQGILFIFERGINNIR 272
Cdd:PLN02724 264 FGyPTGLGALLVRRDAA-KLLKKkyfgGGTVAASiadiDFVKRRERVEQRFEDGTISFLSIAALRHGFKLLNRLTISAIA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 273 QHEEELCQYMIDKLE------EVPDIKIYGPKDSK----KRASVIALNIGDMDSGEVTFL----LDSDYNIATRSGIHCS 338
Cdd:PLN02724 343 MHTWALTHYVANSLRnlkhgnGAPVCVLYGNHTFKlefhIQGPIVTFNLKRADGSWVGHRevekLASLSGIQLRTGCFCN 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489529510 339 P--------LAHTTL------GTL-----------KQGAVRFSIGYFNTKDEIDKAVEALKK 375
Cdd:PLN02724 423 PgacakylgLSHKDLqanfeaGHVcwddqdvihgrPTGAVRVSFGYMSTFEDCQKFIDFIIS 484
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
47-214 |
4.20e-10 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 60.71 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 47 IYDTRENIAKLFNvsnpMNIV-FTSNATDSLNLAIKGVLQEGDHVITTSMEH-NSVIrpikALEKRGIEntVVKCDYEGF 124
Cdd:PRK09331 65 IADFHEDLAEFLG----MDEArVTHGAREGKFAVMHSLCKKGDYVVLDGLAHyTSYV----AAERAGLN--VREVPKTGY 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 125 LDY-----------EDLEKSIKSNTKLIVTTHASNVCGTLIDIKKVGEIAKKHNILFLVDASQTAGVYDIDVNECNIDML 193
Cdd:PRK09331 135 PEYkitpeayaekiEEVKEETGKPPALALLTHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFI 214
|
170 180
....*....|....*....|.
gi 489529510 194 AMPGHKCLFGPQGTGILYVRE 214
Cdd:PRK09331 215 VGSGHKSMAASAPSGVLATTE 235
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
52-278 |
1.53e-09 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 59.00 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 52 ENIAKLFNVSNPMNIVFTSNATDSLNLAIKGVLQEGDHVITTSMEHNSViRPIKALEKRGIENTVVKCDYEGFLDYEDLE 131
Cdd:PLN02409 49 EDVKYIFKTKSGTPFIFPTTGTGAWESALTNTLSPGDKVVSFRIGQFSL-LWIDQMQRLNFDVDVVESPWGQGADLDILK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 132 KSIKSNT----KLIVTTHASNVCGTLIDIKKVGEI--AKKHNILFLVDASQTAGVYDIDVNECNIDMLAMPGHKCLFGPQ 205
Cdd:PLN02409 128 SKLRQDTnhkiKAVCVVHNETSTGVTNDLAGVRKLldCAQHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 206 GTGILYVREGLnLNILKEggtgSKSeeivqPELFPDK------YESGTHN--TPGIA---GLNQGILFIFERGINNIRQH 274
Cdd:PLN02409 208 GLGIVCASPKA-LEASKT----AKS-----PRVFFDWadylkfYKLGTYWpyTPSIQllyGLRAALDLIFEEGLENVIAR 277
|
....
gi 489529510 275 EEEL 278
Cdd:PLN02409 278 HARL 281
|
|
| PRK07671 |
PRK07671 |
bifunctional cystathionine gamma-lyase/homocysteine desulfhydrase; |
79-173 |
2.06e-09 |
|
bifunctional cystathionine gamma-lyase/homocysteine desulfhydrase;
Pssm-ID: 181076 [Multi-domain] Cd Length: 377 Bit Score: 58.58 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 79 AIKGVLQEGDHVITTSMEHNSVIRPI-KALEKRGIENTVVKCDyegflDYEDLEKSIKSNTKLIVTTHASNVCGTLIDIK 157
Cdd:PRK07671 80 AVMMLFSSGDHVILTDDVYGGTYRVMtKVLNRFGIEHTFVDTS-----NLEEVEEAIRPNTKAIYVETPTNPLLKITDIK 154
|
90
....*....|....*.
gi 489529510 158 KVGEIAKKHNILFLVD 173
Cdd:PRK07671 155 KISTIAKEKGLLTIVD 170
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
47-298 |
2.24e-09 |
|
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: 58.56 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 47 IYDTRENIAKLFNvsnpMNIV-FTSNATDSLNLAIKGVLQEGDHVITTSMEH-NSVIrpikALEKRGIEntVVKCDYEGF 124
Cdd:cd06452 46 IKDFHHDLAEFLG----MDEArVTPGAREGKFAVMHSLCEKGDWVVVDGLAHyTSYV----AAERAGLN--VREVPNTGH 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 125 LDY-----------EDLEKSIKSNTKLIVTTHASNVCGTLIDIKKVGEIAKKHNILFLVDASQTAGVYDIDVNECNIDML 193
Cdd:cd06452 116 PEYhitpegyaeviEEVKDEFGKPPALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 194 AMPGHKCLFGPQGTGILYVREGLNLNILKeggtGSKSEEIVQPELFpdkyeSGTHNTPGIAGLNQGILFIFERginnIRQ 273
Cdd:cd06452 196 VGSGHKSMAASAPIGVLATTEEWADIVFR----TSQMFKIKEVELL-----GCTLRGAPLVTLMASFPHVKER----VKR 262
|
250 260
....*....|....*....|....*..
gi 489529510 274 HEEEL--CQYMIDKLEEVPDIKIYGPK 298
Cdd:cd06452 263 WDEEVekARWFVAELEKIEGIKQLGEK 289
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
52-180 |
3.79e-09 |
|
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.
Pssm-ID: 99740 [Multi-domain] Cd Length: 352 Bit Score: 57.55 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 52 ENIAKLFNVSNpmnIVFTSNATDSLNLAIK--GVlQEGDHVITTSMEH----NSVIRpikalekRGIenTVVKCDYE--- 122
Cdd:cd00616 25 KAFAEYLGVKY---AVAVSSGTAALHLALRalGI-GPGDEVIVPSFTFvataNAILL-------LGA--TPVFVDIDpdt 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489529510 123 GFLDYEDLEKSIKSNTKLIVTTH-ASNVCgtliDIKKVGEIAKKHNILFLVDASQTAGV 180
Cdd:cd00616 92 YNIDPELIEAAITPRTKAIIPVHlYGNPA----DMDAIMAIAKRHGLPVIEDAAQALGA 146
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
52-376 |
4.05e-09 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 57.57 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 52 ENIAKLFNVsnPMNIVFTS--NATDSLnlaIKGVLQEGDHVITTSMEHNSVIRpikalekrGIENTvvKCDYEGF--LDY 127
Cdd:cd06454 53 EELAEFHGK--EAALVFSSgyAANDGV---LSTLAGKGDLIISDSLNHASIID--------GIRLS--GAKKRIFkhNDM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 128 EDLEKSIKSNT-----KLIVTTHASNVCGTLIDIKKVGEIAKKHNILFLVDASQTAGVYdidvnecnidmlampghkclf 202
Cdd:cd06454 118 EDLEKLLREARrpygkKLIVTEGVYSMDGDIAPLPELVDLAKKYGAILFVDEAHSVGVY--------------------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 203 GPQGTGILYvREGLNLNILKEGGTGSK-----------SEEIVQ-------PELFpdkyesGTHNTPGIAGLNQGILFIF 264
Cdd:cd06454 177 GPHGRGVEE-FGGLTDDVDIIMGTLGKafgavggyiagSKELIDylrsyarGFIF------STSLPPAVAAAALAALEVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 265 ERGInNIRQHEEELCQYMIDKLEEVpDIKIYGPKDskkraSVIALNIGDMDSGEVTF---LLDsdyniatrSGIHCSPLA 341
Cdd:cd06454 250 QGGP-ERRERLQENVRYLRRGLKEL-GFPVGGSPS-----HIIPPLIGDDPAKAVAFsdaLLE--------RGIYVQAIR 314
|
330 340 350
....*....|....*....|....*....|....*
gi 489529510 342 HTTlGTLKQGAVRFSIGYFNTKDEIDKAVEALKKI 376
Cdd:cd06454 315 YPT-VPRGTARLRISLSAAHTKEDIDRLLEALKEV 348
|
|
| MetC |
COG0626 |
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ... |
72-173 |
1.15e-08 |
|
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; Cystathionine beta-lyase/cystathionine gamma-synthase is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440391 [Multi-domain] Cd Length: 389 Bit Score: 56.21 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 72 ATDSLNLAikgVLQEGDHVIttsmehnsVIRPI---------KALEKRGIENTVVkcdyeGFLDYEDLEKSIKSNTKLIV 142
Cdd:COG0626 85 AISAVLLA---LLKAGDHVV--------ASDDLyggtrrlldKVLARFGIEVTFV-----DPTDLAAVEAAIRPNTKLVF 148
|
90 100 110
....*....|....*....|....*....|.
gi 489529510 143 TTHASNVCGTLIDIKKVGEIAKKHNILFLVD 173
Cdd:COG0626 149 LETPSNPTLEVVDIAAIAAIAHAAGALLVVD 179
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
51-173 |
5.82e-08 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 53.98 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 51 RENIAKLFNVSN-----PMNIVFTSNATDSLNLAIKGVLQEGDHVIttsmehnsVIRP--------IKALEKRGIEntvV 117
Cdd:PRK05764 74 REAIAAKLKRDNgldydPSQVIVTTGAKQALYNAFMALLDPGDEVI--------IPAPywvsypemVKLAGGVPVF---V 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489529510 118 KCDYE-GF-LDYEDLEKSIKSNTKLIVTTHASNVCGTLI---DIKKVGEIAKKHNILFLVD 173
Cdd:PRK05764 143 PTGEEnGFkLTVEQLEAAITPKTKALILNSPSNPTGAVYspeELEAIADVAVEHDIWVLSD 203
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
84-175 |
7.33e-08 |
|
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 53.75 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 84 LQEGDHVITTSMEHNSVIRPIKALEKR-GIENTVVKCDyegflDYEDLEKSIKSNTKLIVTTHASNVCGTLIDIKKVGEI 162
Cdd:cd00614 76 LKAGDHVVASDDLYGGTYRLFERLLPKlGIEVTFVDPD-----DPEALEAAIKPETKLVYVESPTNPTLKVVDIEAIAEL 150
|
90
....*....|...
gi 489529510 163 AKKHNILFLVDAS 175
Cdd:cd00614 151 AHEHGALLVVDNT 163
|
|
| PRK06225 |
PRK06225 |
pyridoxal phosphate-dependent aminotransferase; |
1-173 |
8.27e-08 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235749 [Multi-domain] Cd Length: 380 Bit Score: 53.60 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 1 MIYLDNAATTYPKPERVYNAVLDCMK--NYCANPgragHKLAMRAAREIydtrenIAKLFNVsNPMNIVFTSNATDSLNL 78
Cdd:PRK06225 30 MIWMGQNTNHLGPHEEVREAMIRCIEegEYCKYP----PPEGFPELREL------ILKDLGL-DDDEALITAGATESLYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 79 AIKGVLQEGDHVITT-----------SMEHNSVIR-PIKALEkrgientvvkCDYEgfLDYEDLEKSIKSNTKLIVTTHA 146
Cdd:PRK06225 99 VMRAFLSPGDNAVTPdpgyliidnfaSRFGAEVIEvPIYSEE----------CNYK--LTPELVKENMDENTRLIYLIDP 166
|
170 180 190
....*....|....*....|....*....|
gi 489529510 147 SNVCG---TLIDIKKVGEIAKKHNILFLVD 173
Cdd:PRK06225 167 LNPLGssyTEEEIKEFAEIARDNDAFLLHD 196
|
|
| PRK06176 |
PRK06176 |
cystathionine gamma-synthase; |
79-173 |
1.60e-07 |
|
cystathionine gamma-synthase;
Pssm-ID: 180443 [Multi-domain] Cd Length: 380 Bit Score: 52.59 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 79 AIKGVLQEGDHVITTSMEHNSVIRPI-KALEKRGIENTVVKCDyegflDYEDLEKSIKSNTKLIVTTHASNVCGTLIDIK 157
Cdd:PRK06176 80 AVFSLFQSGDHVLLGDDVYGGTFRLFdKVLVKNGLSCTIIDTS-----DLSQIKKAIKPNTKALYLETPSNPLLKITDLA 154
|
90
....*....|....*.
gi 489529510 158 KVGEIAKKHNILFLVD 173
Cdd:PRK06176 155 QCASVAKDHGLLTIVD 170
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
118-256 |
5.03e-07 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 51.52 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 118 KCDYEGFLDYEDLEKSIKS-NTKLIVtthasnvCGT-----LIDIKKVGEIAKKHNILFLVDASQTAG-----VYDIDVN 186
Cdd:PTZ00094 162 QVNEKGLIDYDKLEELAKAfRPKLII-------AGAsayprDIDYKRFREICDSVGAYLMADIAHTSGlvaagVLPSPFP 234
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 187 ECNIDMLAMpgHKCLFGPQGtGILYVREGLNLNIlkeggtGSKSEEIVQPELfpdkyESGTHNTPgIAGL 256
Cdd:PTZ00094 235 YADVVTTTT--HKSLRGPRS-GLIFYRKKVKPDI------ENKINEAVFPGL-----QGGPHNHQ-IAAI 289
|
|
| PRK08247 |
PRK08247 |
methionine biosynthesis PLP-dependent protein; |
79-173 |
7.88e-07 |
|
methionine biosynthesis PLP-dependent protein;
Pssm-ID: 181320 [Multi-domain] Cd Length: 366 Bit Score: 50.47 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 79 AIKGVL---QEGDHVITTSMEHNSVIRpikaLEKRGIENTVVKCDYEGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLID 155
Cdd:PRK08247 79 AIQLVMslfRSGDELIVSSDLYGGTYR----LFEEHWKKWNVRFVYVNTASLKAIEQAITPNTKAIFIETPTNPLMQETD 154
|
90
....*....|....*...
gi 489529510 156 IKKVGEIAKKHNILFLVD 173
Cdd:PRK08247 155 IAAIAKIAKKHGLLLIVD 172
|
|
| PRK08133 |
PRK08133 |
O-succinylhomoserine sulfhydrylase; Validated |
82-173 |
1.18e-06 |
|
O-succinylhomoserine sulfhydrylase; Validated
Pssm-ID: 181244 [Multi-domain] Cd Length: 390 Bit Score: 50.00 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 82 GVLQEGDHVI-TTSMEHNSVIRPIKALEKRGIENTVVkcdyeGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLIDIKKVG 160
Cdd:PRK08133 95 ALLQAGDHVVsSRSLFGSTVSLFEKIFARFGIETTFV-----DLTDLDAWRAAVRPNTKLFFLETPSNPLTELADIAALA 169
|
90
....*....|...
gi 489529510 161 EIAKKHNILFLVD 173
Cdd:PRK08133 170 EIAHAAGALLVVD 182
|
|
| PRK06767 |
PRK06767 |
methionine gamma-lyase; Provisional |
82-173 |
3.65e-06 |
|
methionine gamma-lyase; Provisional
Pssm-ID: 180685 [Multi-domain] Cd Length: 386 Bit Score: 48.68 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 82 GVLQEGDHVITTSMEHNSVIRPIKALEkrgiENTVVKCDYEGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLIDIKKVGE 161
Cdd:PRK06767 95 GFLKAGDHIICSNGLYGCTYGFLEVLE----EKFMITHSFCDMETEADIENKIRPNTKLIFVETPINPTMKLIDLKQVIR 170
|
90
....*....|..
gi 489529510 162 IAKKHNILFLVD 173
Cdd:PRK06767 171 VAKRNGLLVIVD 182
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
62-173 |
2.01e-05 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 46.38 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 62 NPMNIVFTSNATDSLNLAIKGVLQEGDHVI------------TTSMehNSVIRPIKAlekrGIENtvvkcdyeGFL--DY 127
Cdd:PRK07568 87 EPDEILITNGGSEAILFAMMAICDPGDEILvpepfyanyngfATSA--GVKIVPVTT----KIEE--------GFHlpSK 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489529510 128 EDLEKSIKSNTKLIVTTHASNVCGTLI---DIKKVGEIAKKHNILFLVD 173
Cdd:PRK07568 153 EEIEKLITPKTKAILISNPGNPTGVVYtkeELEMLAEIAKKHDLFLISD 201
|
|
| PRK08361 |
PRK08361 |
aspartate aminotransferase; Provisional |
47-182 |
3.53e-05 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 236248 [Multi-domain] Cd Length: 391 Bit Score: 45.64 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 47 IYDTRENIA----KLFNVS-NPMNIVFTSNATDSLNLAIKGVLQEGDHVITTSMEHNSVIRPIKALEKrGIENTVVKCDY 121
Cdd:PRK08361 72 IPELREAIAeyykKFYGVDvDVDNVIVTAGAYEATYLAFESLLEEGDEVIIPDPAFVCYVEDAKIAEA-KPIRIPLREEN 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489529510 122 EGFLDYEDLEKSIKSNTKLIVTTHASNVCGTLID---IKKVGEIAKKHNILFLVDASQTAGVYD 182
Cdd:PRK08361 151 EFQPDPDELLELITKRTRMIVINYPNNPTGATLDkevAKAIADIAEDYNIYILSDEPYEHFLYE 214
|
|
| PRK07811 |
PRK07811 |
cystathionine gamma-synthase; Provisional |
72-173 |
4.75e-05 |
|
cystathionine gamma-synthase; Provisional
Pssm-ID: 236104 [Multi-domain] Cd Length: 388 Bit Score: 45.02 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 72 ATDSLnlaIKGVLQEGDHVITTSMEHNSVIRPI-KALEKRGIENTVVKCDyegflDYEDLEKSIKSNTKLIVTTHASNVC 150
Cdd:PRK07811 88 ATDCL---LRAVLRPGDHIVIPNDAYGGTFRLIdKVFTRWGVEYTPVDLS-----DLDAVRAAITPRTKLIWVETPTNPL 159
|
90 100
....*....|....*....|...
gi 489529510 151 GTLIDIKKVGEIAKKHNILFLVD 173
Cdd:PRK07811 160 LSITDIAALAELAHDAGAKVVVD 182
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
66-210 |
6.01e-05 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 44.51 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 66 IVFTSNATDSLNLAIKGVLQEGDHVITTSMEHnsvirpIKALEKRGIE--NTV----VKCDYEGFLDYEDLEKSIK---- 135
Cdd:pfam01212 50 ALFVPSGTAANQLALMAHCQRGDEVICGEPAH------IHFDETGGHAelGGVqprpLDGDEAGNMDLEDLEAAIRevga 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 136 ---SNTKLIVTTHASNVCG----TLIDIKKVGEIAKKHNILFLVDA---SQTAGVYDIDVNEC--NIDMLAMPGHKCLFG 203
Cdd:pfam01212 124 difPPTGLISLENTHNSAGgqvvSLENLREIAALAREHGIPVHLDGarfANAAVALGVIVKEItsYADSVTMCLSKGLGA 203
|
....*..
gi 489529510 204 PQGtGIL 210
Cdd:pfam01212 204 PVG-SVL 209
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
67-376 |
8.13e-05 |
|
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: 44.12 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 67 VFTSNATDSLNLAI------------KGVLQEGDH-VITTSMEHNSVIRpiKALEKRGIENTVVKCDYEGFLDYEDLEKS 133
Cdd:cd06450 61 VFTSGGSESNLLALlaardrarkrlkAGGGRGIDKlVIVCSDQAHVSVE--KAAAYLDVKVRLVPVDEDGRMDPEALEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 134 I------KSNTKLIVTTHASNVCGTLIDIKKVGEIAKKHNILFLVDA--------SQTAGVYD--ID-VNECNIDmlamp 196
Cdd:cd06450 139 IdedkaeGLNPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAayggfllpFPEPRHLDfgIErVDSISVD----- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 197 GHKCLFGPQGTGILYVReglnlnILKeggtgskseeivqpelfpdkyesgthntpgiaglnqgILFIFER-GINNIRQHE 275
Cdd:cd06450 214 PHKYGLVPLGCSAVLVR------ALK-------------------------------------LWATLRRfGRDGYGEHI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 276 EELCQ---YMIDKLEEVPDIKIYGPKDskkrASVIALN-IGDMDSGEVTF-LLDSdynIATRSGIHcspLAHTTLGtlKQ 350
Cdd:cd06450 251 DRIVDlakYLAELIRADPGFELLGEPN----LSLVCFRlKPSVKLDELNYdLSDR---LNERGGWH---VPATTLG--GP 318
|
330 340
....*....|....*....|....*..
gi 489529510 351 GAVRFSI-GYFNTKDEIDKAVEALKKI 376
Cdd:cd06450 319 NVLRFVVtNPLTTRDDADALLEDIERA 345
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
12-142 |
1.23e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 43.64 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 12 PKPERVYNAVLDCMKN-------YCANPGraghklamraareIYDTRENIAKL----FNVS-NPMNIVFTSNATDSLNLA 79
Cdd:PRK06836 46 PPPAAVKEALRELAEEedpglhgYMPNAG-------------YPEVREAIAESlnrrFGTPlTADHIVMTCGAAGALNVA 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489529510 80 IKGVLQEGDHVITTS---MEHNSVIrpikalEKRGIENTVVKCDYEGF-LDYEDLEKSIKSNTKLIV 142
Cdd:PRK06836 113 LKAILNPGDEVIVFApyfVEYRFYV------DNHGGKLVVVPTDTDTFqPDLDALEAAITPKTKAVI 173
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
123-256 |
2.35e-04 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 42.81 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 123 GFLDYEDLEKSIKS-NTKLIVtthasnvCGT-----LIDIKKVGEIAKKHNILFLVDASQ-----TAGVYDIDVNECniD 191
Cdd:pfam00464 154 GYIDYDQLEKNAKLfRPKLIV-------AGTsaysrLIDYARFREIADEVGAYLMVDMAHisglvAAGVIPSPFPYA--D 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489529510 192 MLAMPGHKCLFGPQGTGILYvREGLNLNILKEGGTGSKSEEIVQPELFPDkYESGTHNTPgIAGL 256
Cdd:pfam00464 225 VVTTTTHKTLRGPRGGMIFY-RKGVKSVDKTGKEILYELEKKINSAVFPG-LQGGPHNHV-IAAK 286
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
106-174 |
4.56e-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: 41.83 E-value: 4.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489529510 106 ALEKRGIENTVVKCDYEGFLDYEDLEKSIKSNT-KLIVTThaSNVCGTLID-IKKVGEIAKKHNILFLVDA 174
Cdd:cd00613 128 RGEPLGIEVVEVPSDEGGTVDLEALKEEVSEEVaALMVQY--PNTLGVFEDlIKEIADIAHSAGALVYVDG 196
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
102-214 |
6.18e-04 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 41.44 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 102 RPIKALEKRGIENTVVKCDYEGFLDYEDLEKSIKSNTKLivtTHASNV-C----GTLIDIKKVGEIAKKHNILFLVDASQ 176
Cdd:PRK13479 94 RIAQIAEYLGIAHVVLDTGEDEPPDAAEVEAALAADPRI---THVALVhCetttGILNPLDEIAAVAKRHGKRLIVDAMS 170
|
90 100 110
....*....|....*....|....*....|....*...
gi 489529510 177 TAGVYDIDVNECNIDMLAMPGHKCLFGPQGTGILYVRE 214
Cdd:PRK13479 171 SFGAIPIDIAELGIDALISSANKCIEGVPGFGFVIARR 208
|
|
| tyr_amTase_E |
TIGR01264 |
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found ... |
51-173 |
8.77e-04 |
|
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found in animals and Trypanosoma cruzi. It is the first enzyme of a pathway of tyrosine degradation via homogentisate. Several plant enzyme designated as probable tyrosine aminotransferases are very closely related to an experimentally demonstrated nicotianamine aminotransferase, an enzyme in a siderophore (iron uptake chelator) biosynthesis pathway. These plant sequences are excluded from the model seed and score between the trusted an noise cutoffs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273529 [Multi-domain] Cd Length: 401 Bit Score: 40.92 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 51 RENIAKLF-NVSNPM---NIVFTSNATDSLNLAIKGVLQEGDHVIttsmehnsVIRPIKAL-----EKRGIENTVVKC-- 119
Cdd:TIGR01264 79 REAIASYYhNPDGPIeadDVVLCSGCSHAIEMCIAALANAGQNIL--------VPRPGFPLyetlaESMGIEVKLYNLlp 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489529510 120 --DYEGFLDYedLEKSIKSNTKLIVTTHASNVCGTLIDIKKVGEI---AKKHNILFLVD 173
Cdd:TIGR01264 151 dkSWEIDLKQ--LESLIDEKTAALIVNNPSNPCGSVFSRQHLEEIlavAERQCLPIIAD 207
|
|
| PRK07504 |
PRK07504 |
O-succinylhomoserine sulfhydrylase; Reviewed |
79-173 |
1.02e-03 |
|
O-succinylhomoserine sulfhydrylase; Reviewed
Pssm-ID: 168979 [Multi-domain] Cd Length: 398 Bit Score: 40.89 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 79 AIKGVLQEGDHVITTSMEHNSVIRPIKALEKR-GIENTVVkcdyEGfLDYEDLEKSIKSNTKLIVTTHASNVCGTLIDIK 157
Cdd:PRK07504 96 AILCQVKAGDHVVAARALFGSCRYVVETLLPRyGIESTLV----DG-LDLDNWEKAVRPNTKVFFLESPTNPTLEVIDIA 170
|
90
....*....|....*.
gi 489529510 158 KVGEIAKKHNILFLVD 173
Cdd:PRK07504 171 AVAKIANQAGAKLVVD 186
|
|
| PRK06234 |
PRK06234 |
methionine gamma-lyase; Provisional |
69-173 |
1.14e-03 |
|
methionine gamma-lyase; Provisional
Pssm-ID: 168478 [Multi-domain] Cd Length: 400 Bit Score: 40.58 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 69 TSNATDSLNLAIKGVLQEGDHVITTSMEHNSVIRPIK-ALEKRGIENTVVKCDyegflDYEDLEKSIKSNTKLIVTTHAS 147
Cdd:PRK06234 85 AASGMGAISSSLWSALKAGDHVVASDTLYGCTFALLNhGLTRYGVEVTFVDTS-----NLEEVRNALKANTKVVYLETPA 159
|
90 100
....*....|....*....|....*...
gi 489529510 148 NVCGTLIDIKKVGEIAKKHN--ILFLVD 173
Cdd:PRK06234 160 NPTLKVTDIKAISNIAHENNkeCLVFVD 187
|
|
| PRK05994 |
PRK05994 |
O-acetylhomoserine aminocarboxypropyltransferase; Validated |
126-173 |
1.95e-03 |
|
O-acetylhomoserine aminocarboxypropyltransferase; Validated
Pssm-ID: 180344 [Multi-domain] Cd Length: 427 Bit Score: 40.08 E-value: 1.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 489529510 126 DYEDLEKSIKSNTKLIVTTHASNVCGTLIDIKKVGEIAKKHNILFLVD 173
Cdd:PRK05994 137 DPASFERAITPRTKAIFIESIANPGGTVTDIAAIAEVAHRAGLPLIVD 184
|
|
| tyr_nico_aTase |
TIGR01265 |
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ... |
20-173 |
3.84e-03 |
|
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley.
Pssm-ID: 188123 Cd Length: 403 Bit Score: 39.25 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 20 AVLDCMKNYCANPGrAGHKLAMRAAREIYDTReniakLFNVSNPMNIVFTSNATDSLNLAIKGVLQEGDHVI-------- 91
Cdd:TIGR01265 59 DALRSGKFNGYAPS-VGALAAREAVAEYLSSD-----LPGKLTADDVVLTSGCSQAIEICIEALANPGANILvprpgfpl 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489529510 92 --TTSMEHNSVIRPIKALEKRGIEntvvkcdyegfLDYEDLEKSIKSNTKLIVTTHASNVCGTLID---IKKVGEIAKKH 166
Cdd:TIGR01265 133 ydTRAAFSGLEVRLYDLLPEKDWE-----------IDLDGLESLADEKTVAIVVINPSNPCGSVFSrdhLQKIAEVAEKL 201
|
....*..
gi 489529510 167 NILFLVD 173
Cdd:TIGR01265 202 GIPIIAD 208
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
96-172 |
7.98e-03 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 38.20 E-value: 7.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489529510 96 EHNSVIRPIkaLEKRGIENTVVKCDyEGFLDYEDLEKSIKSNTK-LIVTThaSNVCGTLIDIKKVGEIAKKHNILFLV 172
Cdd:PRK00451 166 EYREVLKTY--LKGQGIEVVEVPYE-DGVTDLEALEAAVDDDTAaVVVQY--PNFFGVIEDLEEIAEIAHAGGALFIV 238
|
|
| tnaA |
PRK13238 |
tryptophanase; |
114-178 |
9.46e-03 |
|
tryptophanase;
Pssm-ID: 237314 Cd Length: 460 Bit Score: 37.87 E-value: 9.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489529510 114 NTVVKCDYEGFLDYEDLEKSIKS----NTKLIVTTHASN-VCG---TLIDIKKVGEIAKKHNILFLVDASQTA 178
Cdd:PRK13238 150 DTGSRHPFKGNFDLEKLEALIEEvgaeNVPFIVMTITNNsAGGqpvSMANLRAVYEIAKKYGIPVVIDAARFA 222
|
|
| |
