|
Name |
Accession |
Description |
Interval |
E-value |
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
16-413 |
0e+00 |
|
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine desulfurases involved in FeS cluster formation needed for nitrogen fixation among other vital functions. Many cysteine desulfurases are also active as selenocysteine lyase and/or cysteine sulfinate desulfinase. This subfamily is associated with the six-gene SUF system described in E. coli and Erwinia as an FeS cluster formation system during oxidative stress. The active site Cys is this subfamily resembles GHHC with one or both His conserved. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 131034 [Multi-domain] Cd Length: 403 Bit Score: 663.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 16 KDFPILDQKVNGKRLAYLDSTATSQTPMQVLNVLEDYYKRYNSNVHRGVHTLGSLATDGYENARETVRRFINAKYFEEII 95
Cdd:TIGR01979 5 ADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASDEEIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 96 FTRGTTASINLVAHSYGDANVEEGDEIVVTEMEHHANIVPWQQLAKRKNATLKFIPMTADGELNIEDIKQTINDKTKIVA 175
Cdd:TIGR01979 85 FTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTEKTKLVA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 176 IAHISNVLGTINDVKTIAEIAHQHGAIISVDGAQAAPHMKLDMQEMNADFYSFSGHKMLGPTGIGVLFGKRELLQKMEPI 255
Cdd:TIGR01979 165 ITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQMPPF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 256 EFGGDMIDFVSKYDATWADLPTKFEAGTPLIAQAIGLAEAIRYLERIGFDAIHKYEQELTIYAYEQMSAIEGIEIYGP-P 334
Cdd:TIGR01979 245 LGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRIYGPrD 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446929194 335 KDRRAGVITFNLQDVHPHDVATAVDTEGVAVRAGHHCAQPLMKWLNVSSTARASFYIYNTKEDIDQLINALKQTKEFFS 413
Cdd:TIGR01979 325 AEDRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVRKFFG 403
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
32-405 |
0e+00 |
|
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: 650.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 32 YLDSTATSQTPMQVLNVLEDYYKRYNSNVHRGVHTLGSLATDGYENARETVRRFINAKYFEEIIFTRGTTASINLVAHSY 111
Cdd:cd06453 2 YLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 112 GDANvEEGDEIVVTEMEHHANIVPWQQLAKRKNATLKFIPMTADGELNIEDIKQTINDKTKIVAIAHISNVLGTINDVKT 191
Cdd:cd06453 82 GRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 192 IAEIAHQHGAIISVDGAQAAPHMKLDMQEMNADFYSFSGHKMLGPTGIGVLFGKRELLQKMEPIEFGGDMIDFVSKYDAT 271
Cdd:cd06453 161 IGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEETT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 272 WADLPTKFEAGTPLIAQAIGLAEAIRYLERIGFDAIHKYEQELTIYAYEQMSAIEGIEIYGPPKDrRAGVITFNLQDVHP 351
Cdd:cd06453 241 YADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAED-RAGVVSFNLEGIHP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 446929194 352 HDVATAVDTEGVAVRAGHHCAQPLMKWLNVSSTARASFYIYNTKEDIDQLINAL 405
Cdd:cd06453 320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
10-411 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 646.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 10 DVNEVIKDFPildqkVNGKRLAYLDSTATSQTPMQVLNVLEDYYKRYNSNVHRGVHTLGSLATDGYENARETVRRFINAK 89
Cdd:COG0520 1 DVEAIRADFP-----VLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 90 YFEEIIFTRGTTASINLVAHSYGdaNVEEGDEIVVTEMEHHANIVPWQQLAKRKNATLKFIPMTADGELNIEDIKQTIND 169
Cdd:COG0520 76 SPDEIIFTRGTTEAINLVAYGLG--RLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 170 KTKIVAIAHISNVLGTINDVKTIAEIAHQHGAIISVDGAQAAPHMKLDMQEMNADFYSFSGHKMLGPTGIGVLFGKRELL 249
Cdd:COG0520 154 RTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 250 QKMEPIEFGGDMIDFVSKYDATWADLPTKFEAGTPLIAQAIGLAEAIRYLERIGFDAIHKYEQELTIYAYEQMSAIEGIE 329
Cdd:COG0520 234 EALPPFLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 330 IYGP-PKDRRAGVITFNLQDVHPHDVATAVDTEGVAVRAGHHCAQPLMKWLNVSSTARASFYIYNTKEDIDQLINALKQT 408
Cdd:COG0520 314 ILGPaDPEDRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKL 393
|
...
gi 446929194 409 KEF 411
Cdd:COG0520 394 AEL 396
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
32-401 |
0e+00 |
|
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: 577.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 32 YLDSTATSQTPMQVLNVLEDYYKRYNSNVHRGVHTLGSLATDGYENARETVRRFINAKYFEEIIFTRGTTASINLVAHSY 111
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 112 GDAnVEEGDEIVVTEMEHHANIVPWQQLAKRKNATLKFIPMTADGELNIEDIKQTINDKTKIVAIAHISNVLGTINDVKT 191
Cdd:pfam00266 82 GRS-LKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 192 IAEIAHQHGAIISVDGAQAAPHMKLDMQEMNADFYSFSGHKMLGPTGIGVLFGKRELLQKMEPIEFGGDMIDFVSKYDAT 271
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQEST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 272 WADLPTKFEAGTPLIAQAIGLAEAIRYLERIGFDAIHKYEQELTIYAYEQMSAIEGIEIYGPPkdRRAGVITFNLQDVHP 351
Cdd:pfam00266 241 FADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPE--RRASIISFNFKGVHP 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446929194 352 HDVATAVDTEGVAVRAGHHCAQPLMKWLNVSSTARASFYIYNTKEDIDQL 401
Cdd:pfam00266 319 HDVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
13-413 |
0e+00 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 553.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 13 EVIKDFPILDQKVNGKRLAYLDSTATSQTPMQVLNVLEDYYKRYNSNVHRGVHTLGSLATDGYENARETVRRFINAKYFE 92
Cdd:PLN02855 16 ETRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINASTSR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 93 EIIFTRGTTASINLVAHSYGDANVEEGDEIVVTEMEHHANIVPWQQLAKRKNATLKFIPMTADGELNIEDIKQTINDKTK 172
Cdd:PLN02855 96 EIVFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 173 IVAIAHISNVLGTINDVKTIAEIAHQHGAIISVDGAQAAPHMKLDMQEMNADFYSFSGHKMLGPTGIGVLFGKRELLQKM 252
Cdd:PLN02855 176 LVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLESM 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 253 EPIEFGGDMIDFVSKYDATWADLPTKFEAGTPLIAQAIGLAEAIRYLERIGFDAIHKYEQELTIYAYEQMSAIEGIEIYG 332
Cdd:PLN02855 256 PPFLGGGEMISDVFLDHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRIYG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 333 PPK---DRRAGVITFNLQDVHPHDVATAVDTE-GVAVRAGHHCAQPLMKWLNVSSTARASFYIYNTKEDIDQLINALKQT 408
Cdd:PLN02855 336 PKPsegVGRAALCAFNVEGIHPTDLSTFLDQQhGVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIHALKDT 415
|
....*
gi 446929194 409 KEFFS 413
Cdd:PLN02855 416 IAFFS 420
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
9-407 |
0e+00 |
|
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: 536.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 9 FDVNEVIKDFPILDQKVNGKRLAYLDSTATSQTPMQVLNVLEDYYKRYNSNVHRGVHTLGSLATDGYENARETVRRFINA 88
Cdd:NF041166 225 FDVNAVRRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIGA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 89 KYFEEIIFTRGTTASINLVAHSYGDANVEEGDEIVVTEMEHHANIVPWQQLAKRKNATLKFIPMTADGELNIEDIKQTIN 168
Cdd:NF041166 305 PSVDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLDEYAKLLN 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 169 DKTKIVAIAHISNVLGTINDVKTIAEIAHQHGAIISVDGAQAAPHMKLDMQEMNADFYSFSGHKMLGPTGIGVLFGKREL 248
Cdd:NF041166 385 PRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKRDL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 249 LQKMEPIEFGGDMIDfvskyDATWA-----DLPTKFEAGTPLIAQAIGLAEAIRYLERIGFDAIHKYEQELTIYAYEQMS 323
Cdd:NF041166 465 LEAMPPWQGGGNMIA-----DVTFEktvyqPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATAGLA 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 324 AIEGIEIYGPPKDrRAGVITFNLQDVHPHDVATAVDTEGVAVRAGHHCAQPLMKWLNVSSTARASFYIYNTKEDIDQLIN 403
Cdd:NF041166 540 EVPGLRLIGTAAD-KASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDALVA 618
|
....
gi 446929194 404 ALKQ 407
Cdd:NF041166 619 VLRR 622
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
8-407 |
4.80e-170 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 481.94 E-value: 4.80e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 8 SFDVNEVIKDFPILDQKVNGKRLAYLDSTATSQTPMQVLNVLEDYYKRYNSNVHRGVHTLGSLATDGYENARETVRRFIN 87
Cdd:PRK09295 2 TFSVEKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 88 AKYFEEIIFTRGTTASINLVAHSYGDANVEEGDEIVVTEMEHHANIVPWQQLAKRKNATLKFIPMTADGELNIEDIKQTI 167
Cdd:PRK09295 82 ARSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 168 NDKTKIVAIAHISNVLGTINDVKTIAEIAHQHGAIISVDGAQAAPHMKLDMQEMNADFYSFSGHKMLGPTGIGVLFGKRE 247
Cdd:PRK09295 162 DERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 248 LLQKMEPIEFGGDMIDFVS-KYDATWADLPTKFEAGTPLIAQAIGLAEAIRYLERIGFDAIHKYEQELTIYAYEQMSAIE 326
Cdd:PRK09295 242 LLQEMPPWEGGGSMIATVSlTEGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESVP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 327 GIEIYGPpkDRRAGVITFNLQDVHPHDVATAVDTEGVAVRAGHHCAQPLMKWLNVSSTARASFYIYNTKEDIDQLINALK 406
Cdd:PRK09295 322 DLTLYGP--QNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQ 399
|
.
gi 446929194 407 Q 407
Cdd:PRK09295 400 R 400
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
8-406 |
3.30e-132 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 385.55 E-value: 3.30e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 8 SFDVNEVIKDFPILDQKvngkrLAYLDSTATSQTPMQVLNVLEDYYKRYNSNVHRGVHTLGSLATDGYENARETVRRFIN 87
Cdd:PRK10874 3 VFNPAQFRAQFPALQDA-----GVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 88 AKYFEEIIFTRGTTASINLVAHSYGDANVEEGDEIVVTEMEHHANIVPWQQLAKRKNATLKFIPMTADGELNIEDIKQTI 167
Cdd:PRK10874 78 APDAKNIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 168 NDKTKIVAIAHISNVLGTINDVKTIAEIAHQHGAIISVDGAQAAPHMKLDMQEMNADFYSFSGHKMLGPTGIGVLFGKRE 247
Cdd:PRK10874 158 TPRTRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 248 LLQKMEPIEFGGDMIDFVSKYDATWADLPTKFEAGTPLIAQAIGLAEAIRYLERIGFDAIHKYEQELTIYAYEQMSAIEG 327
Cdd:PRK10874 238 LLEAMSPWQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLPG 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446929194 328 IEIYGPPKdrrAGVITFNLQDVHPHDVATAVDTEGVAVRAGHHCAQPLMKWLNVSSTARASFYIYNTKEDIDQLINALK 406
Cdd:PRK10874 318 FRSFRCQD---SSLLAFDFAGVHHSDLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVD 393
|
|
| FeS_syn_CsdA |
TIGR03392 |
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This ... |
9-413 |
2.97e-127 |
|
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This protein, found Escherichia coli, Yersinia pestis, Photorhabdus luminescens, and related species, and related to SufS, works together with and physically interacts with CsdE (a paralog of SufE). CsdA has cysteine desulfurase activity that is enhanced by CsdE, a sulfur acceptor protein. This gene pair, although involved in FeS cluster biosynthesis, is not found next to other such genes as are its paralogs from the Suf or Isc systems. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274558 [Multi-domain] Cd Length: 398 Bit Score: 373.02 E-value: 2.97e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 9 FDVNEVIKDFPILDQKvngkrLAYLDSTATSQTPMQVLNVLEDYYKRYNSNVHRGVHTLGSLATDGYENARETVRRFINA 88
Cdd:TIGR03392 1 FNPAQFRRQFPALQDA-----TVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 89 KYFEEIIFTRGTTASINLVAHSYGDANVEEGDEIVVTEMEHHANIVPWQQLAKRKNATLKFIPMTADGELNIEDIKQTIN 168
Cdd:TIGR03392 76 PDAENIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIGADLLPDIDQLPELLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 169 DKTKIVAIAHISNVLGTINDVKTIAEIAHQHGAIISVDGAQAAPHMKLDMQEMNADFYSFSGHKMLGPTGIGVLFGKREL 248
Cdd:TIGR03392 156 PRTRILALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKTEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 249 LQKMEPIEFGGDMIDFVSKYDATWADLPTKFEAGTPLIAQAIGLAEAIRYLERIGFDAIHKYEQELTIYAYEQMSAIEGI 328
Cdd:TIGR03392 236 LEAMPPWQGGGKMLSHVSFDGFTPQAVPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQLPGF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 329 EIYGPPKdrrAGVITFNLQDVHPHDVATAVDTEGVAVRAGHHCAQPLMKWLNVSSTARASFYIYNTKEDIDQLINALKQT 408
Cdd:TIGR03392 316 RSFRCQG---SSLLAFDFAGVHHSDLVTLLAEQGIALRAGQHCAQPLMAALGVSGTLRASFAPYNTQQDVDALVNAVGRA 392
|
....*
gi 446929194 409 KEFFS 413
Cdd:TIGR03392 393 LELLV 397
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
9-405 |
1.99e-82 |
|
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: 258.14 E-value: 1.99e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 9 FDVNEVIKDFPILDQkvnGKRlAYLDSTATSQTPMQVLNVLEDYYKRYNSNvhRGVHTLGSLATDGY-ENARETVRRFIN 87
Cdd:TIGR01976 1 FDVEAVRGQFPALAD---GDR-VFFDNPAGTQIPQSVADAVSAALTRSNAN--RGGAYESSRRADQVvDDAREAVADLLN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 88 AkYFEEIIFTRGTTASINLVAHSYGdANVEEGDEIVVTEMEHHANIVPWQQLAKRKNATLKFIPM-TADGELNIEDIKQT 166
Cdd:TIGR01976 75 A-DPPEVVFGANATSLTFLLSRAIS-RRWGPGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVdEATGELHPDDLASL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 167 INDKTKIVAIAHISNVLGTINDVKTIAEIAHQHGAIISVDGAQAAPHMKLDMQEMNADFYSFSGHKMLGPTgIGVLFGKR 246
Cdd:TIGR01976 153 LSPRTRLVAVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPH-MGILWGRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 247 ELLQKMEPiefggdmidfvSKYDATWADLPTKFEAGTPLIAQAIGLAEAIRYLERIG--------------FDAIHKYEQ 312
Cdd:TIGR01976 232 ELLMNLPP-----------YKLTFSYDTGPERFELGTPQYELLAGVVAAVDYLAGLGesangsrrerlvasFQAIDAYEN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 313 ELTIYAYEQMSAIEGIEIYGPPK-DRRAGVITFNLQDVHPHDVATAVDTEGVAVRAGHHCAQPLMKWLNVSS---TARAS 388
Cdd:TIGR01976 301 RLAEYLLVGLSDLPGVTLYGVARlAARVPTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLRRLGLNDeggVVRVG 380
|
410
....*....|....*..
gi 446929194 389 FYIYNTKEDIDQLINAL 405
Cdd:TIGR01976 381 LAHYNTAEEVDRLLEAL 397
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
28-408 |
9.26e-69 |
|
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: 222.23 E-value: 9.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 28 KRLAYLDSTATsqTPM--QVLNVLEDYYKRYNSNVHRgVHTLGSLATDGYENARETVRRFINAKYfEEIIFTRGTTASIN 105
Cdd:COG1104 1 MMMIYLDNAAT--TPVdpEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADP-EEIIFTSGGTEANN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 106 LVAHSYGDANVEEGDEIVVTEMEHHANIVPWQQLAKRkNATLKFIPMTADGELNIEDIKQTINDKTKIVAIAHISNVLGT 185
Cdd:COG1104 77 LAIKGAARAYRKKGKHIITSAIEHPAVLETARFLEKE-GFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 186 INDVKTIAEIAHQHGAIISVDGAQAAPHMKLDMQEMNADFYSFSGHKMLGPTGIGVLFGKRELlqKMEPIEFGGDMidfv 265
Cdd:COG1104 156 IQPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGV--RLEPLIHGGGQ---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 266 skydatwadlptkfE----AGTPLIAQAIGLAEAIRYLERiGFDAIHKYEQELTIYAYEQMSA-IEGIEIYGPPKDRRAG 340
Cdd:COG1104 230 --------------ErglrSGTENVPGIVGLGKAAELAAE-ELEEEAARLRALRDRLEEGLLAaIPGVVINGDPENRLPN 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446929194 341 VITFNLQDVHPHDVATAVDTEGVAVRAGHHCAQ------PLMKWLNVSSTA-----RASFYIYNTKEDIDQLINALKQT 408
Cdd:COG1104 295 TLNFSFPGVEGEALLLALDLAGIAVSSGSACSSgslepsHVLLAMGLDEELahgsiRFSLGRFTTEEEIDRAIEALKEI 373
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
32-259 |
1.23e-37 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 140.85 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 32 YLDSTATSQTPMQVLNVLEDYYKRYN--SNVHRGVHTLGSLATDGYENARETVRRFINAKYfEEIIFTRGTTASINL--- 106
Cdd:PRK14012 6 YLDYSATTPVDPRVAEKMMPYLTMDGtfGNPASRSHRFGWQAEEAVDIARNQIADLIGADP-REIVFTSGATESDNLaik 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 107 -VAHSYGdanvEEGDEIVVTEMEHHANIVPWQQLaKRKNATLKFIPMTADGELNIEDIKQTINDKTKIVAIAHISNVLGT 185
Cdd:PRK14012 85 gAAHFYQ----KKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446929194 186 INDVKTIAEIAHQHGAIISVDGAQAAPHMKLDMQEMNADFYSFSGHKMLGPTGIGVLFGKRELLQKMEPIEFGG 259
Cdd:PRK14012 160 IQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGG 233
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
32-259 |
4.61e-33 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 127.46 E-value: 4.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 32 YLDSTATsqTPM--QVLNVLEDYYKRYNSNVHRGVHTLGSLATDGYENARETVRRFINAKYfEEIIFTRGTTASINL--- 106
Cdd:PLN02651 2 YLDMQAT--TPIdpRVLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADP-KEIIFTSGATESNNLaik 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 107 -VAHSYGDANveegDEIVVTEMEHHANIVPWQQLAKRkNATLKFIPMTADGELNIEDIKQTINDKTKIVAIAHISNVLGT 185
Cdd:PLN02651 79 gVMHFYKDKK----KHVITTQTEHKCVLDSCRHLQQE-GFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446929194 186 INDVKTIAEIAHQHGAIISVDGAQAAPHMKLDMQEMNADFYSFSGHKMLGPTGIGVLFGKRELLQKMEPIEFGG 259
Cdd:PLN02651 154 IQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGG 227
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
32-412 |
4.92e-27 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 110.97 E-value: 4.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 32 YLDSTATsqTPM--QVLNVLEDYYKRYNSNvHRGVHTLGSLATDGYENARETVRRFINAKYfEEIIFTRGTTASINLVAH 109
Cdd:PRK02948 3 YLDYAAT--TPMskEALQTYQKAASQYFGN-ESSLHDIGGTASSLLQVCRKTFAEMIGGEE-QGIYFTSGGTESNYLAIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 110 SYGDANVEEGDEIVVTEMEHHANIVPWQQLAKRkNATLKFIPMTADGELNIEDIKQTINDKTKIVAIAHISNVLGTINDV 189
Cdd:PRK02948 79 SLLNALPQNKKHIITTPMEHASIHSYFQSLESQ-GYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 190 KTIAEIAHQHGAIISVDGAQAAPHMKLDMQEMNADFYSFSGHKMLGPTGIGVLFGKRELlqKMEPI------EFGgdmid 263
Cdd:PRK02948 158 AEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQV--RWKPVfpgtthEKG----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 264 fvskydatwadlptkFEAGT---PLIAQAIGLAEAIryLERIGfDAIHKYEQeLTIYAYEQMSAIE-GIEIYGPPKDRRA 339
Cdd:PRK02948 231 ---------------FRPGTvnvPGIAAFLTAAENI--LKNMQ-EESLRFKE-LRSYFLEQIQTLPlPIEVEGHSTSCLP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 340 GVI-----TFNLQDV----HPHDVATAVdteGVAVRAGHHCAQPLMKWLNVSST-----ARASFYIYNTKEDIDQLINAL 405
Cdd:PRK02948 292 HIIgvtikGIEGQYTmlecNRRGIAIST---GSACQVGKQEPSKTMLAIGKTYEeakqfVRFSFGQQTTKDQIDTTIHAL 368
|
410
....*....|.
gi 446929194 406 ----KQTKEFF 412
Cdd:PRK02948 369 etigNQFYRGV 379
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
75-245 |
5.84e-17 |
|
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: 77.81 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 75 YENARETVRRFINAKyFEEIIFTRGTTASINLVAHSYgdanVEEGDEIVVTEMEHHANIVpwqQLAKRKNATLKFIPM-- 152
Cdd:cd01494 2 LEELEEKLARLLQPG-NDKAVFVPSGTGANEAALLAL----LGPGDEVIVDANGHGSRYW---VAAELAGAKPVPVPVdd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 153 TADGELNIEDIKQTIN-DKTKIVAIAHISNVLGTINDVKTIAEIAHQHGAIISVDGAQAAPHM---KLDMQEMNADFYSF 228
Cdd:cd01494 74 AGYGGLDVAILEELKAkPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASpapGVLIPEGGADVVTF 153
|
170
....*....|....*..
gi 446929194 229 SGHKMLGPTGIGVLFGK 245
Cdd:cd01494 154 SLHKNLGGEGGGVVIVK 170
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
96-247 |
7.37e-14 |
|
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: 72.42 E-value: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 96 FTRGTTASINLVAHSYgdanVEEGDEIVVTEMEHHANIVPwqqlAKRKNATLKFIPMTADGE--LNIEDIKQTINDKT-- 171
Cdd:cd06452 64 VTPGAREGKFAVMHSL----CEKGDWVVVDGLAHYTSYVA----AERAGLNVREVPNTGHPEyhITPEGYAEVIEEVKde 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 172 --KIVAIAHISNV---LGTINDVKTIAEIAHQHGAIISVDGAQAAPHMKLDMQEMNADFYSFSGHK-MLGPTGIGVLFGK 245
Cdd:cd06452 136 fgKPPALALLTHVdgnYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSGHKsMAASAPIGVLATT 215
|
..
gi 446929194 246 RE 247
Cdd:cd06452 216 EE 217
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
80-242 |
1.97e-13 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 71.12 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 80 ETVRRFINAkyfEEIIFTRGTTASINLVAHSYgdanVEEGDEIVVTEMEHHANIVPwqqlAKRKNATLKFIPMTADGELN 159
Cdd:PRK09331 70 EDLAEFLGM---DEARVTHGAREGKFAVMHSL----CKKGDYVVLDGLAHYTSYVA----AERAGLNVREVPKTGYPEYK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 160 I------EDIKQTINDKTKIVAIAHISNV---LGTINDVKTIAEIAHQHGAIISVDGAQAAPHMKLDMQEMNADFYSFSG 230
Cdd:PRK09331 139 ItpeayaEKIEEVKEETGKPPALALLTHVdgnYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGSG 218
|
170
....*....|...
gi 446929194 231 HK-MLGPTGIGVL 242
Cdd:PRK09331 219 HKsMAASAPSGVL 231
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
116-343 |
3.93e-12 |
|
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: 66.93 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 116 VEEGDEIVVTEMEHHANIvpWQQLAKRKNAtlKFIPMTAD-GE-LNIEDIKQTINDKT-KIVAIAHISNVLGTINDVKTI 192
Cdd:cd06451 71 LEPGDKVLVGVNGVFGDR--WADMAERYGA--DVDVVEKPwGEaVSPEEIAEALEQHDiKAVTLTHNETSTGVLNPLEGI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 193 AEIAHQHGAIISVDGAQAAPHMKLDMQEMNADfYSFSG-HKMLG-PTGIG-VLFGKR--ELLQKMEPIEFG----GDMID 263
Cdd:cd06451 147 GALAKKHDALLIVDAVSSLGGEPFRMDEWGVD-VAYTGsQKALGaPPGLGpIAFSERalERIKKKTKPKGFyfdlLLLLK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 264 FVSKYDATWAdlptkfeagTPLIAQAIGLAEAIRYLERIGFDAIHKYEQELTIYAYEQMSAIeGIEIYGPPKDRRAGVIT 343
Cdd:cd06451 226 YWGEGYSYPH---------TPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEAL-GLKLLAKPELRSPTVTA 295
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
150-407 |
1.39e-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: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 150 IPMTADGELNIEDIKQTINDKTK-------IVAIAhisnvlGTIN-----DVKTIAEIAHQHGAIISVDGAQ---AAPHM 214
Cdd:COG0076 194 VPVDEDGRMDPDALEAAIDEDRAaglnpiaVVATA------GTTNtgaidPLAEIADIAREHGLWLHVDAAYggfALPSP 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 215 KLdmQEM-----NADFYSFSGHKMLG-PTGIG-VLFGKRELLQKMEPIEFggdmiDFVSKYDATWADLPTK-FEAGTPli 286
Cdd:COG0076 268 EL--RHLldgieRADSITVDPHKWLYvPYGCGaVLVRDPELLREAFSFHA-----SYLGPADDGVPNLGDYtLELSRR-- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 287 AQAIGLAEAIRYLERIGFDAIHKYEQELTIYAYEQMSAIEGIEIYGPPkdrRAGVITF-------NLQDVHPHDVATAVD 359
Cdd:COG0076 339 FRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPP---ELNIVCFrykpaglDEEDALNYALRDRLR 415
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446929194 360 TEGVAVRAGHHcaqplmkwLNVSSTARASfyIYN---TKEDIDQLINALKQ 407
Cdd:COG0076 416 ARGRAFLSPTK--------LDGRVVLRLV--VLNprtTEDDVDALLDDLRE 456
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
28-371 |
2.90e-11 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 65.27 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 28 KRL---AYLD-STATSQTPMQVLNVLEDYykryNSNVHRGVHT---LGSLATDGYENARETVRRFINAKYFE-EIIFTRG 99
Cdd:PLN02724 30 ARLkgvVYLDhAGATLYSESQLEAALADF----SSNVYGNPHSqsdSSMRSSDTIESARQQVLEYFNAPPSDyACVFTSG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 100 TTASINLVAHSYgdaNVEEGDEIVVTeMEHHANIVPWQQLAKRKNAT-----------------------LKFIPMTADG 156
Cdd:PLN02724 106 ATAALKLVGETF---PWSSESHFCYT-LENHNSVLGIREYALEKGAAaiavdieeaanqptnsqgsvvvkSRGLQRRNTS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 157 ELNI-EDIKQTINdktkIVAIAHISNVLG---TINDVKTIAEIAHQHGA-----IISVDGAQAAPHMKLDMQEMNADFYS 227
Cdd:PLN02724 182 KLQKrEDDGEAYN----LFAFPSECNFSGakfPLDLVKLIKDNQHSNFSksgrwMVLLDAAKGCGTSPPDLSRYPADFVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 228 FSGHKMLG-PTGIGVLFGKRELLQKMEPIEFGGDM-------IDFVSKYDatwaDLPTKFEAGTpliAQAIGLAeAIRY- 298
Cdd:PLN02724 258 VSFYKIFGyPTGLGALLVRRDAAKLLKKKYFGGGTvaasiadIDFVKRRE----RVEQRFEDGT---ISFLSIA-ALRHg 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 299 ---LERIGFDAIHKYEQELTIYAYEQMSAIE-----------GIEIYGPPKDRRAGVITFNLQD-----VHPHDVATAVD 359
Cdd:PLN02724 330 fklLNRLTISAIAMHTWALTHYVANSLRNLKhgngapvcvlyGNHTFKLEFHIQGPIVTFNLKRadgswVGHREVEKLAS 409
|
410
....*....|..
gi 446929194 360 TEGVAVRAGHHC 371
Cdd:PLN02724 410 LSGIQLRTGCFC 421
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
72-407 |
3.39e-11 |
|
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: 64.28 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 72 TDGYENARETVRRFINAKYF-----EEIIFTRGTTASINLVAHSYgdanVEEGDEIVVTEmehhanivP----WQQLAKR 142
Cdd:cd00609 35 DPGLPELREAIAEWLGRRGGvdvppEEIVVTNGAQEALSLLLRAL----LNPGDEVLVPD--------PtypgYEAAARL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 143 KNATLKFIPMTADG--ELNIEDIKQTINDKTKIVAIAHISNVLGTI---NDVKTIAEIAHQHGAIISVDGA------QAA 211
Cdd:cd00609 103 AGAEVVPVPLDEEGgfLLDLELLEAAKTPKTKLLYLNNPNNPTGAVlseEELEELAELAKKHGILIISDEAyaelvyDGE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 212 PHMKLDMQEMNAD---FYSFSghKMLGPTG--IGVLFGKRELLQKMepiefggdmidFVSKYDATWadlptkfeAGTPLI 286
Cdd:cd00609 183 PPPALALLDAYERvivLRSFS--KTFGLPGlrIGYLIAPPEELLER-----------LKKLLPYTT--------SGPSTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 287 AQAIGLA---EAIRYLERIgfdaIHKYEQELTiYAYEQMSAIEGIEIYGPPkdrragvITFNL-----QDVHPHDVATAV 358
Cdd:cd00609 242 SQAAAAAaldDGEEHLEEL----RERYRRRRD-ALLEALKELGPLVVVKPS-------GGFFLwldlpEGDDEEFLERLL 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446929194 359 DTEGVAVRAGHHCAQPLMKWLNVSSTarasfyiyNTKEDIDQLINALKQ 407
Cdd:cd00609 310 LEAGVVVRPGSAFGEGGEGFVRLSFA--------TPEEELEEALERLAE 350
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
136-343 |
2.26e-10 |
|
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: 61.64 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 136 WQQLAKRKNATLKFIPMTADGELNIEDIKQTI--NDKTKIVAIAHI--SNvlGTINDVKTIAEIAHQHGAIISVD----- 206
Cdd:COG0075 89 WAEIAERYGAEVVVLEVPWGEAVDPEEVEEALaaDPDIKAVAVVHNetST--GVLNPLEEIGALAKEHGALLIVDavssl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 207 GAqaaphMKLDMQEMNADFYSFSGHKML-GPTGIGVLFGKRELLQKMEPIEFGGDMIDFvSKYDATWADLPTKFEAGTPL 285
Cdd:COG0075 167 GG-----VPLDMDEWGIDVVVSGSQKCLmLPPGLAFVAVSERALEAIEARKLPSYYLDL-KLWLKYWEKGQTPYTPPVSL 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446929194 286 IAqaiGLAEAIRYLERIGFDAIHKYEQELTIYAYEQMSAIeGIEIYgPPKDRRAGVIT 343
Cdd:COG0075 241 LY---ALREALDLILEEGLENRFARHRRLAEALRAGLEAL-GLELF-AEEEYRSPTVT 293
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
121-348 |
1.10e-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: 59.52 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 121 EIVVTEMEHHAnivpWQQLAKRKNATLKFIPMTADGELNIEDIKQTINDKTK-------IVAIAHISNvLGTINDVKTIA 193
Cdd:cd06450 97 VIVCSDQAHVS----VEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEDKAeglnpimVVATAGTTD-TGAIDPLEEIA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 194 EIAHQHGAIISVDGAQ---AAPHMKLDmQEMN----ADFYSFSGHKMLG-PTGIGVLFGKrellqkmepiefggdmidfv 265
Cdd:cd06450 172 DLAEKYDLWLHVDAAYggfLLPFPEPR-HLDFgierVDSISVDPHKYGLvPLGCSAVLVR-------------------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 266 skydatwadlptkfeagtpliaqAIGLAEAIRYLERIGFDAIHKYEQELTIYAYEQMSAIEGIEIYGPPK---------- 335
Cdd:cd06450 231 -----------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNlslvcfrlkp 287
|
250
....*....|...
gi 446929194 336 DRRAGVITFNLQD 348
Cdd:cd06450 288 SVKLDELNYDLSD 300
|
|
| Cys_Met_Meta_PP |
pfam01053 |
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and ... |
96-212 |
3.07e-09 |
|
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: 58.40 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 96 FTRGTTASINLVAHSygdanVEEGDEIVVTEMEHHANIVPWQQLAKRKNATLKFIPMTadgelNIEDIKQTINDKTKIVA 175
Cdd:pfam01053 68 FSSGMAAITAAILAL-----LKAGDHIVATDDLYGGTYRLFNKVLPRFGIEVTFVDTS-----DPEDLEAAIKPNTKAVY 137
|
90 100 110
....*....|....*....|....*....|....*..
gi 446929194 176 IAHISNVLGTINDVKTIAEIAHQHGAIISVDGAQAAP 212
Cdd:pfam01053 138 LETPTNPLLKVVDIEAIAKLAKKHGILVVVDNTFASP 174
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
91-251 |
1.26e-08 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 55.68 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 91 FEEIIFT-RGTTAsiNLVAHSygdANVEEGDEIVVTEmehHANIVPWQQ--LAKRKNATLKFIPMTADGELNIEDIKQTI 167
Cdd:pfam01212 47 KEAALFVpSGTAA--NQLALM---AHCQRGDEVICGE---PAHIHFDETggHAELGGVQPRPLDGDEAGNMDLEDLEAAI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 168 -------NDKTKIVAIAHISNVLG----TINDVKTIAEIAHQHGAIISVDGAQ---AAPHMKLDMQEM--NADFYSFSGH 231
Cdd:pfam01212 119 revgadiFPPTGLISLENTHNSAGgqvvSLENLREIAALAREHGIPVHLDGARfanAAVALGVIVKEItsYADSVTMCLS 198
|
170 180
....*....|....*....|.
gi 446929194 232 KMLG-PTGiGVLFGKRELLQK 251
Cdd:pfam01212 199 KGLGaPVG-SVLAGSDDFIAK 218
|
|
| PLN02509 |
PLN02509 |
cystathionine beta-lyase |
96-251 |
1.98e-08 |
|
cystathionine beta-lyase
Pssm-ID: 178125 [Multi-domain] Cd Length: 464 Bit Score: 56.19 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 96 FTRGTtASINLVAHSygdanVEEGDEIVVTEMEHHANIVPWQQLAKRKNATLKFIPMTadgelNIEDIKQTINDKTKIVA 175
Cdd:PLN02509 154 FTSGM-AALSAVTHL-----IKNGEEIVAGDDVYGGSDRLLSQVVPRSGVVVKRVNTT-----NLDEVAAAIGPQTKLVW 222
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446929194 176 IAHISNVLGTINDVKTIAEIAHQHGAIISVDGAQAAPHMKLDMqEMNADFYSFSGHKML-GPTGI--GVLFGKRELLQK 251
Cdd:PLN02509 223 LESPTNPRQQISDIRKIAEMAHAQGALVLVDNSIMSPVLSRPL-ELGADIVMHSATKFIaGHSDVmaGVLAVKGEKLAK 300
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
72-405 |
3.60e-08 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 55.00 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 72 TDGYENARETVRRFINAKYF------EEIIFTRGTTASINLVAHSYGDAnveeGDEIVVTEMEH--HANIVPWQQLAKRK 143
Cdd:pfam00155 38 TDGHPELREALAKFLGRSPVlkldreAAVVFGSGAGANIEALIFLLANP----GDAILVPAPTYasYIRIARLAGGEVVR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 144 NATLKfipmTADGELNIEDIKQTINDKTKIVAIAHISNVLGTI---NDVKTIAEIAHQHGAIISVD--------GAQAAP 212
Cdd:pfam00155 114 YPLYD----SNDFHLDFDALEAALKEKPKVVLHTSPHNPTGTVatlEELEKLLDLAKEHNILLLVDeayagfvfGSPDAV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 213 HMKLDMQEMNADF--YSFSghKMLGPTG--IGVLFGKRELLQKMEpiefggDMIDFVSkydatwadlptkfeagTPLIAQ 288
Cdd:pfam00155 190 ATRALLAEGPNLLvvGSFS--KAFGLAGwrVGYILGNAAVISQLR------KLARPFY----------------SSTHLQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 289 AIGLAEAIRYLERIGF-DAIHKYEQELTIYAYEQMSAIeGIEIYGPPkdrrAGVITFnlqDVHPHDVATA-----VDTEG 362
Cdd:pfam00155 246 AAAAAALSDPLLVASElEEMRQRIKERRDYLRDGLQAA-GLSVLPSQ----AGFFLL---TGLDPETAKElaqvlLEEVG 317
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446929194 363 VAVRAGHHCAQPlmKWLNVSSTARasfyiynTKEDIDQLINAL 405
Cdd:pfam00155 318 VYVTPGSSPGVP--GWLRITVAGG-------TEEELEELLEAI 351
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
102-212 |
5.63e-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: 54.13 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 102 ASINLVAHSYgdanVEEGDEIVVTEMEHHANIVPWQQLAKRKNATLKFIPMTadgelNIEDIKQTINDKTKIVAIAHISN 181
Cdd:cd00614 66 AAISTVLLAL----LKAGDHVVASDDLYGGTYRLFERLLPKLGIEVTFVDPD-----DPEALEAAIKPETKLVYVESPTN 136
|
90 100 110
....*....|....*....|....*....|.
gi 446929194 182 VLGTINDVKTIAEIAHQHGAIISVDGAQAAP 212
Cdd:cd00614 137 PTLKVVDIEAIAELAHEHGALLVVDNTFATP 167
|
|
| SelA |
COG1921 |
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis]; |
160-252 |
2.75e-07 |
|
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441524 Cd Length: 399 Bit Score: 52.43 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 160 IEDIKQTINDKTKIVAIAHISN--VLGTINDV--KTIAEIAHQHGAIISVD-GAQAAPHMKL-------DMQE---MNAD 224
Cdd:COG1921 144 LRDYEAAITENTAALLKVHTSNyrIVGFTEEVslAELAELAHEHGLPVIVDlGSGSLVDLSKyglphepTVQEylaAGAD 223
|
90 100
....*....|....*....|....*....
gi 446929194 225 FYSFSGHKML-GPTGiGVLFGKRELLQKM 252
Cdd:COG1921 224 LVTFSGDKLLgGPQA-GIIVGKKELIERI 251
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
116-314 |
3.39e-07 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 52.07 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 116 VEEGDEIVVTEMEHHANIvpWQQLAKRKNATLKFIPMTADGELNIEDIKQTI----NDKTKIVAIAHISNVLGTINDVKT 191
Cdd:PLN02409 81 LSPGDKVVSFRIGQFSLL--WIDQMQRLNFDVDVVESPWGQGADLDILKSKLrqdtNHKIKAVCVVHNETSTGVTNDLAG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 192 IAEI--AHQHGAIISVDGAQAAPHMKLDMQEMNADF-YSFSGHKMLGPTGIGVLFGKRELLQKME----PIEFggdmidf 264
Cdd:PLN02409 159 VRKLldCAQHPALLLVDGVSSIGALDFRMDEWGVDVaLTGSQKALSLPTGLGIVCASPKALEASKtaksPRVF------- 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446929194 265 vskYDatWADLPTKFEAG-----TPLIAQAIGLAEAIRYLERIGFDAIHKYEQEL 314
Cdd:PLN02409 232 ---FD--WADYLKFYKLGtywpyTPSIQLLYGLRAALDLIFEEGLENVIARHARL 281
|
|
| PRK08248 |
PRK08248 |
homocysteine synthase; |
108-238 |
3.77e-07 |
|
homocysteine synthase;
Pssm-ID: 236201 [Multi-domain] Cd Length: 431 Bit Score: 51.77 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 108 AHSYGDANVEE-GDEIVVTEMEHHANIVPWQQLAKRKNATLKFIPMTadgelNIEDIKQTINDKTKIVAIAHISNVLGTI 186
Cdd:PRK08248 91 AITYSILNIASaGDEIVSSSSLYGGTYNLFAHTLPKLGITVKFVDPS-----DPENFEAAITDKTKALFAETIGNPKGDV 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446929194 187 NDVKTIAEIAHQHGAIISVDGAQAAPHMkLDMQEMNADFYSFSGHKMLGPTG 238
Cdd:PRK08248 166 LDIEAVAAIAHEHGIPLIVDNTFASPYL-LRPIEHGADIVVHSATKFIGGHG 216
|
|
| PRK05994 |
PRK05994 |
O-acetylhomoserine aminocarboxypropyltransferase; Validated |
154-238 |
1.42e-06 |
|
O-acetylhomoserine aminocarboxypropyltransferase; Validated
Pssm-ID: 180344 [Multi-domain] Cd Length: 427 Bit Score: 50.10 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 154 ADGElNIEDIKQTINDKTKIVAIAHISNVLGTINDVKTIAEIAHQHGAIISVDGAQAAPHMkLDMQEMNADFYSFSGHKM 233
Cdd:PRK05994 133 ADAD-DPASFERAITPRTKAIFIESIANPGGTVTDIAAIAEVAHRAGLPLIVDNTLASPYL-IRPIEHGADIVVHSLTKF 210
|
....*
gi 446929194 234 LGPTG 238
Cdd:PRK05994 211 LGGHG 215
|
|
| AHBA_syn |
cd00616 |
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ... |
114-406 |
2.85e-06 |
|
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: 49.08 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 114 ANVEEGDEIVVTEMEHHANIVPWQQLakrkNATLKFIPMTAD-GELNIEDIKQTINDKTKIVAIAHIsnvLGTINDVKTI 192
Cdd:cd00616 53 LGIGPGDEVIVPSFTFVATANAILLL----GATPVFVDIDPDtYNIDPELIEAAITPRTKAIIPVHL---YGNPADMDAI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 193 AEIAHQHGAIISVDGAQAapHMKLDMQEMNADF-----YSFSGHKMLGpTGIG--VLFGKRELLQKMEPI-EFGGDmidf 264
Cdd:cd00616 126 MAIAKRHGLPVIEDAAQA--LGATYKGRKVGTFgdagaFSFHPTKNLT-TGEGgaVVTNDEELAERARLLrNHGRD---- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 265 VSKYDATWADLPTKFEAgTPLIAqAIGLAeairYLERIgfDAIHKYEQELTIYAYEQMSAIEGIEIYGPPKDRRAG---- 340
Cdd:cd00616 199 RDRFKYEHEILGYNYRL-SEIQA-AIGLA----QLEKL--DEIIARRREIAERYKELLADLPGIRLPDVPPGVKHSyhly 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 341 -VITFNLQDVHPHDVATAVDTEGVAVR---AGHHCAQPLMKWLNVSS-----TARAS-------FYIYNTKEDIDQLINA 404
Cdd:cd00616 271 vIRLDPEAGESRDELIEALKEAGIETRvhyPPLHHQPPYKKLLGYPPgdlpnAEDLAervlslpLHPSLTEEEIDRVIEA 350
|
..
gi 446929194 405 LK 406
Cdd:cd00616 351 LR 352
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
153-206 |
3.45e-06 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 48.98 E-value: 3.45e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 446929194 153 TADGELNIEDIKQTINDKTKIVAIAHiSNVLGTINDVKTIAEIAHQHGA--IISVD 206
Cdd:PRK00451 187 YEDGVTDLEALEAAVDDDTAAVVVQY-PNFFGVIEDLEEIAEIAHAGGAlfIVGVD 241
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
69-406 |
7.48e-06 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 47.71 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 69 SLATDGYENArETVRRFIN--AKYF--EEIIFTRGTTASiNLVAHSygdANVEEGDEIVVTEmehHANIVPWQQLAKRKN 144
Cdd:cd06502 22 NVGDDVYGED-PTTAKLEAraAELFgkEAALFVPSGTAA-NQLALA---AHTQPGGSVICHE---TAHIYTDEAGAPEFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 145 ATLKFIPM-TADGELNIEDIKQTI---ND----KTKIVAI--AHISNVLGTINDVKTIAEIAHQHGAIISVDGAQ---AA 211
Cdd:cd06502 94 SGVKLLPVpGENGKLTPEDLEAAIrprDDihfpPPSLVSLenTTEGGTVYPLDELKAISALAKENGLPLHLDGARlanAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 212 PHMKLDMQE--MNADFYSFSGHKMLGPTGIGVLFGKRELLQKMEPI--EFGGDMidfvSKydatwadlptkfeaGTPLIA 287
Cdd:cd06502 174 AALGVALKTykSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRrkQAGGGM----RQ--------------SGFLAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 288 QAIGLAEAIRYLERIGFDaiHKYEQELTiyayeqmsaiEGIEIYGPPKDrragvitfnlQDVHPHDVATAVDTEGVAVRA 367
Cdd:cd06502 236 AGLAALENDLWLRRLRHD--HEMARRLA----------EALEELGGLES----------EVQTNIVLLDPVEANAVFVEL 293
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446929194 368 GHHCAQPLMKWLNV----SSTARASFYIYNTKEDIDQLINALK 406
Cdd:cd06502 294 SKEAIERRGEGVLFyawgEGGVRFVTHWDTTEEDVDELLSALK 336
|
|
| MetC |
COG0626 |
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ... |
137-206 |
1.61e-05 |
|
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: 46.58 E-value: 1.61e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 137 QQLAKRKNATLKFIPMTadgelNIEDIKQTINDKTKIVAIAHISNVLGTINDVKTIAEIAHQHGAIISVD 206
Cdd:COG0626 115 DKVLARFGIEVTFVDPT-----DLAAVEAAIRPNTKLVFLETPSNPTLEVVDIAAIAAIAHAAGALLVVD 179
|
|
| PRK08363 |
PRK08363 |
alanine aminotransferase; Validated |
92-206 |
2.40e-05 |
|
alanine aminotransferase; Validated
Pssm-ID: 181402 Cd Length: 398 Bit Score: 46.34 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 92 EEIIFTRGTTASINLVahsYGdANVEEGDEIVVTEMEHHanivPWQQLAKRKNAT-LKFIPMTADG-ELNIEDIKQTIND 169
Cdd:PRK08363 94 DDVRVTAAVTEALQLI---FG-ALLDPGDEILIPGPSYP----PYTGLVKFYGGVpVEYRTIEEEGwQPDIDDIRKKITE 165
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446929194 170 KTKIVAIAHISNVLGTINDVKTIAEI---AHQHGAIISVD 206
Cdd:PRK08363 166 KTKAIAVINPNNPTGALYEKKTLKEIldiAGEHDLPVISD 205
|
|
| PRK08133 |
PRK08133 |
O-succinylhomoserine sulfhydrylase; Validated |
119-251 |
3.43e-05 |
|
O-succinylhomoserine sulfhydrylase; Validated
Pssm-ID: 181244 [Multi-domain] Cd Length: 390 Bit Score: 45.76 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 119 GDEIVVTEMEHHANIVPWQQLAKRKNATLKFIPMTadgelNIEDIKQTINDKTKIVAIAHISNVLGTINDVKTIAEIAHQ 198
Cdd:PRK08133 100 GDHVVSSRSLFGSTVSLFEKIFARFGIETTFVDLT-----DLDAWRAAVRPNTKLFFLETPSNPLTELADIAALAEIAHA 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446929194 199 HGAIISVDGAQAAPHMKLDMqEMNADFYSFSGHKMLGPTGI---GVLFGKRELLQK 251
Cdd:PRK08133 175 AGALLVVDNCFCTPALQQPL-KLGADVVIHSATKYLDGQGRvlgGAVVGSKELMEE 229
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
92-206 |
9.72e-05 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 44.16 E-value: 9.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 92 EEIIFTRGTTASINLVAHSYgdanVEEGDEIVvtemehhaNIVP-WQQL---AKRKNATLKFIPMT-ADGEL-NIEDIKQ 165
Cdd:PRK07324 81 ENILQTNGATGANFLVLYAL----VEPGDHVI--------SVYPtYQQLydiPESLGAEVDYWQLKeENGWLpDLDELRR 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446929194 166 TINDKTKIVAIAHISNVLGTINDV---KTIAEIAHQHGAIISVD 206
Cdd:PRK07324 149 LVRPNTKLICINNANNPTGALMDRaylEEIVEIARSVDAYVLSD 192
|
|
| PRK06225 |
PRK06225 |
pyridoxal phosphate-dependent aminotransferase; |
140-368 |
1.18e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235749 [Multi-domain] Cd Length: 380 Bit Score: 43.97 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 140 AKRKNATLKFIPM---TADGELNIEDIKQTINDKTKIVAIAHISNVLG---TINDVKTIAEIAHQHGAIISVD------- 206
Cdd:PRK06225 124 ASRFGAEVIEVPIyseECNYKLTPELVKENMDENTRLIYLIDPLNPLGssyTEEEIKEFAEIARDNDAFLLHDctyrdfa 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 207 -----GAQAAPhmkldmqEMNADFYSFSghKMLGPTG--IGVLFGKRellqkmepiefggDMIDFVSKYDATwaDLptkf 279
Cdd:PRK06225 204 rehtlAAEYAP-------EHTVTSYSFS--KIFGMAGlrIGAVVATP-------------DLIEVVKSIVIN--DL---- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 280 eaGTPLIAQA---IGLAEAIRYLERIgfDAIHKYEQELTiyaYEQMSAIEGIEIYGPPKDRRAGVITFNLQDVHPHDVAT 356
Cdd:PRK06225 256 --GTNVIAQEaaiAGLKVKDEWIDRI--RRTTFKNQKLI---KEAVDEIEGVFLPVYPSHGNMMVIDISEAGIDPEDLVE 328
|
250
....*....|..
gi 446929194 357 AVDTEGVAVRAG 368
Cdd:PRK06225 329 YLLERKIFVRQG 340
|
|
| ARO8 |
COG1167 |
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ... |
92-372 |
1.73e-04 |
|
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440781 [Multi-domain] Cd Length: 471 Bit Score: 43.66 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 92 EEIIFTRGTTASINLVAHSYGDAnveeGDEIVVTEMEHHANIvpwqQLAKRKNATLKFIPMTADGeLNIEDIKQTInDKT 171
Cdd:COG1167 171 DQILITSGAQQALDLALRALLRP----GDTVAVESPTYPGAL----AALRAAGLRLVPVPVDEDG-LDLDALEAAL-RRH 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 172 KIVAI---AHISNVLGTINDV---KTIAEIAHQHGAII---------SVDGAQAAPhmkldMQEMNAD---FY--SFSgh 231
Cdd:COG1167 241 RPRAVyvtPSHQNPTGATMSLerrRALLELARRHGVPIieddydselRYDGRPPPP-----LAALDAPgrvIYigSFS-- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 232 KMLGPT-GIGVLFGKRELLQKMEPIefggdmidfvsKYDATWadlptkfeaGTPLIAQAIgLAEairYLERIGFDAI--- 307
Cdd:COG1167 314 KTLAPGlRLGYLVAPGRLIERLARL-----------KRATDL---------GTSPLTQLA-LAE---FLESGHYDRHlrr 369
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446929194 308 --HKYEQeltiyAYEQMSAI------EGIEIYGPPkdrrAG---VITFNlQDVHPHDVATAVDTEGVAVRAGHHCA 372
Cdd:COG1167 370 lrREYRA-----RRDLLLAAlarhlpDGLRVTGPP----GGlhlWLELP-EGVDAEALAAAALARGILVAPGSAFS 435
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
150-271 |
3.04e-04 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 42.72 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 150 IPMTADGELNIEDIKQTI-NDKTKIVAI-AHI-SNVLGTINDVKTIAEIAHQHGA---IISVDGAQAAPHMKL--DMQEM 221
Cdd:PRK02769 137 ITSLPNGEIDYDDLISKIkENKNQPPIIfANIgTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPFvnNPPPF 216
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446929194 222 N----ADFYSFSGHKMLG-PTGIGVLFGKRELLQKMEpiefggDMIDFVSKYDAT 271
Cdd:PRK02769 217 SfadgIDSIAISGHKFIGsPMPCGIVLAKKKYVERIS------VDVDYIGSRDQT 265
|
|
| PRK08247 |
PRK08247 |
methionine biosynthesis PLP-dependent protein; |
159-235 |
3.42e-04 |
|
methionine biosynthesis PLP-dependent protein;
Pssm-ID: 181320 [Multi-domain] Cd Length: 366 Bit Score: 42.38 E-value: 3.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446929194 159 NIEDIKQTINDKTKIVAIAHISNVLGTINDVKTIAEIAHQHGAIISVDGAQAAPHMKLDMqEMNADFYSFSGHKMLG 235
Cdd:PRK08247 125 SLKAIEQAITPNTKAIFIETPTNPLMQETDIAAIAKIAKKHGLLLIVDNTFYTPVLQRPL-EEGADIVIHSATKYLG 200
|
|
| PRK07811 |
PRK07811 |
cystathionine gamma-synthase; Provisional |
159-215 |
3.51e-04 |
|
cystathionine gamma-synthase; Provisional
Pssm-ID: 236104 [Multi-domain] Cd Length: 388 Bit Score: 42.32 E-value: 3.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446929194 159 NIEDIKQTINDKTKIVAIAHISNVLGTINDVKTIAEIAHQHGAIISVDGAQAAPHMK 215
Cdd:PRK07811 135 DLDAVRAAITPRTKLIWVETPTNPLLSITDIAALAELAHDAGAKVVVDNTFASPYLQ 191
|
|
| GcvP1 |
COG0403 |
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ... |
140-206 |
5.59e-04 |
|
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440172 [Multi-domain] Cd Length: 442 Bit Score: 41.94 E-value: 5.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446929194 140 AKRKNATLKFIPMtADGELNIEDIKQTINDKTKIVAIAHiSNVLGTINDVKTIAEIAHQHGA--IISVD 206
Cdd:COG0403 176 AEPLGIEVVEVPD-EDGVTDLEALKALLDDDVAGVLVQY-PNFFGVIEDLRAIAEAAHAAGAlvIVAAD 242
|
|
| PRK07683 |
PRK07683 |
aminotransferase A; Validated |
71-196 |
5.72e-04 |
|
aminotransferase A; Validated
Pssm-ID: 236075 Cd Length: 387 Bit Score: 42.02 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 71 ATDGYENARETVRRFINAKYF------EEIIFTRGTTASINLVAHSYgdanVEEGDEIVVTemehhANIVP-WQQLAKRK 143
Cdd:PRK07683 63 HNAGLLELRKAACNFVKDKYDlhyspeSEIIVTIGASEAIDIAFRTI----LEPGTEVILP-----APIYPgYEPIIRLC 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446929194 144 NATLKFIPMTADG-ELNIEDIKQTINDKTKIVAIAHISNVLGTINDVKTIAEIA 196
Cdd:PRK07683 134 GAKPVFIDTRSTGfRLTAEALENAITEKTRCVVLPYPSNPTGVTLSKEELQDIA 187
|
|
| SelA |
pfam03841 |
L-seryl-tRNA selenium transferase; |
160-252 |
6.31e-04 |
|
L-seryl-tRNA selenium transferase;
Pssm-ID: 309101 Cd Length: 367 Bit Score: 41.56 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 160 IEDIKQTINDKTKIVAIAHISN--VLGTINDVKT--IAEIAHQHGAIISVD------------GAQAAPHMKLDMQEmNA 223
Cdd:pfam03841 126 LKDYEQAINENTALLMKVHTSNyrIQGFTKEVELaeLVELGHEKGLPVYEDlgsgslvdlsqyGLPKEPTVQELIAQ-GV 204
|
90 100
....*....|....*....|....*....
gi 446929194 224 DFYSFSGHKMLGPTGIGVLFGKRELLQKM 252
Cdd:pfam03841 205 DLVSFSGDKLLGGPQAGIIVGKKELIERI 233
|
|
| MET17 |
COG2873 |
O-acetylhomoserine/O-acetylserine sulfhydrylase, pyridoxal phosphate-dependent [Amino acid ... |
159-212 |
7.40e-04 |
|
O-acetylhomoserine/O-acetylserine sulfhydrylase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; O-acetylhomoserine/O-acetylserine sulfhydrylase, pyridoxal phosphate-dependent is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 442120 [Multi-domain] Cd Length: 428 Bit Score: 41.55 E-value: 7.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446929194 159 NIEDIKQTINDKTKIVAIAHISNVLGTINDVKTIAEIAHQHGAIISVDGAQAAP 212
Cdd:COG2873 137 DPEAFEAAIDPNTKAIFGETIGNPALDVLDIEAIAEIAHEHGVPLIVDNTFATP 190
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
24-204 |
8.07e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 41.38 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 24 KVNGKRLAYldstATSQTPMQVLNVLEDYYKRYNSNVHRgvhtlgslatdgyenaretvrrfinakyfEEIIFTRGTTAS 103
Cdd:PRK07568 54 NYDEEVLAY----SHSQGIPELREAFAKYYKKWGIDVEP-----------------------------DEILITNGGSEA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 104 INLVAHSYGDanveEGDEIVVTEmEHHANivpWQQLAKRKNATLKFIPMTADGEL---NIEDIKQTINDKTKIVAIAHIS 180
Cdd:PRK07568 101 ILFAMMAICD----PGDEILVPE-PFYAN---YNGFATSAGVKIVPVTTKIEEGFhlpSKEEIEKLITPKTKAILISNPG 172
|
170 180
....*....|....*....|....*...
gi 446929194 181 NVLGTI---NDVKTIAEIAHQHG-AIIS 204
Cdd:PRK07568 173 NPTGVVytkEELEMLAEIAKKHDlFLIS 200
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
76-235 |
8.09e-04 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 41.08 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 76 ENARETvrrFINAKYFeeiIFTRGTTASINLVahsyGDANVEEGDEIVVTEMEHHANIvpwqQLAKRKNATLKFIPMTAD 155
Cdd:cd00615 66 ELAARA---FGAKHTF---FLVNGTSSSNKAV----ILAVCGPGDKILIDRNCHKSVI----NGLVLSGAVPVYLKPERN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 156 GELNI------EDIKQTINDKTKIVAIAHIS-NVLGTINDVKTIAEIAHQHGAIISVDGAQAA-----PHMKLDMQEMNA 223
Cdd:cd00615 132 PYYGIaggippETFKKALIEHPDAKAAVITNpTYYGICYNLRKIVEEAHHRGLPVLVDEAHGAhfrfhPILPSSAAMAGA 211
|
170
....*....|..
gi 446929194 224 DFYSFSGHKMLG 235
Cdd:cd00615 212 DIVVQSTHKTLP 223
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
114-210 |
9.04e-04 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 41.21 E-value: 9.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 114 ANVEEGDEIVV-------TemehhANIVPWQqlakrkNATLKFI---PmtADGELNIEDIKQTINDKTKIVAIAHIsnvL 183
Cdd:COG0399 65 LGIGPGDEVITpaftfvaT-----ANAILYV------GATPVFVdidP--DTYNIDPEALEAAITPRTKAIIPVHL---Y 128
|
90 100
....*....|....*....|....*..
gi 446929194 184 GTINDVKTIAEIAHQHGAIISVDGAQA 210
Cdd:COG0399 129 GQPADMDAIMAIAKKHGLKVIEDAAQA 155
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
92-203 |
1.08e-03 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 40.88 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 92 EEIIFTRGTTASI-NLVAhsygdANVEEGDEIV------VTemehHANIVpwqQLAkrkNATLKFIPMTADG--ELNIED 162
Cdd:PRK05764 92 SQVIVTTGAKQALyNAFM-----ALLDPGDEVIipapywVS----YPEMV---KLA---GGVPVFVPTGEENgfKLTVEQ 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446929194 163 IKQTINDKTKIVAIAHISNVLGTI---NDVKTIAEIAHQHGAII 203
Cdd:PRK05764 157 LEAAITPKTKALILNSPSNPTGAVyspEELEAIADVAVEHDIWV 200
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
80-210 |
1.18e-03 |
|
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.
Pssm-ID: 395827 Cd Length: 360 Bit Score: 40.73 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 80 ETVRRFINAKYfeEIIFTRGTTAsINLVAHSYGdanVEEGDEIVVTEMEHHANIvpwqQLAKRKNATLKFIPMTAD-GEL 158
Cdd:pfam01041 31 RAFAAYLGVKH--AIAVSSGTAA-LHLALRALG---VGPGDEVITPSFTFVATA----NAALRLGAKPVFVDIDPDtYNI 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446929194 159 NIEDIKQTINDKTKIVAIAHIsnvLGTINDVKTIAEIAHQHGAIISVDGAQA 210
Cdd:pfam01041 101 DPEAIEAAITPRTKAIIPVHL---YGQPADMDAIRAIAARHGLPVIEDAAHA 149
|
|
| PRK07682 |
PRK07682 |
aminotransferase; |
79-206 |
1.31e-03 |
|
aminotransferase;
Pssm-ID: 181082 [Multi-domain] Cd Length: 378 Bit Score: 40.49 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 79 RETVRRFINAKYF------EEIIFTRGTTASINLVAHsygdANVEEGDEIVVTEmehhANIVPWQQLAKRKNATLKFIPM 152
Cdd:PRK07682 63 RQEIAKYLKKRFAvsydpnDEIIVTVGASQALDVAMR----AIINPGDEVLIVE----PSFVSYAPLVTLAGGVPVPVAT 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 446929194 153 TADG--ELNIEDIKQTINDKTKIVAIAHISNVLGTI---NDVKTIAEIAHQHGAIISVD 206
Cdd:PRK07682 135 TLENefKVQPAQIEAAITAKTKAILLCSPNNPTGAVlnkSELEEIAVIVEKHDLIVLSD 193
|
|
| PRK06234 |
PRK06234 |
methionine gamma-lyase; Provisional |
159-249 |
2.23e-03 |
|
methionine gamma-lyase; Provisional
Pssm-ID: 168478 [Multi-domain] Cd Length: 400 Bit Score: 39.81 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 159 NIEDIKQTINDKTKIVAIAHISNVLGTINDVKTIAEIAHQH--GAIISVDGAQAAPHMKLDMqEMNADFYSFSGHKMLGP 236
Cdd:PRK06234 138 NLEEVRNALKANTKVVYLETPANPTLKVTDIKAISNIAHENnkECLVFVDNTFCTPYIQRPL-QLGADVVVHSATKYLNG 216
|
90
....*....|....*.
gi 446929194 237 TG---IGVLFGKRELL 249
Cdd:PRK06234 217 HGdviAGFVVGKEEFI 232
|
|
| PRK09028 |
PRK09028 |
cystathionine beta-lyase; Provisional |
139-212 |
2.34e-03 |
|
cystathionine beta-lyase; Provisional
Pssm-ID: 181615 [Multi-domain] Cd Length: 394 Bit Score: 40.10 E-value: 2.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446929194 139 LAKRKNATLKFIPMTADGelniedIKQTINDKTKIVAIAHISNVLGTINDVKTIAEIAHQHGAIISVDGAQAAP 212
Cdd:PRK09028 121 LKGFGIETTYYDPMIGEG------IRELIRPNTKVLFLESPGSITMEVQDVPTLSRIAHEHDIVVMLDNTWASP 188
|
|
| PRK04366 |
PRK04366 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPB; |
150-208 |
3.49e-03 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPB;
Pssm-ID: 235292 Cd Length: 481 Bit Score: 39.33 E-value: 3.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446929194 150 IPMTADGELNIEDIKQTINDKTKIVAIAHiSNVLGTIN-DVKTIAEIAHQHGAIISVDGA 208
Cdd:PRK04366 188 IPSNEDGLVDLEALKAAVGEDTAALMLTN-PNTLGLFErNILEIAEIVHEAGGLLYYDGA 246
|
|
| YnbB |
COG4100 |
Cystathionine beta-lyase family protein involved in aluminum resistance [Inorganic ion ... |
148-206 |
3.72e-03 |
|
Cystathionine beta-lyase family protein involved in aluminum resistance [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 443276 Cd Length: 409 Bit Score: 39.32 E-value: 3.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446929194 148 KFIPMTADGELNIEDIKQTINDKTKIVAI----------AHisnvlgTINDVKTIAEIAHQH--GAIISVD 206
Cdd:COG4100 135 RQVPLTEDGKIDLEAIKKAINEKTKMVLIqrsrgyswrpSL------TIEEIGEIIKFVKSInpDVICFVD 199
|
|
| PRK05967 |
PRK05967 |
cystathionine beta-lyase; Provisional |
162-212 |
7.33e-03 |
|
cystathionine beta-lyase; Provisional
Pssm-ID: 235657 [Multi-domain] Cd Length: 395 Bit Score: 38.25 E-value: 7.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446929194 162 DIKQTINDKTKIV-AIAHISNVLgTINDVKTIAEIAHQHGAIISVDGAQAAP 212
Cdd:PRK05967 141 GIAKLMRPNTKVVhTEAPGSNTF-EMQDIPAIAEAAHRHGAIVMMDNTWATP 191
|
|
| |
