|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02414 |
PLN02414 |
glycine dehydrogenase (decarboxylating) |
55-823 |
0e+00 |
|
glycine dehydrogenase (decarboxylating)
Pssm-ID: 178035 [Multi-domain] Cd Length: 993 Bit Score: 1138.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 55 RLLERLLPRH------------DDFARRHIGPGDKDRREMLQALGLASIDELIEKTVPASIRlKRPLKLE---DPVCENE 119
Cdd:PLN02414 11 GLLRRLVNEQtrsisvealkpsDTFPRRHNSATPEEQKAMAEYCGFDSLDALIDATVPKSIR-LDSMKLSkydEGLTESQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 120 ILETLHAIASKNQIWRSYIGMGYYNCSVPQTILRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANAS 199
Cdd:PLN02414 90 MLEHMKSLASKNKVFKSYIGMGYYNTHVPPVILRNILENPGWYTQYTPYQAEIAQGRLESLLNYQTMITDLTGLPMSNAS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 200 LLDEATAAAEAMQLCHRHNKRKR--FFIDPRCHPQTIAVVQTRAKYRGVIVELKLPHEMDFSGKDVSGVLFQYPDTEGKV 277
Cdd:PLN02414 170 LLDEGTAAAEAMAMCNNILKGKKkkFLIASNCHPQTIDVCQTRADGLGLEVVVADEKDFDYSSGDVCGVLVQYPATDGEV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 278 EDFTELVERAHQTGSLTCCATDLLALCILRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVRESLVRMMPGRMVGVTR 357
Cdd:PLN02414 250 LDYAEFVKNAHANGVKVVMATDLLALTMLKPPGEWGADIVVGSAQRFGVPMGYGGPHAAFLATSQEYKRLMPGRIIGVSV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 358 DATGKEVYRLALQTREQHIRRDKATSNICTAQALLANMAAMFAIYHGSHGLQHIAKRVHNATLILSEGLKRAGHQLQHDL 437
Cdd:PLN02414 330 DSSGKPALRMAMQTREQHIRRDKATSNICTAQALLANMAAMYAVYHGPEGLKTIAQRVHGLAGVFAAGLKKLGFQVQSLP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 438 FFDTLKVQCGcSLKEVLGRAAQRQINFRLFDDGTLGISLDETVTEKDLDDLLWIFGCESSTELVAEGMGEEWRGLLGSSF 517
Cdd:PLN02414 410 FFDTVKVKCS-DADAIADAAAKVGINLRVVDANTVTVSFDETTTLEDVDKLFKVFAGGKPVPFTAESLAPEVDSSIPSSL 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 518 KRTSPFLTHQVFNSYHSETNLVRYMKKLENKDISLVHSMIPLGSCTMKLNSSSELTPITWREFANIHPFVPLDQAQGYQQ 597
Cdd:PLN02414 489 ARESPYLTHPIFNQYHSEHELLRYLHRLQNKDLSLVHSMIPLGSCTMKLNATTEMMPVTWPEFANIHPFAPVDQAQGYQE 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 598 LFQELEKDLCELTGYDRVSFQPNSGAQGEYAGLATIRAYLDQKGERHRTVCLIPKSAHGTNPASAYMAGMKIQPVEVDRY 677
Cdd:PLN02414 569 MFEDLGDLLCEITGFDSFSLQPNAGAAGEYAGLMVIRAYHLSRGDHHRNVCIIPVSAHGTNPASAAMCGMKIVVVGTDAK 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 678 GNIDVAHLKAMVDKHKENLAAIMITYPSTNGVFEENISDVCALIHQHGGQVYLDGANMNAQVGICRPGDFGSDVSHLNLH 757
Cdd:PLN02414 649 GNINIEELRKAAEAHKDNLAALMVTYPSTHGVYEEGIDEICDIIHDNGGQVYMDGANMNAQVGLTSPGFIGADVCHLNLH 728
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 758 KTFCIPHGGGGPGMGPIGVKKHLVPFLPSHPIV----CLKPnEDTWPVGTVSAAPWGSSSILPISWAYIK 823
Cdd:PLN02414 729 KTFCIPHGGGGPGMGPIGVKKHLAPFLPSHPVVptggIPRP-EKTQPLGTISAAPWGSALILPISYTYIA 797
|
|
| gcvP |
TIGR00461 |
glycine dehydrogenase (decarboxylating); This apparently ubiquitous enzyme is found in ... |
70-823 |
0e+00 |
|
glycine dehydrogenase (decarboxylating); This apparently ubiquitous enzyme is found in bacterial, mammalian and plant sources. The enzyme catalyzes the reaction: GLYCINE + LIPOYLPROTEIN = S-AMINOMETHYL-DIHYDROLIPOYLPROTEIN + CO2. It is part of the glycine decarboxylase multienzyme complex (GDC) consisting of four proteins P, H, L and T. Active site in E.coli is located as the (K) residues at position 713 of the SEED alignment. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273089 [Multi-domain] Cd Length: 939 Bit Score: 1011.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 70 RHIGPGDKDRREMLQALGLASIDELIEKTVPASIRLKRPLKLEDPVCENEILETLHAIASKNQIWRSYIGMGYYNCSVPQ 149
Cdd:TIGR00461 1 RHLGPGETEQRQMLQTLGFDTLNALIDQAVPPAIRFPRPLQLPAPQSEYGALAQLKSIASKNQVFRSYIGMGYYDTILPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 150 TILRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANASLLDEATAAAEAMQLCHRHNKRK--RFFIDP 227
Cdd:TIGR00461 81 VIQRNILENPGWYTAYTPYQPEISQGRLEALLNFQTVVMDLTGLEIANASLLDEGTAAAEAMALSYGVSKSKanAFFVAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 228 RCHPQTIAVVQTRAKYRGVIVELKLPHEMDFSgKDVSGVLFQYPDTEGKVEDFTELVERAHQTGSLTCCATDLLALCILR 307
Cdd:TIGR00461 161 DCHPQTIEVIKTRANPFGIEVIVGDHHTFSFS-TDVFGALLQYPATDGAIYDYRSLIDKLHSHKALVSVAADPMALTLLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 308 PPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVRESLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSNICT 387
Cdd:TIGR00461 240 PPGELGADIVVGSTQRFGVPMGYGGPHAAFFATKDEYQRKMPGRIVGVSKDAHGNTALRLALQTREQHIRRDKATSNICT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 388 AQALLANMAAMFAIYHGSHGLQHIAKRVHNATLILSEGLKRAGHQLQHDLFFDTLKVQCG-CSLKEVLGRAAQRQINFRL 466
Cdd:TIGR00461 320 AQVLLANMASMYGVYHGPTGLKNIALRIHQLTVILAIGLKRLNYSLNNDYFFDTLRVGVGeQSAPAILKAAEGRGINLRP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 467 FDDGTLGISLDETVTEKDLDDLLWIFGCESSTELVAEGMGEEWRGLLGSSFKRTSPFLTHQVFNSYHSETNLVRYMKKLE 546
Cdd:TIGR00461 400 LVPGEVGISLDETTTVQDVLDLWQVFAGKDNLPFTPEELWSDVKTSFPADLTRQDEILQDAVFNQYHSETEMLRYLHQLE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 547 NKDISLVHSMIPLGSCTMKLNSSSELTPITWREFANIHPFVPLDQAQGYQQLFQELEKDLCELTGYDRVSFQPNSGAQGE 626
Cdd:TIGR00461 480 SKDLALNTSMIPLGSCTMKLNATAEMMPITWPEFGKIHPFAPAGQTEGYQILIAQLEAWLGEITGFDAISLQPNSGAQGE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 627 YAGLATIRAYLDQKGERHRTVCLIPKSAHGTNPASAYMAGMKIQPVEVDRYGNIDVAHLKAMVDKHKENLAAIMITYPST 706
Cdd:TIGR00461 560 YAGLQVIRQYHESRGEEHRNICLIPESAHGTNPASAVMAGMQVVPVKCDGEGNIDLEDLTSKAEQYGDRLAALMVTYPST 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 707 NGVFEENISDVCALIHQHGGQVYLDGANMNAQVGICRPGDFGSDVSHLNLHKTFCIPHGGGGPGMGPIGVKKHLVPFLPS 786
Cdd:TIGR00461 640 HGVFEATIGTICDIVHRFGGQVYLDGANMNAQVGLTSPGDFGADVCHLNLHKTFCIPHGGGGPGMGPIGVKSHLQPFLPR 719
|
730 740 750
....*....|....*....|....*....|....*...
gi 564333277 787 HPIVCLKPNE-DTWPVGTVSAAPWGSSSILPISWAYIK 823
Cdd:TIGR00461 720 HSLNSTAELQgEDQSIGMVSAAPYGSASILPISWMYIA 757
|
|
| GDC-P |
pfam02347 |
Glycine cleavage system P-protein; This family consists of Glycine cleavage system P-proteins ... |
69-492 |
0e+00 |
|
Glycine cleavage system P-protein; 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 catalyzed by this protein is:- Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2
Pssm-ID: 396772 [Multi-domain] Cd Length: 428 Bit Score: 766.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 69 RRHIGPGDKDRREMLQALGLASIDELIEKTVPASIRLKRPLKLEDPVCENEILETLHAIASKNQIWRSYIGMGYYNCSVP 148
Cdd:pfam02347 1 DRHIGPSEKDQQEMLATLGYSSLDDLIGKAVPKNIRFAKPLQLPAPKSEYEALAELEAIASKNTVYRSFIGMGYYDTILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 149 QTILRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANASLLDEATAAAEAMQLCHRHNKRK--RFFID 226
Cdd:pfam02347 81 PVILRNILENPEWYTAYTPYQPEISQGRLEALLNFQTMICDLTGLDIANASLLDEGTAAAEAMALAARASKKKgkKFVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 227 PRCHPQTIAVVQTRAKYRGVIVELKLPHEMDFSG-KDVSGVLFQYPDTEGKVEDFTELVERAHQTGSLTCCATDLLALCI 305
Cdd:pfam02347 161 KDVHPQTLEVLKTRAKPFGIEIVEVDYTEEGVTDlKDVFGVLVQYPNTDGRIEDYKELIELAHQRKSLVVVAADLLALTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 306 LRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVRESLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSNI 385
Cdd:pfam02347 241 LKPPGEFGADIAVGSAQRFGVPLGYGGPHAGFFAVKKELVRKMPGRLVGVSKDANGKRALRLALQTREQHIRRDKATSNI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 386 CTAQALLANMAAMFAIYHGSHGLQHIAKRVHNATLILSEGLKRAGHQLQHDLFFDTLKVQCG-CSLKEVLGRAAQRQINF 464
Cdd:pfam02347 321 CTAQALLANMASMYAVYHGPNGLKEIARRIHSLTLYLAKALKKLGHELVHKHFFDTLLIEVEdKAVEEVLARAEARGINL 400
|
410 420
....*....|....*....|....*...
gi 564333277 465 RLFDDGTLGISLDETVTEKDLDDLLWIF 492
Cdd:pfam02347 401 RYVDLGHVGIALDETVTKEDIDDLLQVF 428
|
|
| GcvP1 |
COG0403 |
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ... |
65-493 |
0e+00 |
|
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: 656.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 65 DDFARRHIGPGDKDRREMLQALGLASIDELIEKtVPASIRLKRPLKLEDPVCENEILETLHAIASKNQIWRSYIGMGYYN 144
Cdd:COG0403 1 DEFAMRYIPPTEEDRAEMLAAIGVDSLDELFDD-IPAEIRLKRPLDLPEALSEAELLRHLRALAAKNKVLTSFIGAGYYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 145 CSVPQTIlRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANASLLDEATAAAEAMQLCHRHNKR-KRF 223
Cdd:COG0403 80 HYVPAVV-RNILERPEFYTAYTPYQPEISQGRLQALFEFQTMVAELTGMDVANASLYDGATAAAEAMLMARRVTKRsNKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 224 FIDPRCHPQTIAVVQTRAKYRGV-IVELKLPH-EMDFS------GKDVSGVLFQYPDTEGKVEDFTELVERAHQTGSLTC 295
Cdd:COG0403 159 LVSEDVHPQTRAVLKTYAEPLGIeVVEVPDEDgVTDLEalkallDDDVAGVLVQYPNFFGVIEDLRAIAEAAHAAGALVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 296 CATDLLALCILRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVRESLVRMMPGRMVGVTRDATGKEVYRLALQTREQH 375
Cdd:COG0403 239 VAADPLSLGLLKPPGELGADIVVGEGQRLGVPLGFGGPHAGFFATREKLVRQMPGRLVGVTVDADGKRAFRLTLQTREQH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 376 IRRDKATSNICTAQALLANMAAMFAIYHGSHGLQHIAKRVHNATLILSEGLKRAGHQLQ-HDLFFDTLKVQCGCSLKEVL 454
Cdd:COG0403 319 IRREKATSNICTNQALLALAASMYAVYHGPEGLKEIAERIHQKAHYLAERLAALGVEVPfNGPFFDEFVVRLPKPAAEIN 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 564333277 455 GRAAQRQI----NFRLFDDGTLGISLDETVTEKDLDDLLWIFG 493
Cdd:COG0403 399 AALLEKGIlgglNLRRVDDDTLLVAVTETTTKEDIDALVEALA 441
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
117-492 |
6.17e-177 |
|
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: 516.40 E-value: 6.17e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 117 ENEILETLHAIASKNQIWR---SYIGMGYYNCSVPQTILRNLLENsGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGL 193
Cdd:cd00613 1 ETEVLRHLKRLASKNKALDqsmSFLGSGTYKHNPPAVIKRNILEN-EFYTAYTPYQPEISQGRLQALFELQTMLCELTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 194 DMANASLLDEATAAAEAMQLCHRHNK--RKRFFIDPRCHPQTIAVVQTRAKYRGV-IVELKLPHEM--------DFSGKD 262
Cdd:cd00613 80 DVANASLQDEATAAAEAAGLAAIRAYhkRNKVLVPDSAHPTNPAVARTRGEPLGIeVVEVPSDEGGtvdlealkEEVSEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 263 VSGVLFQYPDTEGKVEDF-TELVERAHQTGSLTCCATDLLALCILRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVR 341
Cdd:cd00613 160 VAALMVQYPNTLGVFEDLiKEIADIAHSAGALVYVDGDNLNLTGLKPPGEYGADIVVGNLQKTGVPHGGGGPGAGFFAVK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 342 ESLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSNICTAQALLANMAAMFAIYHGSHGLQHIAKRVHNATLI 421
Cdd:cd00613 240 KELVRFLPGRLVGVTKDAEGNRAFRLALQTREQHIRREKATSNICTGQALLALMAAMYIVYLGPEGLKEIAERAHLNANY 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564333277 422 LSEGLKRAGHQLQ-HDLFFDTLKVQCGC---SLKEVLGRAAQRQINFR----LFDDGTLGISLDETVTEKDLDDLLWIF 492
Cdd:cd00613 320 LAKRLKEVGGVLPfNGPFFHEFVLRLPPlygIRAEDLAKALIDGGFHAptmyLPVDGTLMIEPTETETKEELDALLEAL 398
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02414 |
PLN02414 |
glycine dehydrogenase (decarboxylating) |
55-823 |
0e+00 |
|
glycine dehydrogenase (decarboxylating)
Pssm-ID: 178035 [Multi-domain] Cd Length: 993 Bit Score: 1138.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 55 RLLERLLPRH------------DDFARRHIGPGDKDRREMLQALGLASIDELIEKTVPASIRlKRPLKLE---DPVCENE 119
Cdd:PLN02414 11 GLLRRLVNEQtrsisvealkpsDTFPRRHNSATPEEQKAMAEYCGFDSLDALIDATVPKSIR-LDSMKLSkydEGLTESQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 120 ILETLHAIASKNQIWRSYIGMGYYNCSVPQTILRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANAS 199
Cdd:PLN02414 90 MLEHMKSLASKNKVFKSYIGMGYYNTHVPPVILRNILENPGWYTQYTPYQAEIAQGRLESLLNYQTMITDLTGLPMSNAS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 200 LLDEATAAAEAMQLCHRHNKRKR--FFIDPRCHPQTIAVVQTRAKYRGVIVELKLPHEMDFSGKDVSGVLFQYPDTEGKV 277
Cdd:PLN02414 170 LLDEGTAAAEAMAMCNNILKGKKkkFLIASNCHPQTIDVCQTRADGLGLEVVVADEKDFDYSSGDVCGVLVQYPATDGEV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 278 EDFTELVERAHQTGSLTCCATDLLALCILRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVRESLVRMMPGRMVGVTR 357
Cdd:PLN02414 250 LDYAEFVKNAHANGVKVVMATDLLALTMLKPPGEWGADIVVGSAQRFGVPMGYGGPHAAFLATSQEYKRLMPGRIIGVSV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 358 DATGKEVYRLALQTREQHIRRDKATSNICTAQALLANMAAMFAIYHGSHGLQHIAKRVHNATLILSEGLKRAGHQLQHDL 437
Cdd:PLN02414 330 DSSGKPALRMAMQTREQHIRRDKATSNICTAQALLANMAAMYAVYHGPEGLKTIAQRVHGLAGVFAAGLKKLGFQVQSLP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 438 FFDTLKVQCGcSLKEVLGRAAQRQINFRLFDDGTLGISLDETVTEKDLDDLLWIFGCESSTELVAEGMGEEWRGLLGSSF 517
Cdd:PLN02414 410 FFDTVKVKCS-DADAIADAAAKVGINLRVVDANTVTVSFDETTTLEDVDKLFKVFAGGKPVPFTAESLAPEVDSSIPSSL 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 518 KRTSPFLTHQVFNSYHSETNLVRYMKKLENKDISLVHSMIPLGSCTMKLNSSSELTPITWREFANIHPFVPLDQAQGYQQ 597
Cdd:PLN02414 489 ARESPYLTHPIFNQYHSEHELLRYLHRLQNKDLSLVHSMIPLGSCTMKLNATTEMMPVTWPEFANIHPFAPVDQAQGYQE 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 598 LFQELEKDLCELTGYDRVSFQPNSGAQGEYAGLATIRAYLDQKGERHRTVCLIPKSAHGTNPASAYMAGMKIQPVEVDRY 677
Cdd:PLN02414 569 MFEDLGDLLCEITGFDSFSLQPNAGAAGEYAGLMVIRAYHLSRGDHHRNVCIIPVSAHGTNPASAAMCGMKIVVVGTDAK 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 678 GNIDVAHLKAMVDKHKENLAAIMITYPSTNGVFEENISDVCALIHQHGGQVYLDGANMNAQVGICRPGDFGSDVSHLNLH 757
Cdd:PLN02414 649 GNINIEELRKAAEAHKDNLAALMVTYPSTHGVYEEGIDEICDIIHDNGGQVYMDGANMNAQVGLTSPGFIGADVCHLNLH 728
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 758 KTFCIPHGGGGPGMGPIGVKKHLVPFLPSHPIV----CLKPnEDTWPVGTVSAAPWGSSSILPISWAYIK 823
Cdd:PLN02414 729 KTFCIPHGGGGPGMGPIGVKKHLAPFLPSHPVVptggIPRP-EKTQPLGTISAAPWGSALILPISYTYIA 797
|
|
| gcvP |
TIGR00461 |
glycine dehydrogenase (decarboxylating); This apparently ubiquitous enzyme is found in ... |
70-823 |
0e+00 |
|
glycine dehydrogenase (decarboxylating); This apparently ubiquitous enzyme is found in bacterial, mammalian and plant sources. The enzyme catalyzes the reaction: GLYCINE + LIPOYLPROTEIN = S-AMINOMETHYL-DIHYDROLIPOYLPROTEIN + CO2. It is part of the glycine decarboxylase multienzyme complex (GDC) consisting of four proteins P, H, L and T. Active site in E.coli is located as the (K) residues at position 713 of the SEED alignment. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273089 [Multi-domain] Cd Length: 939 Bit Score: 1011.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 70 RHIGPGDKDRREMLQALGLASIDELIEKTVPASIRLKRPLKLEDPVCENEILETLHAIASKNQIWRSYIGMGYYNCSVPQ 149
Cdd:TIGR00461 1 RHLGPGETEQRQMLQTLGFDTLNALIDQAVPPAIRFPRPLQLPAPQSEYGALAQLKSIASKNQVFRSYIGMGYYDTILPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 150 TILRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANASLLDEATAAAEAMQLCHRHNKRK--RFFIDP 227
Cdd:TIGR00461 81 VIQRNILENPGWYTAYTPYQPEISQGRLEALLNFQTVVMDLTGLEIANASLLDEGTAAAEAMALSYGVSKSKanAFFVAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 228 RCHPQTIAVVQTRAKYRGVIVELKLPHEMDFSgKDVSGVLFQYPDTEGKVEDFTELVERAHQTGSLTCCATDLLALCILR 307
Cdd:TIGR00461 161 DCHPQTIEVIKTRANPFGIEVIVGDHHTFSFS-TDVFGALLQYPATDGAIYDYRSLIDKLHSHKALVSVAADPMALTLLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 308 PPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVRESLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSNICT 387
Cdd:TIGR00461 240 PPGELGADIVVGSTQRFGVPMGYGGPHAAFFATKDEYQRKMPGRIVGVSKDAHGNTALRLALQTREQHIRRDKATSNICT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 388 AQALLANMAAMFAIYHGSHGLQHIAKRVHNATLILSEGLKRAGHQLQHDLFFDTLKVQCG-CSLKEVLGRAAQRQINFRL 466
Cdd:TIGR00461 320 AQVLLANMASMYGVYHGPTGLKNIALRIHQLTVILAIGLKRLNYSLNNDYFFDTLRVGVGeQSAPAILKAAEGRGINLRP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 467 FDDGTLGISLDETVTEKDLDDLLWIFGCESSTELVAEGMGEEWRGLLGSSFKRTSPFLTHQVFNSYHSETNLVRYMKKLE 546
Cdd:TIGR00461 400 LVPGEVGISLDETTTVQDVLDLWQVFAGKDNLPFTPEELWSDVKTSFPADLTRQDEILQDAVFNQYHSETEMLRYLHQLE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 547 NKDISLVHSMIPLGSCTMKLNSSSELTPITWREFANIHPFVPLDQAQGYQQLFQELEKDLCELTGYDRVSFQPNSGAQGE 626
Cdd:TIGR00461 480 SKDLALNTSMIPLGSCTMKLNATAEMMPITWPEFGKIHPFAPAGQTEGYQILIAQLEAWLGEITGFDAISLQPNSGAQGE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 627 YAGLATIRAYLDQKGERHRTVCLIPKSAHGTNPASAYMAGMKIQPVEVDRYGNIDVAHLKAMVDKHKENLAAIMITYPST 706
Cdd:TIGR00461 560 YAGLQVIRQYHESRGEEHRNICLIPESAHGTNPASAVMAGMQVVPVKCDGEGNIDLEDLTSKAEQYGDRLAALMVTYPST 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 707 NGVFEENISDVCALIHQHGGQVYLDGANMNAQVGICRPGDFGSDVSHLNLHKTFCIPHGGGGPGMGPIGVKKHLVPFLPS 786
Cdd:TIGR00461 640 HGVFEATIGTICDIVHRFGGQVYLDGANMNAQVGLTSPGDFGADVCHLNLHKTFCIPHGGGGPGMGPIGVKSHLQPFLPR 719
|
730 740 750
....*....|....*....|....*....|....*...
gi 564333277 787 HPIVCLKPNE-DTWPVGTVSAAPWGSSSILPISWAYIK 823
Cdd:TIGR00461 720 HSLNSTAELQgEDQSIGMVSAAPYGSASILPISWMYIA 757
|
|
| GDC-P |
pfam02347 |
Glycine cleavage system P-protein; This family consists of Glycine cleavage system P-proteins ... |
69-492 |
0e+00 |
|
Glycine cleavage system P-protein; 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 catalyzed by this protein is:- Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2
Pssm-ID: 396772 [Multi-domain] Cd Length: 428 Bit Score: 766.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 69 RRHIGPGDKDRREMLQALGLASIDELIEKTVPASIRLKRPLKLEDPVCENEILETLHAIASKNQIWRSYIGMGYYNCSVP 148
Cdd:pfam02347 1 DRHIGPSEKDQQEMLATLGYSSLDDLIGKAVPKNIRFAKPLQLPAPKSEYEALAELEAIASKNTVYRSFIGMGYYDTILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 149 QTILRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANASLLDEATAAAEAMQLCHRHNKRK--RFFID 226
Cdd:pfam02347 81 PVILRNILENPEWYTAYTPYQPEISQGRLEALLNFQTMICDLTGLDIANASLLDEGTAAAEAMALAARASKKKgkKFVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 227 PRCHPQTIAVVQTRAKYRGVIVELKLPHEMDFSG-KDVSGVLFQYPDTEGKVEDFTELVERAHQTGSLTCCATDLLALCI 305
Cdd:pfam02347 161 KDVHPQTLEVLKTRAKPFGIEIVEVDYTEEGVTDlKDVFGVLVQYPNTDGRIEDYKELIELAHQRKSLVVVAADLLALTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 306 LRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVRESLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSNI 385
Cdd:pfam02347 241 LKPPGEFGADIAVGSAQRFGVPLGYGGPHAGFFAVKKELVRKMPGRLVGVSKDANGKRALRLALQTREQHIRRDKATSNI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 386 CTAQALLANMAAMFAIYHGSHGLQHIAKRVHNATLILSEGLKRAGHQLQHDLFFDTLKVQCG-CSLKEVLGRAAQRQINF 464
Cdd:pfam02347 321 CTAQALLANMASMYAVYHGPNGLKEIARRIHSLTLYLAKALKKLGHELVHKHFFDTLLIEVEdKAVEEVLARAEARGINL 400
|
410 420
....*....|....*....|....*...
gi 564333277 465 RLFDDGTLGISLDETVTEKDLDDLLWIF 492
Cdd:pfam02347 401 RYVDLGHVGIALDETVTKEDIDDLLQVF 428
|
|
| GcvP1 |
COG0403 |
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ... |
65-493 |
0e+00 |
|
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: 656.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 65 DDFARRHIGPGDKDRREMLQALGLASIDELIEKtVPASIRLKRPLKLEDPVCENEILETLHAIASKNQIWRSYIGMGYYN 144
Cdd:COG0403 1 DEFAMRYIPPTEEDRAEMLAAIGVDSLDELFDD-IPAEIRLKRPLDLPEALSEAELLRHLRALAAKNKVLTSFIGAGYYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 145 CSVPQTIlRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANASLLDEATAAAEAMQLCHRHNKR-KRF 223
Cdd:COG0403 80 HYVPAVV-RNILERPEFYTAYTPYQPEISQGRLQALFEFQTMVAELTGMDVANASLYDGATAAAEAMLMARRVTKRsNKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 224 FIDPRCHPQTIAVVQTRAKYRGV-IVELKLPH-EMDFS------GKDVSGVLFQYPDTEGKVEDFTELVERAHQTGSLTC 295
Cdd:COG0403 159 LVSEDVHPQTRAVLKTYAEPLGIeVVEVPDEDgVTDLEalkallDDDVAGVLVQYPNFFGVIEDLRAIAEAAHAAGALVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 296 CATDLLALCILRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVRESLVRMMPGRMVGVTRDATGKEVYRLALQTREQH 375
Cdd:COG0403 239 VAADPLSLGLLKPPGELGADIVVGEGQRLGVPLGFGGPHAGFFATREKLVRQMPGRLVGVTVDADGKRAFRLTLQTREQH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 376 IRRDKATSNICTAQALLANMAAMFAIYHGSHGLQHIAKRVHNATLILSEGLKRAGHQLQ-HDLFFDTLKVQCGCSLKEVL 454
Cdd:COG0403 319 IRREKATSNICTNQALLALAASMYAVYHGPEGLKEIAERIHQKAHYLAERLAALGVEVPfNGPFFDEFVVRLPKPAAEIN 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 564333277 455 GRAAQRQI----NFRLFDDGTLGISLDETVTEKDLDDLLWIFG 493
Cdd:COG0403 399 AALLEKGIlgglNLRRVDDDTLLVAVTETTTKEDIDALVEALA 441
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
117-492 |
6.17e-177 |
|
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: 516.40 E-value: 6.17e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 117 ENEILETLHAIASKNQIWR---SYIGMGYYNCSVPQTILRNLLENsGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGL 193
Cdd:cd00613 1 ETEVLRHLKRLASKNKALDqsmSFLGSGTYKHNPPAVIKRNILEN-EFYTAYTPYQPEISQGRLQALFELQTMLCELTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 194 DMANASLLDEATAAAEAMQLCHRHNK--RKRFFIDPRCHPQTIAVVQTRAKYRGV-IVELKLPHEM--------DFSGKD 262
Cdd:cd00613 80 DVANASLQDEATAAAEAAGLAAIRAYhkRNKVLVPDSAHPTNPAVARTRGEPLGIeVVEVPSDEGGtvdlealkEEVSEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 263 VSGVLFQYPDTEGKVEDF-TELVERAHQTGSLTCCATDLLALCILRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVR 341
Cdd:cd00613 160 VAALMVQYPNTLGVFEDLiKEIADIAHSAGALVYVDGDNLNLTGLKPPGEYGADIVVGNLQKTGVPHGGGGPGAGFFAVK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 342 ESLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSNICTAQALLANMAAMFAIYHGSHGLQHIAKRVHNATLI 421
Cdd:cd00613 240 KELVRFLPGRLVGVTKDAEGNRAFRLALQTREQHIRREKATSNICTGQALLALMAAMYIVYLGPEGLKEIAERAHLNANY 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564333277 422 LSEGLKRAGHQLQ-HDLFFDTLKVQCGC---SLKEVLGRAAQRQINFR----LFDDGTLGISLDETVTEKDLDDLLWIF 492
Cdd:cd00613 320 LAKRLKEVGGVLPfNGPFFHEFVLRLPPlygIRAEDLAKALIDGGFHAptmyLPVDGTLMIEPTETETKEELDALLEAL 398
|
|
| GcvP2 |
COG1003 |
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport ... |
512-837 |
7.38e-173 |
|
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440627 Cd Length: 468 Bit Score: 508.42 E-value: 7.38e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 512 LLGSSFKRTSPflthqVFNSYHSETNLVRYMKKLENKDISLVHSMIPLGSCTMKLNSSSELTPITWREFANIHPFVPLDQ 591
Cdd:COG1003 13 LLPEALLRKSP-----VFLPEVSETEVLRHYTRLSQKNLGLDTGMIPLGSCTMKYNPKINEEPATLPGFANLHPFQPEET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 592 AQGYQQLFQELEKDLCELTGYDRVSFQPNSGAQGEYAGLATIRAYLDQKGERHRTVCLIPKSAHGTNPASAYMAGMKIQP 671
Cdd:COG1003 88 VQGYLELMYELEEWLAEITGMDAVSLQPNAGAQGEYAGLLAIRAYHESRGEGHRNEILIPDSAHGTNPASAAMAGFKVVV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 672 VEVDRYGNIDVAHLKAMVDkhkENLAAIMITYPSTNGVFEENISDVCALIHQHGGQVYLDGANMNAQVGICRPGDFGSDV 751
Cdd:COG1003 168 VKSDEDGNVDLEDLKAKVG---DRTAALMLTNPSTHGVFEEDIKEICDIVHEAGGLVYYDGANLNAIVGLARPGDMGFDV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 752 SHLNLHKTFCIphggggpgmgpigVKKHLVPFLPSHPIVclkPNEDTWPVGT-------VSAAPWGSSSILPISWAYIKT 824
Cdd:COG1003 245 CHLNLHKTFSTphggggpgsgpvgVKEHLAPFLPGPPVV---KDGDKYRLDYdrpksigRSAAFYGNAGVLVRAYAYIRM 321
|
330
....*....|....*..
gi 564333277 825 ----PLSSVSHASVLAA 837
Cdd:COG1003 322 mgaeGLREATEVAVLNA 338
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
76-488 |
2.42e-125 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 385.26 E-value: 2.42e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 76 DKDRREMLQALGLASIDELIEKtVPASIRLKRPLKLEDPVCENEILETLHAIASKNQIWR---SYIGMGYYNCSVPqTIL 152
Cdd:PRK00451 9 EEDIREMLDAIGVKSIDELFAD-IPEELRLKRPLDLPPGLSEMELLRHLRELAAKNKTAEeypSFLGAGAYDHYIP-AVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 153 RNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANASLLDEATAAAEAMQLCHRHNKRKRFFIDPRCHPQ 232
Cdd:PRK00451 87 DHIISRSEFYTAYTPYQPEISQGTLQAIFEYQTMICELTGMDVANASMYDGATALAEAALMAVRITKRKKVLVSGAVHPE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 233 TIAVVQTRAKYRGV-IVELKLPHEM-------DFSGKDVSGVLFQYPDTEGKVEDFTELVERAHQTGSLTCCATDLLALC 304
Cdd:PRK00451 167 YREVLKTYLKGQGIeVVEVPYEDGVtdlealeAAVDDDTAAVVVQYPNFFGVIEDLEEIAEIAHAGGALFIVGVDPVSLG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 305 ILRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVRESLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSN 384
Cdd:PRK00451 247 LLKPPGEYGADIVVGEGQPLGIPLSFGGPYLGFFATRKKLVRQMPGRLVGETVDADGKRGFVLTLQAREQHIRREKATSN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 385 ICTAQALLANMAAMFAIYHGSHGLQHIAKRVHNATLILSEGLKRAGHQLQHDL-FFDTLKVQCGCSLKEVLGRAAQRQI- 462
Cdd:PRK00451 327 ICTNQALNALAAAIYMSLLGPEGLRELAEQNHQKAHYLAERLAEIGGVELFDGpFFNEFVVRLPKPAEEVNEALLEKGIl 406
|
410 420 430
....*....|....*....|....*....|...
gi 564333277 463 -------NFRLFDDGTLgISLDETVTEKDLDDL 488
Cdd:PRK00451 407 ggydlgrYYPELGNHLL-VCVTEKRTKEDIDAL 438
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
535-824 |
2.76e-104 |
|
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: 328.42 E-value: 2.76e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 535 ETNLVRYMKKLENKDISLVHSMIPLGSCTMKLNSSSELTPITWR-EFANIHPFVPLDQAQGYQQLFQELEKDLCELTGYD 613
Cdd:cd00613 1 ETEVLRHLKRLASKNKALDQSMSFLGSGTYKHNPPAVIKRNILEnEFYTAYTPYQPEISQGRLQALFELQTMLCELTGMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 614 --RVSFQPNSGAQGEYAGLATIRAYLdqkgerHRTVCLIPKSAHGTNPASAYMA----GMKIQPVEVDRYGNIDvahLKA 687
Cdd:cd00613 81 vaNASLQDEATAAAEAAGLAAIRAYH------KRNKVLVPDSAHPTNPAVARTRgeplGIEVVEVPSDEGGTVD---LEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 688 MVDKHKENLAAIMITYPSTNGVFEENISDVCALIHQHGGQVYLDGANMNAQvGICRPGDFGSDVSHLNLHKTF------- 760
Cdd:cd00613 152 LKEEVSEEVAALMVQYPNTLGVFEDLIKEIADIAHSAGALVYVDGDNLNLT-GLKPPGEYGADIVVGNLQKTGvphgggg 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 761 ------CiphggggpgmgpigVKKHLVPFLPSHPIVCLKPNEDTwPVGTVSAA---------------PWGSSSILPISW 819
Cdd:cd00613 231 pgagffA--------------VKKELVRFLPGRLVGVTKDAEGN-RAFRLALQtreqhirrekatsniCTGQALLALMAA 295
|
....*
gi 564333277 820 AYIKT 824
Cdd:cd00613 296 MYIVY 300
|
|
| PRK04366 |
PRK04366 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPB; |
534-837 |
2.07e-89 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPB;
Pssm-ID: 235292 Cd Length: 481 Bit Score: 292.02 E-value: 2.07e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 534 SETNLVRYMKKLENKDISLVHSMIPLGSCTMKLNssseltP-ITWR-----EFANIHPFVPLDQAQGYQQLFQELEKDLC 607
Cdd:PRK04366 50 SELEVVRHYTRLSQKNYGVDTGFYPLGSCTMKYN------PkINEKvarlpGFAELHPLQPEETVQGALELMYELQEWLK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 608 ELTGYDRVSFQPNSGAQGEYAGLATIRAYLDQKGERHRTVCLIPKSAHGTNPASAYMAGMKIQPVEVDRYGNIDVAHLKA 687
Cdd:PRK04366 124 EITGMDAVTLQPAAGAHGELTGLLMIRAYHEARGDTKRTEVIVPDSAHGTNPASAAMAGFKVVEIPSNEDGLVDLEALKA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 688 MVDkhkENLAAIMITYPSTNGVFEENISDVCALIHQHGGQVYLDGANMNAQVGICRPGDFGSDVSHLNLHKTFCIPHGGG 767
Cdd:PRK04366 204 AVG---EDTAALMLTNPNTLGLFERNILEIAEIVHEAGGLLYYDGANLNAILGKARPGDMGFDVVHLNLHKTFSTPHGGG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 768 GPGMGPIGVKKHLVPFLPsHPIVclKPNEDTW--------PVGTVSAApWGSSSILPISWAYIKT----PLSSVSHASVL 835
Cdd:PRK04366 281 GPGSGPVGVKEELAPFLP-VPVV--EKDGDRYrldydrpkSIGRVRAF-YGNFGVLVRAYAYIRSlgaeGLREVSEDAVL 356
|
..
gi 564333277 836 AA 837
Cdd:PRK04366 357 NA 358
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
598-761 |
1.73e-12 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 66.25 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 598 LFQELEKDLCELT--GYDRVSFQPnSGAQGEYAGLATIRayldqkgERHRTVcLIPKSAHGTNPAS-AYMAGMKIQPVEV 674
Cdd:cd01494 1 KLEELEEKLARLLqpGNDKAVFVP-SGTGANEAALLALL-------GPGDEV-IVDANGHGSRYWVaAELAGAKPVPVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 675 DRYGNiDVAHLKAMVD-KHKENLAAIMITYPSTNGVFEENISDVCALIHQHGGQVYLDGANMNAQVGI--CRPGDFGSDV 751
Cdd:cd01494 72 DDAGY-GGLDVAILEElKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPApgVLIPEGGADV 150
|
170
....*....|
gi 564333277 752 SHLNLHKTFC 761
Cdd:cd01494 151 VTFSLHKNLG 160
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
590-733 |
2.16e-06 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 50.29 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 590 DQAQGYQQLFQELEKDLCELTGYDRVSFQPnSGAQGEYAGLATirayLDQKGerHRTVCLIPksAHG---TNPASAYMAG 666
Cdd:pfam01212 25 DEVYGGDPTVNRLEDRVAELFGKEAALFVP-SGTAANQLALMA----HCQRG--DEVICGEP--AHIhfdETGGHAELGG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564333277 667 MKIQPVEVDRYGNIDVAHLKAMVDKHK----ENLAAIMITypSTNG------VFEENISDVCALIHQHGGQVYLDGA 733
Cdd:pfam01212 96 VQPRPLDGDEAGNMDLEDLEAAIREVGadifPPTGLISLE--NTHNsaggqvVSLENLREIAALAREHGIPVHLDGA 170
|
|
| GcvP1 |
COG0403 |
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ... |
592-751 |
3.34e-05 |
|
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: 47.33 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 592 AQG-------YQQLfqelekdLCELTG--------YDrvsfqpnsGAQ--GEYAGLAtIRAyldqkGERHRTVcLIPKSA 654
Cdd:COG0403 107 SQGrlqalfeFQTM-------VAELTGmdvanaslYD--------GATaaAEAMLMA-RRV-----TKRSNKV-LVSEDV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 655 HgtnPAS-----AYMAGMKIQPVEVDRY-GNIDVAHLKAMVDkhkENLAAIMITYPSTNGVFEEnISDVCALIHQHGGQV 728
Cdd:COG0403 165 H---PQTravlkTYAEPLGIEVVEVPDEdGVTDLEALKALLD---DDVAGVLVQYPNFFGVIED-LRAIAEAAHAAGALV 237
|
170 180
....*....|....*....|...
gi 564333277 729 YLdGANMNAQVGICRPGDFGSDV 751
Cdd:COG0403 238 IV-AADPLSLGLLKPPGELGADI 259
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
592-751 |
3.25e-04 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 43.97 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 592 AQGYQQL---FQELekdLCELTGYDrVSfqpNS----GAQ--GEYAGLAtIRAyldqkgERHRTVcLIPKSAHgtnPAS- 661
Cdd:PRK00451 107 SQGTLQAifeYQTM---ICELTGMD-VA---NAsmydGATalAEAALMA-VRI------TKRKKV-LVSGAVH---PEYr 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 662 ------AYMAGMKIQPVEVDRyGNIDVAHLKAMVDkhkENLAAIMITYPSTNGVFEEnISDVCALIHQHGGQVYLdGANM 735
Cdd:PRK00451 169 evlktyLKGQGIEVVEVPYED-GVTDLEALEAAVD---DDTAAVVVQYPNFFGVIED-LEEIAEIAHAGGALFIV-GVDP 242
|
170
....*....|....*.
gi 564333277 736 NAQVGICRPGDFGSDV 751
Cdd:PRK00451 243 VSLGLLKPPGEYGADI 258
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
627-733 |
6.10e-04 |
|
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: 42.96 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 627 YAGLAT---IRAYLDQKGER--HRTVCLIPKSAHGTNPASAYMAGMKIQPVEVDRYGNIDVAHLKAMVDKHK-ENLAAIM 700
Cdd:cd06450 72 LALLAArdrARKRLKAGGGRgiDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEDKaEGLNPIM 151
|
90 100 110
....*....|....*....|....*....|....*.
gi 564333277 701 I--TYPSTN-GVFeENISDVCALIHQHGGQVYLDGA 733
Cdd:cd06450 152 VvaTAGTTDtGAI-DPLEEIADLAEKYDLWLHVDAA 186
|
|
| tnaA |
PRK13238 |
tryptophanase; |
678-733 |
2.38e-03 |
|
tryptophanase;
Pssm-ID: 237314 Cd Length: 460 Bit Score: 41.34 E-value: 2.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564333277 678 GNIDVAHLKAMVDKH-KENLAAIMITypSTNG------VFEENISDVCALIHQHGGQVYLDGA 733
Cdd:PRK13238 159 GNFDLEKLEALIEEVgAENVPFIVMT--ITNNsaggqpVSMANLRAVYEIAKKYGIPVVIDAA 219
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
590-733 |
8.96e-03 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 39.24 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564333277 590 DQAQGYQQLFQELEKDLCELTGYDRVSFQPNsgaqGEYAGLATIRAYLDQKGErhrtvCLIPKSAHGTNP---ASAYMAG 666
Cdd:cd06502 25 DDVYGEDPTTAKLEARAAELFGKEAALFVPS----GTAANQLALAAHTQPGGS-----VICHETAHIYTDeagAPEFLSG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564333277 667 MKIQPVEVDRyGNIDV----AHLKAMVDKHKENLAAIMITyPSTNG---VFEENISDVCALIHQHGGQVYLDGA 733
Cdd:cd06502 96 VKLLPVPGEN-GKLTPedleAAIRPRDDIHFPPPSLVSLE-NTTEGgtvYPLDELKAISALAKENGLPLHLDGA 167
|
|
|