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Conserved domains on  [gi|1419359305|gb|AXA73603|]
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DegT/DnrJ/EryC1/StrS family aminotransferase [Achromobacter insolitus]

Protein Classification

DegT/DnrJ/EryC1/StrS family aminotransferase( domain architecture ID 10001360)

DegT/DnrJ/EryC1/StrS family aminotransferase such as Bacillus subtilis 3-oxo-glucose-6-phosphate:glutamate aminotransferase and Saccharopolyspora erythraea erythromycin biosynthesis sensory transduction protein EryC1

CATH:  3.40.640.10|3.90.1150.10
EC:  2.6.1.-
Gene Ontology:  GO:0008483
PubMed:  17109392
SCOP:  4000675

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
13-360 5.61e-165

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440168  Cd Length: 364  Bit Score: 465.31  E-value: 5.61e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  13 RIKDKIDAGIQRVLAHGQFILGPEVAELEQKLAAYAGTEFCISCANGTDALQIVQMALGIGPGDEVITPGFNYIATAESV 92
Cdd:COG0399     8 SIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVATANAI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  93 VLLGAKPVYVDVDPRTCNLDPAKLEAAITPRTKAIIPVSLYGQCADLDAINAVAERHGIPVIEDAAQSYGATYKGRKSCN 172
Cdd:COG0399    88 LYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKGKKVGT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 173 LSAISCTSFFPSKPLGCyGDGGAIFTNDPDLARVIRQIARHGQDR--RYHHVRIGVNSRLDTLQAAILLPKLELLDEELA 250
Cdd:COG0399   168 FGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDRdaKYEHVELGYNYRMDELQAAIGLAQLKRLDEFIA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 251 LRDQVAASYTAAFHAAGFTDTPYVADGNVSAWAQYTILVP---HRAALQEHLKAQGIPTAVHYPIPLNKQPAVRD---DS 324
Cdd:COG0399   247 RRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDegeDRDELIAALKARGIGTRVHYPIPLHLQPAYRDlgyRP 326

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1419359305 325 VSLPVGDSLAEKVMSLPMHPYLTTDLVQQIVQAVAQ 360
Cdd:COG0399   327 GDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIRE 362
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
13-360 5.61e-165

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 465.31  E-value: 5.61e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  13 RIKDKIDAGIQRVLAHGQFILGPEVAELEQKLAAYAGTEFCISCANGTDALQIVQMALGIGPGDEVITPGFNYIATAESV 92
Cdd:COG0399     8 SIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVATANAI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  93 VLLGAKPVYVDVDPRTCNLDPAKLEAAITPRTKAIIPVSLYGQCADLDAINAVAERHGIPVIEDAAQSYGATYKGRKSCN 172
Cdd:COG0399    88 LYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKGKKVGT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 173 LSAISCTSFFPSKPLGCyGDGGAIFTNDPDLARVIRQIARHGQDR--RYHHVRIGVNSRLDTLQAAILLPKLELLDEELA 250
Cdd:COG0399   168 FGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDRdaKYEHVELGYNYRMDELQAAIGLAQLKRLDEFIA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 251 LRDQVAASYTAAFHAAGFTDTPYVADGNVSAWAQYTILVP---HRAALQEHLKAQGIPTAVHYPIPLNKQPAVRD---DS 324
Cdd:COG0399   247 RRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDegeDRDELIAALKARGIGTRVHYPIPLHLQPAYRDlgyRP 326

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1419359305 325 VSLPVGDSLAEKVMSLPMHPYLTTDLVQQIVQAVAQ 360
Cdd:COG0399   327 GDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIRE 362
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 22-358 1.14e-144

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: 413.48  E-value: 1.14e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  22 IQRVLAHGQFILGPEVAELEQKLAAYAGTEFCISCANGTDALQIVQMALGIGPGDEVITPGFNYIATAESVVLLGAKPVY 101
Cdd:cd00616     5 VEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGATPVF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 102 VDVDPRTCNLDPAKLEAAITPRTKAIIPVSLYGQCADLDAINAVAERHGIPVIEDAAQSYGATYKGRKSCNLSAISCTSF 181
Cdd:cd00616    85 VDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAGAFSF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 182 FPSKPLgCYGDGGAIFTNDPDLARVIRQIARHGQDRRYH---HVRIGVNSRLDTLQAAILLPKLELLDEELALRDQVAAS 258
Cdd:cd00616   165 HPTKNL-TTGEGGAVVTNDEELAERARLLRNHGRDRDRFkyeHEILGYNYRLSEIQAAIGLAQLEKLDEIIARRREIAER 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 259 YTAAFHAAGFTDTPYVADGNVSAWAQYTILVP-----HRAALQEHLKAQGIPTAVHYPIPLNKQPAVRD---DSVSLPVG 330
Cdd:cd00616   244 YKELLADLPGIRLPDVPPGVKHSYHLYVIRLDpeageSRDELIEALKEAGIETRVHYPPLHHQPPYKKLlgyPPGDLPNA 323

                         330       340
                  ....*....|....*....|....*...
gi 1419359305 331 DSLAEKVMSLPMHPYLTTDLVQQIVQAV 358
Cdd:cd00616   324 EDLAERVLSLPLHPSLTEEEIDRVIEAL 351
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 12-358 6.43e-140

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: 401.66  E-value: 6.43e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  12 NRIKDKIDAGIQRVLAHGQFILGPEVAELEQKLAAYAGTEFCISCANGTDALQIVQMALGIGPGDEVITPGFNYIATAES 91
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  92 VVLLGAKPVYVDVDPRTCNLDPAKLEAAITPRTKAIIPVSLYGQCADLDAINAVAERHGIPVIEDAAQSYGATYKGRKSC 171
Cdd:pfam01041  81 ALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 172 NLSAISCTSFFPSKPLgCYGDGGAIFTNDPDLARVIRQIARHG----QDRRYHHVRIGVNSRLDTLQAAILLPKLELLDE 247
Cdd:pfam01041 161 TLGDAATFSFHPTKNL-TTGEGGAVVTNDPELAEKARVLRNHGmvrkADKRYWHEVLGYNYRMTEIQAAIGLAQLERLDE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 248 ELALRDQVAASYTAAFHAA-GFTDTPYVADGNVSAWAQYTILVP----HRAALQEHLKAQGIPTAVHYPIPLNKQPAVRD 322
Cdd:pfam01041 240 FIARRREIAALYQTLLADLpGFTPLTTPPEADVHAWHLFPILVPeeaiNRDELVEALKEAGIGTRVHYPIPLHLQPYYRD 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1419359305 323 D----SVSLPVGDSLAEKVMSLPMHPYLTTDLVQQIVQAV 358
Cdd:pfam01041 320 LfgyaPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAV 359
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
20-364 7.25e-69

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 221.05  E-value: 7.25e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  20 AGIQRVLAHGQFILGPEVAELEQKLAAYAGTEFCISCANGTDALQIVQMALGIGPGDEVITPGFNYIATAESVVLLGAKP 99
Cdd:PRK11658   18 AAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWVSTLNMIVLLGATP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 100 VYVDVDPRTCNLDPAKLEAAITPRTKAIIPVSLYGQCADLDAINAVAERHGIPVIEDAAQSYGATYKGRKSCNlSAISCT 179
Cdd:PRK11658   98 VMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYYKGRHIGA-RGTAIF 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 180 SFFPSKPLGCyGDGGAIFTNDPDLARVIRQIARHGQ-----DRRYHH-------VRIGVNSRLDTLQAAILLPKLELLDE 247
Cdd:PRK11658  177 SFHAIKNITC-AEGGLVVTDDDELADRLRSLKFHGLgvdafDRQTQGrapqaevLTPGYKYNLADINAAIALVQLAKLEA 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 248 ELALRDQVAASYTAAFHAAGFTDTPYVADGNVSAWAQYTILVPH------RAALQEHLKAQGIPTAVHYpIPLNKQPAVR 321
Cdd:PRK11658  256 LNARRREIAARYLQALADLPFQPLSLPAWPHQHAWHLFIIRVDEercgisRDALMEALKERGIGTGLHF-RAAHTQKYYR 334

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1419359305 322 DD--SVSLPVGDSLAEKVMSLPMHPYLTTDLVQQIVQAVAQGIER 364
Cdd:PRK11658  335 ERfpTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIAGQ 379
am_tr_V_VC1184 TIGR01976
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ...
 44-159 2.38e-06

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: 48.98  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  44 LAAYAGtEFCIScANGTDALQIVQMALG--IGPGDEVITPGFNYIATAESVVLL----GAKPVYVDVDPRTCNLDPAKLE 117
Cdd:TIGR01976  73 LNADPP-EVVFG-ANATSLTFLLSRAISrrWGPGDEVIVTRLDHEANISPWLQAaeraGAKVKWARVDEATGELHPDDLA 150

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1419359305 118 AAITPRTK--AIIPVS-LYGQCADLDAINAVAERHGIPVIEDAAQ 159
Cdd:TIGR01976 151 SLLSPRTRlvAVTAASnTLGSIVDLAAITELVHAAGALVVVDAVH 195
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
13-360 5.61e-165

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 465.31  E-value: 5.61e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  13 RIKDKIDAGIQRVLAHGQFILGPEVAELEQKLAAYAGTEFCISCANGTDALQIVQMALGIGPGDEVITPGFNYIATAESV 92
Cdd:COG0399     8 SIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFVATANAI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  93 VLLGAKPVYVDVDPRTCNLDPAKLEAAITPRTKAIIPVSLYGQCADLDAINAVAERHGIPVIEDAAQSYGATYKGRKSCN 172
Cdd:COG0399    88 LYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKGKKVGT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 173 LSAISCTSFFPSKPLGCyGDGGAIFTNDPDLARVIRQIARHGQDR--RYHHVRIGVNSRLDTLQAAILLPKLELLDEELA 250
Cdd:COG0399   168 FGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDRdaKYEHVELGYNYRMDELQAAIGLAQLKRLDEFIA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 251 LRDQVAASYTAAFHAAGFTDTPYVADGNVSAWAQYTILVP---HRAALQEHLKAQGIPTAVHYPIPLNKQPAVRD---DS 324
Cdd:COG0399   247 RRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDegeDRDELIAALKARGIGTRVHYPIPLHLQPAYRDlgyRP 326

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1419359305 325 VSLPVGDSLAEKVMSLPMHPYLTTDLVQQIVQAVAQ 360
Cdd:COG0399   327 GDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIRE 362
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 22-358 1.14e-144

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: 413.48  E-value: 1.14e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  22 IQRVLAHGQFILGPEVAELEQKLAAYAGTEFCISCANGTDALQIVQMALGIGPGDEVITPGFNYIATAESVVLLGAKPVY 101
Cdd:cd00616     5 VEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGATPVF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 102 VDVDPRTCNLDPAKLEAAITPRTKAIIPVSLYGQCADLDAINAVAERHGIPVIEDAAQSYGATYKGRKSCNLSAISCTSF 181
Cdd:cd00616    85 VDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAGAFSF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 182 FPSKPLgCYGDGGAIFTNDPDLARVIRQIARHGQDRRYH---HVRIGVNSRLDTLQAAILLPKLELLDEELALRDQVAAS 258
Cdd:cd00616   165 HPTKNL-TTGEGGAVVTNDEELAERARLLRNHGRDRDRFkyeHEILGYNYRLSEIQAAIGLAQLEKLDEIIARRREIAER 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 259 YTAAFHAAGFTDTPYVADGNVSAWAQYTILVP-----HRAALQEHLKAQGIPTAVHYPIPLNKQPAVRD---DSVSLPVG 330
Cdd:cd00616   244 YKELLADLPGIRLPDVPPGVKHSYHLYVIRLDpeageSRDELIEALKEAGIETRVHYPPLHHQPPYKKLlgyPPGDLPNA 323

                         330       340
                  ....*....|....*....|....*...
gi 1419359305 331 DSLAEKVMSLPMHPYLTTDLVQQIVQAV 358
Cdd:cd00616   324 EDLAERVLSLPLHPSLTEEEIDRVIEAL 351
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 12-358 6.43e-140

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: 401.66  E-value: 6.43e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  12 NRIKDKIDAGIQRVLAHGQFILGPEVAELEQKLAAYAGTEFCISCANGTDALQIVQMALGIGPGDEVITPGFNYIATAES 91
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  92 VVLLGAKPVYVDVDPRTCNLDPAKLEAAITPRTKAIIPVSLYGQCADLDAINAVAERHGIPVIEDAAQSYGATYKGRKSC 171
Cdd:pfam01041  81 ALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 172 NLSAISCTSFFPSKPLgCYGDGGAIFTNDPDLARVIRQIARHG----QDRRYHHVRIGVNSRLDTLQAAILLPKLELLDE 247
Cdd:pfam01041 161 TLGDAATFSFHPTKNL-TTGEGGAVVTNDPELAEKARVLRNHGmvrkADKRYWHEVLGYNYRMTEIQAAIGLAQLERLDE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 248 ELALRDQVAASYTAAFHAA-GFTDTPYVADGNVSAWAQYTILVP----HRAALQEHLKAQGIPTAVHYPIPLNKQPAVRD 322
Cdd:pfam01041 240 FIARRREIAALYQTLLADLpGFTPLTTPPEADVHAWHLFPILVPeeaiNRDELVEALKEAGIGTRVHYPIPLHLQPYYRD 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1419359305 323 D----SVSLPVGDSLAEKVMSLPMHPYLTTDLVQQIVQAV 358
Cdd:pfam01041 320 LfgyaPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAV 359
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
20-364 7.25e-69

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 221.05  E-value: 7.25e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  20 AGIQRVLAHGQFILGPEVAELEQKLAAYAGTEFCISCANGTDALQIVQMALGIGPGDEVITPGFNYIATAESVVLLGAKP 99
Cdd:PRK11658   18 AAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTWVSTLNMIVLLGATP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 100 VYVDVDPRTCNLDPAKLEAAITPRTKAIIPVSLYGQCADLDAINAVAERHGIPVIEDAAQSYGATYKGRKSCNlSAISCT 179
Cdd:PRK11658   98 VMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYYKGRHIGA-RGTAIF 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 180 SFFPSKPLGCyGDGGAIFTNDPDLARVIRQIARHGQ-----DRRYHH-------VRIGVNSRLDTLQAAILLPKLELLDE 247
Cdd:PRK11658  177 SFHAIKNITC-AEGGLVVTDDDELADRLRSLKFHGLgvdafDRQTQGrapqaevLTPGYKYNLADINAAIALVQLAKLEA 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 248 ELALRDQVAASYTAAFHAAGFTDTPYVADGNVSAWAQYTILVPH------RAALQEHLKAQGIPTAVHYpIPLNKQPAVR 321
Cdd:PRK11658  256 LNARRREIAARYLQALADLPFQPLSLPAWPHQHAWHLFIIRVDEercgisRDALMEALKERGIGTGLHF-RAAHTQKYYR 334

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1419359305 322 DD--SVSLPVGDSLAEKVMSLPMHPYLTTDLVQQIVQAVAQGIER 364
Cdd:PRK11658  335 ERfpTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIAGQ 379
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 55-358 4.40e-65

TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional


Pssm-ID: 183283  Cd Length: 375  Bit Score: 210.85  E-value: 4.40e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  55 SCangTDALQIVQMALGIGPGDEVITPGFNYIATAESVVLLGAKPVYVDVDPRTCNLDPAKLEAAITPRTKAIIPVSLYG 134
Cdd:PRK11706   54 SC---TAALEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAG 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 135 QCADLDAINAVAERHGIPVIEDAAQSYGATYKGRKSCNLSAISCTSFFPSKPLGCyGDGGAIFTNDPDL---ARVIR--- 208
Cdd:PRK11706  131 VACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTA-GEGGALLINDPALierAEIIRekg 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 209 ----QIARhGQDRRYHHVRIGVNSRLDTLQAAILLPKLELLDEELALRDQVAASYTAAF---HAAGFTDTPYVADGNVSA 281
Cdd:PRK11706  210 tnrsQFFR-GQVDKYTWVDIGSSYLPSELQAAYLWAQLEAADRINQRRLALWQRYYDALaplAEAGRIELPSIPDDCKHN 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 282 WAQYTILVP---HRAALQEHLKAQGIPTAVHYpIPLNKQPAVRD---DSVSLPVGDSLAEKVMSLPMHPYLTTDLVQQIV 355
Cdd:PRK11706  289 AHMFYIKLRdleDRSALINFLKEAGIMAVFHY-IPLHSSPAGERfgrFHGEDRYTTKESERLLRLPLFYNLTDVEQRTVI 367


                  ...
gi 1419359305 356 QAV 358
Cdd:PRK11706  368 DTI 370
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
 34-216 4.46e-37

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 138.86  E-value: 4.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  34 GPEVAELEQKLAAYAGTEFCISCANGTDALQIVQMAL--------GIGPGDEVITPGFNYIATAESVVLLGAKPVYVDVD 105
Cdd:PRK15407   62 GRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFSALtspklgdrALKPGDEVITVAAGFPTTVNPIIQNGLVPVFVDVE 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 106 PRTCNLDPAKLEAAITPRTKAI-IPVSLyGQCADLDAINAVAERHGIPVIEDAAQSYGATYKGRKSCNLSAISCTSFFPS 184
Cdd:PRK15407  142 LPTYNIDASLLEAAVSPKTKAImIAHTL-GNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGRMTGTFGDIATLSFYPA 220

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1419359305 185 KPLgCYGDGGAIFTNDPDLARVIRQIARHGQD 216
Cdd:PRK15407  221 HHI-TMGEGGAVFTNDPLLKKIIESFRDWGRD 251
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 15-212 6.70e-17

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: 80.85  E-value: 6.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  15 KDKIDAGIQRVLAHGQFILGPEV--AELEQKLAAYAGTEFCISCAN--------GTDALQIVQMALgIGPGDEVITPGFN 84
Cdd:cd00609    14 PEVLEALAAAALRAGLLGYYPDPglPELREAIAEWLGRRGGVDVPPeeivvtngAQEALSLLLRAL-LNPGDEVLVPDPT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  85 YIATAESVVLLGAKPVYVDVDP-RTCNLDPAKLEAAITPRTKAII------PVslyGQC---ADLDAINAVAERHGIPVI 154
Cdd:cd00609    93 YPGYEAAARLAGAEVVPVPLDEeGGFLLDLELLEAAKTPKTKLLYlnnpnnPT---GAVlseEELEELAELAKKHGILII 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1419359305 155 EDAAqsYGA-TYKGRKSCNLSA-------ISCTSFfpSKPLGCYG-DGGAIFTNDPDLARVIRQIAR 212
Cdd:cd00609   170 SDEA--YAElVYDGEPPPALALldayervIVLRSF--SKTFGLPGlRIGYLIAPPEELLERLKKLLP 232
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 39-156 2.62e-16

Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 79.40  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  39 ELEQKLAAYAGTEF--------CISCANGTDALQIVQMALgIGPGDEVI--TPGF-NYiatAESVVLLGAKPVYVDVDPR 107
Cdd:COG0436    71 ELREAIAAYYKRRYgvdldpdeILVTNGAKEALALALLAL-LNPGDEVLvpDPGYpSY---RAAVRLAGGKPVPVPLDEE 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1419359305 108 T-CNLDPAKLEAAITPRTKAII------PV-SLYGQcADLDAINAVAERHGIPVIED 156
Cdd:COG0436   147 NgFLPDPEALEAAITPRTKAIVlnspnnPTgAVYSR-EELEALAELAREHDLLVISD 202
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 68-156 1.15e-15

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 77.47  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  68 MALgIGPGDEVITPGFNYIATAESVVLLGAKPVYVDVDPRT-CNLDPAKLEAAITPRTKAIIPVS-------LYGQcADL 139
Cdd:PRK05764  109 MAL-LDPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENgFKLTVEQLEAAITPKTKALILNSpsnptgaVYSP-EEL 186

                          90
                  ....*....|....*..
gi 1419359305 140 DAINAVAERHGIPVIED 156
Cdd:PRK05764  187 EAIADVAVEHDIWVLSD 203
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
2-214 2.29e-14

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 73.49  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305   2 IDFVDLKAQQNR---IKDKIDAGIQRVLAHGQFILGP--EVAELEQKLAAYAGTEFCIS--------CANGTDALQIVQM 68
Cdd:pfam00155   1 TDKINLGSNEYLgdtLPAVAKAEKDALAGGTRNLYGPtdGHPELREALAKFLGRSPVLKldreaavvFGSGAGANIEALI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  69 ALGIGPGDEVITPGFNYIATAESVVLLGAKPVYVDV-DPRTCNLDPAKLEAAITPRTKAIIPVSLY---GQ---CADLDA 141
Cdd:pfam00155  81 FLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPLyDSNDFHLDFDALEAALKEKPKVVLHTSPHnptGTvatLEELEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 142 INAVAERHGIPVIEDAAqsYGATYKGRKS-----CNLSA----ISCTSFfpSKPLGCYGDGGAIFTNDPDLARVIRQIAR 212
Cdd:pfam00155 161 LLDLAKEHNILLLVDEA--YAGFVFGSPDavatrALLAEgpnlLVVGSF--SKAFGLAGWRVGYILGNAAVISQLRKLAR 236


                  ..
gi 1419359305 213 HG 214
Cdd:pfam00155 237 PF 238
PRK07682 PRK07682
aminotransferase;
39-156 1.16e-13

aminotransferase;


Pssm-ID: 181082 [Multi-domain]  Cd Length: 378  Bit Score: 71.30  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  39 ELEQKLAAYAGTEFCISCANGTDALQIV--QMALGIG------PGDEVITPGFNYIATAESVVLLGAKPVYVDVDPRT-C 109
Cdd:PRK07682   61 ELRQEIAKYLKKRFAVSYDPNDEIIVTVgaSQALDVAmraiinPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENeF 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1419359305 110 NLDPAKLEAAITPRTKAII------PV-SLYGQcADLDAINAVAERHGIPVIED 156
Cdd:PRK07682  141 KVQPAQIEAAITAKTKAILlcspnnPTgAVLNK-SELEEIAVIVEKHDLIVLSD 193
PRK06108 PRK06108
pyridoxal phosphate-dependent aminotransferase;
37-156 1.42e-13

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180404  Cd Length: 382  Bit Score: 71.13  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  37 VAELEQKLAAYAGTEFCIS--------CANGTDALQIVQMALgIGPGDEVI--TPGF-NYIATAEsvvLLGAKPVYVDVD 105
Cdd:PRK06108   63 IPELREALARYVSRLHGVAtpperiavTSSGVQALMLAAQAL-VGPGDEVVavTPLWpNLVAAPK---ILGARVVCVPLD 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1419359305 106 PRT--CNLDPAKLEAAITPRTKAII------PVSLYGQCADLDAINAVAERHGIPVIED 156
Cdd:PRK06108  139 FGGggWTLDLDRLLAAITPRTRALFinspnnPTGWTASRDDLRAILAHCRRHGLWIVAD 197
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
53-160 1.27e-12

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 68.24  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  53 CISCANGTDALQIVQMALG-IGPGDEVITPGF----NYIATAESVVLLGAKPVYVDVDPrTCNLDPAKLEAAITPRTK-- 125
Cdd:COG0520    80 IIFTRGTTEAINLVAYGLGrLKPGDEILITEMehhsNIVPWQELAERTGAEVRVIPLDE-DGELDLEALEALLTPRTKlv 158

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1419359305 126 AIIPVS-LYGQCADLDAINAVAERHGIPVIEDAAQS 160
Cdd:COG0520   159 AVTHVSnVTGTVNPVKEIAALAHAHGALVLVDGAQS 194
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 37-199 2.30e-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: 64.71  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  37 VAELEQKLAAYAGT--EFCISCANGTDALQIVQMALGiGPGDEVITPGFNYIA-TAESVVLLGAKPVYVDVDPRTCNLDP 113
Cdd:cd01494     2 LEELEEKLARLLQPgnDKAVFVPSGTGANEAALLALL-GPGDEVIVDANGHGSrYWVAAELAGAKPVPVPVDDAGYGGLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 114 AKL--EAAITPRTKAII---PVSLYGQCADLDAINAVAERHGIPVIEDAAQSYGATY-KGRKSCNLSAISCTsFFPSKPL 187
Cdd:cd01494    81 VAIleELKAKPNVALIVitpNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPaPGVLIPEGGADVVT-FSLHKNL 159

                         170
                  ....*....|..
gi 1419359305 188 GCYGdGGAIFTN 199
Cdd:cd01494   160 GGEG-GGVVIVK 170
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 35-209 3.83e-12

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: 66.84  E-value: 3.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  35 PEVAELEQKLAAYAGTEFCISCANGTDALQIVQMALgIGPGDEVITPG------FNYIATAESvvLLGAKPVYVDVDprt 108
Cdd:cd00614    40 PTVDALEKKLAALEGGEAALAFSSGMAAISTVLLAL-LKAGDHVVASDdlyggtYRLFERLLP--KLGIEVTFVDPD--- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 109 cnlDPAKLEAAITPRTKAII---PVSLYGQCADLDAINAVAERHGIPVIEDA---------AQSYGAtykgrkscNLSAI 176
Cdd:cd00614   114 ---DPEALEAAIKPETKLVYvesPTNPTLKVVDIEAIAELAHEHGALLVVDNtfatpylqrPLELGA--------DIVVH 182

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1419359305 177 SCTSFfpskpLGCYGD--GGAIFTNDPDLARVIRQ 209
Cdd:cd00614   183 SATKY-----IGGHSDviAGVVVGSGEALIQRLRF 212
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
35-214 3.87e-12

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 66.09  E-value: 3.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  35 PEVAELEQKLAAYAGTEFCISCANGTDALQIVQMALgIGPGDEVIT--PGFNYIATAESVVLL-GAKPVYVDVdPRTCNL 111
Cdd:pfam01212  32 PTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAH-CQRGDEVICgePAHIHFDETGGHAELgGVQPRPLDG-DEAGNM 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 112 DPAKLEAAITPRTKAIIP----VSL-------YGQC---ADLDAINAVAERHGIPVIEDAAQSYGATykgrKSCNLSAIS 177
Cdd:pfam01212 110 DLEDLEAAIREVGADIFPptglISLenthnsaGGQVvslENLREIAALAREHGIPVHLDGARFANAA----VALGVIVKE 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1419359305 178 CTSFFP------SKPLGCyGDGGAIFTNDPDLARVIRQIARHG 214
Cdd:pfam01212 186 ITSYADsvtmclSKGLGA-PVGSVLAGSDDFIAKAIRQRKYLG 227
PRK05994 PRK05994
O-acetylhomoserine aminocarboxypropyltransferase; Validated
 32-156 1.38e-11

O-acetylhomoserine aminocarboxypropyltransferase; Validated


Pssm-ID: 180344 [Multi-domain]  Cd Length: 427  Bit Score: 65.50  E-value: 1.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  32 ILGPEVAELEQKLAAYAGTEFCISCANGtDALQIVQMALGIGPGDEVITPGFNYIAT----AESVVLLGAKPVYVDVDpr 107
Cdd:PRK05994   60 ITNPTNAVLEERVAALEGGTAALAVASG-HAAQFLVFHTLLQPGDEFIAARKLYGGSinqfGHAFKSFGWQVRWADAD-- 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1419359305 108 tcnlDPAKLEAAITPRTKAIIPVSLY---GQCADLDAINAVAERHGIPVIED 156
Cdd:PRK05994  137 ----DPASFERAITPRTKAIFIESIAnpgGTVTDIAAIAEVAHRAGLPLIVD 184
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
35-188 3.28e-10

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 60.98  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  35 PEVaelEQKLAAYAGTEFCIS---------C-ANGtdALQIVQMALgIGPGDEVIT--PGF----NYIATAesvvllGAK 98
Cdd:PRK06836   76 PEV---REAIAESLNRRFGTPltadhivmtCgAAG--ALNVALKAI-LNPGDEVIVfaPYFveyrFYVDNH------GGK 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  99 PVYVDVDPRTCNLDPAKLEAAITPRTKAII------PV-SLYGQcADLDAINAVAER------HGIPVIEDaaQSYGA-T 164
Cdd:PRK06836  144 LVVVPTDTDTFQPDLDALEAAITPKTKAVIinspnnPTgVVYSE-ETLKALAALLEEkskeygRPIYLISD--EPYREiV 220

                         170       180
                  ....*....|....*....|....*....
gi 1419359305 165 YKGRKSCNL-----SAISCTSFfpSKPLG 188
Cdd:PRK06836  221 YDGAEVPYIfkyydNSIVVYSF--SKSLS 247
PRK05957 PRK05957
pyridoxal phosphate-dependent aminotransferase;
35-167 7.57e-10

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235654  Cd Length: 389  Bit Score: 59.70  E-value: 7.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  35 PEVAELEQKLAAYAGTEF----CISCANGTDaLQIVQMALGI-GPGDEVITPGFNYIATAESVVLLGAKPVYVDVDpRTC 109
Cdd:PRK05957   69 PLLEAITQKLQQDNGIELnneqAIVVTAGSN-MAFMNAILAItDPGDEIILNTPYYFNHEMAITMAGCQPILVPTD-DNY 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1419359305 110 NLDPAKLEAAITPRTKAIIPVS-------LYGQcADLDAINAVAERHGIPVIEDAAQSYgATYKG 167
Cdd:PRK05957  147 QLQPEAIEQAITPKTRAIVTISpnnptgvVYPE-ALLRAVNQICAEHGIYHISDEAYEY-FTYDG 209
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 54-162 1.06e-08

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: 56.10  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  54 ISCANGTDALQIVQMALG--IGPGDEVITPGF----NYIATAESVVLLGAKPVYVDVDPRTcNLDPAKLEAAITPRTK-- 125
Cdd:pfam00266  65 IFTSGTTEAINLVALSLGrsLKPGDEIVITEMehhaNLVPWQELAKRTGARVRVLPLDEDG-LLDLDELEKLITPKTKlv 143

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1419359305 126 AIIPVS-LYGQCADLDAINAVAERHGIPVIEDAAQSYG 162
Cdd:pfam00266 144 AITHVSnVTGTIQPVPEIGKLAHQYGALVLVDAAQAIG 181
PRK09082 PRK09082
methionine aminotransferase; Validated
 28-156 1.09e-08

methionine aminotransferase; Validated


Pssm-ID: 181642 [Multi-domain]  Cd Length: 386  Bit Score: 56.08  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  28 HGQFILGPEVAELEQKLAA-----Y-----AGTEFCIScANGTDALQIVQMALgIGPGDEVITPGFNYIATAESVVLLGA 97
Cdd:PRK09082   60 HNQYPPMTGVAALREAIAAktarlYgrqydADSEITVT-AGATEALFAAILAL-VRPGDEVIVFDPSYDSYAPAIELAGG 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1419359305  98 KPVYVDVDPRTCNLDPAKLEAAITPRTKAII------PVSLYGQCADLDAINAVAERHGIPVIED 156
Cdd:PRK09082  138 RAVRVALQPPDFRVDWQRFAAAISPRTRLIIlntphnPSGTVWSAADMRALWQLIAGTDIYVLSD 202
PRK08247 PRK08247
methionine biosynthesis PLP-dependent protein;
40-156 1.48e-08

methionine biosynthesis PLP-dependent protein;


Pssm-ID: 181320 [Multi-domain]  Cd Length: 366  Bit Score: 55.86  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  40 LEQKLAAYAGTEFCISCANGTDALQIVqMALgIGPGDEVITP----GFNYIATAESVVLLGAKPVYVDvdprTCNLDpaK 115
Cdd:PRK08247   57 LEQAIADLEGGDQGFACSSGMAAIQLV-MSL-FRSGDELIVSsdlyGGTYRLFEEHWKKWNVRFVYVN----TASLK--A 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1419359305 116 LEAAITPRTKAII---PVSLYGQCADLDAINAVAERHGIPVIED 156
Cdd:PRK08247  129 IEQAITPNTKAIFietPTNPLMQETDIAAIAKIAKKHGLLLIVD 172
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 58-160 1.62e-08

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: 55.55  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  58 NGTDALQIVQMALG--IGPGDEVITpgfnyiATAE--SVVL--------LGAKPVYVDVDPrTCNLDPAKLEAAITPRTK 125
Cdd:cd06453    69 NTTEAINLVAYGLGraNKPGDEIVT------SVMEhhSNIVpwqqlaerTGAKLKVVPVDD-DGQLDLEALEKLLTERTK 141

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1419359305 126 --AIIPVS-LYGQCADLDAINAVAERHGIPVIEDAAQS 160
Cdd:cd06453   142 lvAVTHVSnVLGTINPVKEIGEIAHEAGVPVLVDGAQS 179
PRK07550 PRK07550
aminotransferase;
73-156 3.07e-08

aminotransferase;


Pssm-ID: 181026 [Multi-domain]  Cd Length: 386  Bit Score: 54.96  E-value: 3.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  73 GPGDEVITPG---FNYIATAEsvvLLGAKPVYVDVDPRTCNL-DPAKLEAAITPRTKAIIPVSLYGQC------ADLDAI 142
Cdd:PRK07550  112 GAGDEVILPLpwyFNHKMWLD---MLGIRPVYLPCDEGPGLLpDPAAAEALITPRTRAIALVTPNNPTgvvyppELLHEL 188

                          90
                  ....*....|....
gi 1419359305 143 NAVAERHGIPVIED 156
Cdd:PRK07550  189 YDLARRHGIALILD 202
PRK07777 PRK07777
putative succinyldiaminopimelate transaminase DapC;
23-156 5.08e-08

putative succinyldiaminopimelate transaminase DapC;


Pssm-ID: 236095 [Multi-domain]  Cd Length: 387  Bit Score: 54.27  E-value: 5.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  23 QRVLAHG--QFILGPEVAELEQKLAAY----------AGTEFCIScANGTDALQIVQMALgIGPGDEVITPGFNYIATAE 90
Cdd:PRK07777   47 QEAIAGGvnQYPPGPGIPELRAAIAAQrrrrygleydPDTEVLVT-VGATEAIAAAVLGL-VEPGDEVLLIEPYYDSYAA 124

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1419359305  91 SVVLLGAKPVYVDVDP--RTCNLDPAKLEAAITPRTKAII------PVSLYGQCADLDAINAVAERHGIPVIED 156
Cdd:PRK07777  125 VIAMAGAHRVPVPLVPdgRGFALDLDALRAAVTPRTRALIvnsphnPTGTVLTAAELAAIAELAVEHDLLVITD 198
PRK08248 PRK08248
homocysteine synthase;
32-156 1.04e-07

homocysteine synthase;


Pssm-ID: 236201 [Multi-domain]  Cd Length: 431  Bit Score: 53.31  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  32 ILGPEVAELEQKLAAYAGTEFCISCANGTDAL--QIVQMAlgiGPGDEVITP----GFNYIATAESVVLLGAKPVYVDVD 105
Cdd:PRK08248   61 IMNPTTDVFEKRIAALEGGIGALAVSSGQAAItySILNIA---SAGDEIVSSsslyGGTYNLFAHTLPKLGITVKFVDPS 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1419359305 106 prtcnlDPAKLEAAITPRTKAIIPVSL---YGQCADLDAINAVAERHGIPVIED 156
Cdd:PRK08248  138 ------DPENFEAAITDKTKALFAETIgnpKGDVLDIEAVAAIAHEHGIPLIVD 185
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
72-156 1.27e-07

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 52.80  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  72 IGPGDEVITPGFNYIATAESVVLLGAKPVYVD-VDPRTCNLDPAKLEAAITPRTKAII---PVSLYGQC---ADLDAINA 144
Cdd:PRK06348  110 LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAIIlnsPNNPTGAVfskETLEEIAK 189

                          90
                  ....*....|..
gi 1419359305 145 VAERHGIPVIED 156
Cdd:PRK06348  190 IAIEYDLFIISD 201
PRK08363 PRK08363
alanine aminotransferase; Validated
 60-156 3.21e-07

alanine aminotransferase; Validated


Pssm-ID: 181402  Cd Length: 398  Bit Score: 51.73  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  60 TDALQIVQMALgIGPGDEVITPGFNYIATAESVVLLGAKPV-YVDVDPRTCNLDPAKLEAAITPRTKAIIPVS------- 131
Cdd:PRK08363  103 TEALQLIFGAL-LDPGDEILIPGPSYPPYTGLVKFYGGVPVeYRTIEEEGWQPDIDDIRKKITEKTKAIAVINpnnptga 181

                          90       100
                  ....*....|....*....|....*
gi 1419359305 132 LYGQcADLDAINAVAERHGIPVIED 156
Cdd:PRK08363  182 LYEK-KTLKEILDIAGEHDLPVISD 205
PRK07683 PRK07683
aminotransferase A; Validated
 74-128 4.88e-07

aminotransferase A; Validated


Pssm-ID: 236075  Cd Length: 387  Bit Score: 51.26  E-value: 4.88e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1419359305  74 PGDEVITPGFNYIATAESVVLLGAKPVYVDVDPRTCNLDPAKLEAAITPRTKAII 128
Cdd:PRK07683  112 PGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEALENAITEKTRCVV 166
PRK06107 PRK06107
aspartate transaminase;
37-149 5.22e-07

aspartate transaminase;


Pssm-ID: 180403  Cd Length: 402  Bit Score: 51.27  E-value: 5.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  37 VAELEQKLA-AYAGTEFCIscanGTDALQIVQMAL--GIGPGDEVITPGFNYIATAESVVLLGAKPVYVDVDPRT-CNLD 112
Cdd:PRK06107   80 IAKLERRNGlHYADNEITV----GGGAKQAIFLALmaTLEAGDEVIIPAPYWVSYPDMVLANDGTPVIVACPEEQgFKLT 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1419359305 113 PAKLEAAITPRTKAII------PVSLYGQCADLDAINAVAERH 149
Cdd:PRK06107  156 PEALEAAITPRTRWLIlnapsnPTGAVYSRAELRALADVLLRH 198
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 42-158 7.13e-07

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: 50.32  E-value: 7.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  42 QKLAAYA-GTEFCISCANGTD-ALQIVQMALgIGPGDEVITPGFNYIATAESVVLLGAKPVYVD------------VDPR 107
Cdd:cd00615    65 QELAARAfGAKHTFFLVNGTSsSNKAVILAV-CGPGDKILIDRNCHKSVINGLVLSGAVPVYLKpernpyygiaggIPPE 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1419359305 108 TcnLDPAKLEAaitPRTKAII---PvSLYGQCADLDAINAVAERHGIPVIEDAA 158
Cdd:cd00615   144 T--FKKALIEH---PDAKAAVitnP-TYYGICYNLRKIVEEAHHRGLPVLVDEA 191
PRK08912 PRK08912
aminotransferase;
37-128 1.78e-06

aminotransferase;


Pssm-ID: 181580  Cd Length: 387  Bit Score: 49.59  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  37 VAELEQKLAAYAG----------TEFCIScANGTDALQIVQMALgIGPGDEVITPGFNYIATAESVVLLGAKPVYVDVDP 106
Cdd:PRK08912   65 LPELRQAVAAHYArfqgldldpeTEVMVT-SGATEALAAALLAL-VEPGDEVVLFQPLYDAYLPLIRRAGGVPRLVRLEP 142

                          90       100
                  ....*....|....*....|..
gi 1419359305 107 RTCNLDPAKLEAAITPRTKAII 128
Cdd:PRK08912  143 PHWRLPRAALAAAFSPRTKAVL 164
am_tr_V_VC1184 TIGR01976
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ...
 44-159 2.38e-06

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: 48.98  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  44 LAAYAGtEFCIScANGTDALQIVQMALG--IGPGDEVITPGFNYIATAESVVLL----GAKPVYVDVDPRTCNLDPAKLE 117
Cdd:TIGR01976  73 LNADPP-EVVFG-ANATSLTFLLSRAISrrWGPGDEVIVTRLDHEANISPWLQAaeraGAKVKWARVDEATGELHPDDLA 150

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1419359305 118 AAITPRTK--AIIPVS-LYGQCADLDAINAVAERHGIPVIEDAAQ 159
Cdd:TIGR01976 151 SLLSPRTRlvAVTAASnTLGSIVDLAAITELVHAAGALVVVDAVH 195
PRK12414 PRK12414
putative aminotransferase; Provisional
 20-156 1.15e-05

putative aminotransferase; Provisional


Pssm-ID: 183514  Cd Length: 384  Bit Score: 46.70  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  20 AGIQRVL--AHGQFILGPEVAELEQKLAAY----------AGTEFCIScANGTDALQIVQMALgIGPGDEVI--TPGFNy 85
Cdd:PRK12414   49 EGVARAMrdGHNQYAPMAGIAALREALAEKterlygarydPASEVTVI-ASASEGLYAAISAL-VHPGDEVIyfEPSFD- 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1419359305  86 iATAESVVLLGAKPVYVDVDPRTCNLDPAKLEAAITPRTKAII------PVSLYGQCADLDAINAVAERHGIPVIED 156
Cdd:PRK12414  126 -SYAPIVRLQGATPVAIKLSPEDFRVNWDEVAAAITPRTRMIIvntphnPSATVFSAADLARLAQLTRNTDIVILSD 201
PRK07568 PRK07568
pyridoxal phosphate-dependent aminotransferase;
59-156 2.29e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181036  Cd Length: 397  Bit Score: 46.00  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  59 GTDALQIVQMALgIGPGDEVITPG-F--NYIATAESvvlLGAKPVYVDVDPRTCNLDPAK--LEAAITPRTKAII----- 128
Cdd:PRK07568   97 GSEAILFAMMAI-CDPGDEILVPEpFyaNYNGFATS---AGVKIVPVTTKIEEGFHLPSKeeIEKLITPKTKAILisnpg 172

                          90       100       110
                  ....*....|....*....|....*....|
gi 1419359305 129 -PVS-LYGQcADLDAINAVAERHGIPVIED 156
Cdd:PRK07568  173 nPTGvVYTK-EELEMLAEIAKKHDLFLISD 201
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 86-162 3.61e-05

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: 45.42  E-value: 3.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  86 IATAESVVLLGAKPVYVDVDpRTCNLDPAKLEAAITPRTkaiIPVSL-Y-----GQCADLDAINAVAERHGIPVIEDAAQ 159
Cdd:COG1104   104 LETARFLEKEGFEVTYLPVD-EDGRVDLEALEAALRPDT---ALVSVmHannetGTIQPIAEIAEIAKEHGVLFHTDAVQ 179


                  ...
gi 1419359305 160 SYG 162
Cdd:COG1104   180 AVG 182
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 56-156 4.25e-05

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: 45.20  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  56 CANGTDALQIVQMALgIGPGDEVIT--PGF-NYIATAESvvlLGAKPVYVDVDPRtcNLDPAKLEAAI-TPRTKAIIPVS 131
Cdd:COG1167   176 TSGAQQALDLALRAL-LRPGDTVAVesPTYpGALAALRA---AGLRLVPVPVDED--GLDLDALEAALrRHRPRAVYVTP 249

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1419359305 132 LY----GQCADLD---AINAVAERHGIPVIED 156
Cdd:COG1167   250 SHqnptGATMSLErrrALLELARRHGVPIIED 281
PRK08133 PRK08133
O-succinylhomoserine sulfhydrylase; Validated
 35-150 4.73e-05

O-succinylhomoserine sulfhydrylase; Validated


Pssm-ID: 181244 [Multi-domain]  Cd Length: 390  Bit Score: 44.99  E-value: 4.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  35 PEVAELEQKLAAYAGTEFCISCANGTDALQIVQMALgIGPGDEVITPGFNYIATaesVVLL-------GAKPVYVDVDpr 107
Cdd:PRK08133   61 PTVTMFQERLAALEGAEACVATASGMAAILAVVMAL-LQAGDHVVSSRSLFGST---VSLFekifarfGIETTFVDLT-- 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1419359305 108 tcnlDPAKLEAAITPRTKAII---PVSLYGQCADLDAINAVAERHG 150
Cdd:PRK08133  135 ----DLDAWRAAVRPNTKLFFletPSNPLTELADIAALAEIAHAAG 176
PRK07811 PRK07811
cystathionine gamma-synthase; Provisional
 35-204 4.87e-05

cystathionine gamma-synthase; Provisional


Pssm-ID: 236104 [Multi-domain]  Cd Length: 388  Bit Score: 45.02  E-value: 4.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  35 PEVAELEQKLAAYAGTEFCISCANGTDALQIVQMALgIGPGDEVITPGFNYIAT----AESVVLLGAKPVYVDVDprtcn 110
Cdd:PRK07811   61 PTRTALEEQLAALEGGAYGRAFSSGMAATDCLLRAV-LRPGDHIVIPNDAYGGTfrliDKVFTRWGVEYTPVDLS----- 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 111 lDPAKLEAAITPRTKAI---IPVSLYGQCADLDAINAVAERHGIPVIEDA--AQSY-------GAtykgrkscNLSAISC 178
Cdd:PRK07811  135 -DLDAVRAAITPRTKLIwveTPTNPLLSITDIAALAELAHDAGAKVVVDNtfASPYlqqplalGA--------DVVVHST 205

                         170       180
                  ....*....|....*....|....*...
gi 1419359305 179 TsffpsKPLGCYGD--GGAIFTNDPDLA 204
Cdd:PRK07811  206 T-----KYIGGHSDvvGGALVTNDEELD 228
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 39-163 6.46e-05

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 44.47  E-value: 6.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  39 ELEQKLAAYAGTEFCISCANGTDALQIVQMALGiGPGDEVITPGFNYIATAESVVLLGA-KPVYVDVDPRTCNldpAKLE 117
Cdd:cd06454    50 ELEEELAEFHGKEAALVFSSGYAANDGVLSTLA-GKGDLIISDSLNHASIIDGIRLSGAkKRIFKHNDMEDLE---KLLR 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1419359305 118 AAITPRTKAIIPV-SLY---GQCADLDAINAVAERHGIPVIEDAAQSYGA 163
Cdd:cd06454   126 EARRPYGKKLIVTeGVYsmdGDIAPLPELVDLAKKYGAILFVDEAHSVGV 175
OKR_DC_1 pfam01276
Orn/Lys/Arg decarboxylase, major domain;
17-158 1.02e-04

Orn/Lys/Arg decarboxylase, major domain;


Pssm-ID: 396025 [Multi-domain]  Cd Length: 417  Bit Score: 44.03  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  17 KIDAGIQRVlAHGQfILGPEVAELE-QKLAAYA-GTEFCISCANGTD-ALQIVQMALgIGPGDEVITPGFNYIATAESVV 93
Cdd:pfam01276  48 RIDVCIEDV-ELGD-LLDHEGAIKEaQKYAARVfGADKSYFVVNGTSgSNKTVGMAV-CTPGDTILIDRNCHKSIHHALM 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  94 LLGAKPVYVD-----------VDPRTCNLDPAKLEAAITPRTK----AIIPVSLY-GQCADLDAINAVAERHGIPVIEDA 157
Cdd:pfam01276 125 LSGATPVYLEpsrnaygiiggIPLHEFQEETLKEAIAEVPDAKgprlAVITNPTYdGVLYNAKEIVDTLHHLSDPILFDS 204


                  .
gi 1419359305 158 A 158
Cdd:pfam01276 205 A 205
PLN02855 PLN02855
Bifunctional selenocysteine lyase/cysteine desulfurase
 58-160 2.04e-04

Bifunctional selenocysteine lyase/cysteine desulfurase


Pssm-ID: 215460 [Multi-domain]  Cd Length: 424  Bit Score: 43.20  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  58 NGTDALQIVQMALG---IGPGDEVItpgfnyIATAE---SVV---LL----GAKPVYVDVDPRTcNLDPAKLEAAITPRT 124
Cdd:PLN02855  102 NATEAINLVAYTWGlanLKPGDEVI------LSVAEhhsNIVpwqLVaqktGAVLKFVGLTPDE-VLDVEQLKELLSEKT 174

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1419359305 125 K--AIIPVS-LYGQCADLDAINAVAERHGIPVIEDAAQS 160
Cdd:PLN02855  175 KlvATHHVSnVLGSILPVEDIVHWAHAVGAKVLVDACQS 213
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 35-205 2.36e-04

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: 42.71  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  35 PEVAELEQKLAAYAGTEFCISCANGTDALQIVQMALgIGPGDEVITPGFNYIATAES---VVLLGAKPvyVDVDPRTCNL 111
Cdd:cd06502    32 PTTAKLEARAAELFGKEAALFVPSGTAANQLALAAH-TQPGGSVICHETAHIYTDEAgapEFLSGVKL--LPVPGENGKL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 112 DPAKLEAAIT-------PRTKAI-----IPVSLYGQCADLDAINAVAERHGIPVIEDAAQSYGA--TYKGRKSCNLSAIS 177
Cdd:cd06502   109 TPEDLEAAIRprddihfPPPSLVslentTEGGTVYPLDELKAISALAKENGLPLHLDGARLANAaaALGVALKTYKSGVD 188

                         170       180
                  ....*....|....*....|....*...
gi 1419359305 178 CTSFFPSKPLGCYgdGGAIFTNDPDLAR 205
Cdd:cd06502   189 SVSFCLSKGGGAP--VGAVVVGNRDFIA 214
PRK07309 PRK07309
pyridoxal phosphate-dependent aminotransferase;
60-167 3.05e-04

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235985  Cd Length: 391  Bit Score: 42.40  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  60 TDALQIVQMALgIGPGDEVITPGFNYIATAESVVLLGAKPVYVDVDPRTCNLDPAKLEAAITPR---TKAII------PV 130
Cdd:PRK07309  101 TEALSASLTAI-LEPGDKVLLPAPAYPGYEPIVNLVGAEIVEIDTTENDFVLTPEMLEKAILEQgdkLKAVIlnypanPT 179

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1419359305 131 SLYGQCADLDAINAVAERHGIPVIEDAAQSYgATYKG 167
Cdd:PRK07309  180 GVTYSREQIKALADVLKKYDIFVISDEVYSE-LTYTG 215
tnaA PRK13238
tryptophanase;
72-209 5.68e-04

tryptophanase;


Pssm-ID: 237314  Cd Length: 460  Bit Score: 41.72  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  72 IGPGDEVITpgfNYI--ATAESVVLLGAKPV--YVDV--DPRTC-----NLDPAKLEAAITP----RTKAII-------- 128
Cdd:PRK13238  114 IKKGDVVPS---NYHfdTTRAHIELNGATAVdlVIDEalDTGSRhpfkgNFDLEKLEALIEEvgaeNVPFIVmtitnnsa 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 129 ---PVSLygqcADLDAINAVAERHGIPVIEDAA---------QSYGATYKG-------RKSCNLSAISCTSffpSKPLGC 189
Cdd:PRK13238  191 ggqPVSM----ANLRAVYEIAKKYGIPVVIDAArfaenayfiKQREPGYKDksikeiaREMFSYADGLTMS---AKKDAM 263

                         170       180
                  ....*....|....*....|
gi 1419359305 190 YGDGGAIFTNDPDLARVIRQ 209
Cdd:PRK13238  264 VNIGGLLCFRDEDLFTECRT 283
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 18-165 6.58e-04

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: 41.12  E-value: 6.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  18 IDAGIQRVLAHgqfiLGPEVA----ELEQKLAAYAGTE----FCIScANGTDALQIVqMALGIGPGDEVITPGFNYIAT- 88
Cdd:cd06451    15 LKAMNRPMLGH----RSPEFLalmdEILEGLRYVFQTEngltFLLS-GSGTGAMEAA-LSNLLEPGDKVLVGVNGVFGDr 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  89 -AESVVLLGAKPVYVDVDPRTcNLDPAKLEAAIT-PRTKAIIPV---SLYGQCADLDAINAVAERHGIPVIEDAAQSYGA 163
Cdd:cd06451    89 wADMAERYGADVDVVEKPWGE-AVSPEEIAEALEqHDIKAVTLThneTSTGVLNPLEGIGALAKKHDALLIVDAVSSLGG 167


                  ..
gi 1419359305 164 TY 165
Cdd:cd06451   168 EP 169
PRK05939 PRK05939
cystathionine gamma-synthase family protein;
35-156 1.00e-03

cystathionine gamma-synthase family protein;


Pssm-ID: 235650 [Multi-domain]  Cd Length: 397  Bit Score: 40.83  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  35 PEVAELEQKLAAYAGTEFCISCANGTDALQIVQMALgIGPGDEVITPGF---NYIATAESVVLLGAKPVYVDVdprtcnL 111
Cdd:PRK05939   47 PTTAALEAKITKMEGGVGTVCFATGMAAIAAVFLTL-LRAGDHLVSSQFlfgNTNSLFGTLRGLGVEVTMVDA------T 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1419359305 112 DPAKLEAAITPRTKAII------PVSlygQCADLDAINAVAERHGIPVIED 156
Cdd:PRK05939  120 DVQNVAAAIRPNTRMVFvetianPGT---QVADLAGIGALCRERGLLYVVD 167
PRK09265 PRK09265
aminotransferase AlaT; Validated
 74-156 1.66e-03

aminotransferase AlaT; Validated


Pssm-ID: 181738  Cd Length: 404  Bit Score: 40.18  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  74 PGDEVITPGFNY-IATAeSVVLLGAKPVYVDVDPRT-CNLDPAKLEAAITPRTKAIIPV-------SLYGQcADLDAINA 144
Cdd:PRK09265  118 NGDEVLVPAPDYpLWTA-AVSLSGGKPVHYLCDEEAgWFPDLDDIRSKITPRTKAIVIInpnnptgAVYSK-ELLEEIVE 195

                          90
                  ....*....|..
gi 1419359305 145 VAERHGIPVIED 156
Cdd:PRK09265  196 IARQHNLIIFAD 207
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 94-163 2.11e-03

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: 39.49  E-value: 2.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1419359305  94 LLGAKPVYVDVDPRTcNLDPAKLEAAITPRTK---------AIIPVSLYGQCADLDAINAVAERHGIPVIEDAAqsYGA 163
Cdd:cd06450   114 YLDVKVRLVPVDEDG-RMDPEALEAAIDEDKAeglnpimvvATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAA--YGG 189
PRK05613 PRK05613
O-acetylhomoserine/O-acetylserine sulfhydrylase;
35-194 3.70e-03

O-acetylhomoserine/O-acetylserine sulfhydrylase;


Pssm-ID: 168128 [Multi-domain]  Cd Length: 437  Bit Score: 39.08  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  35 PEVAELEQKLAAYAGTEFCISCANGTDALQIVQMALGiGPGDEVITPGFNYIATaESVVLLGAKPVYVDVDPRTCNLDPA 114
Cdd:PRK05613   69 PTVEALENRIASLEGGVHAVAFASGQAAETAAILNLA-GAGDHIVTSPRLYGGT-ETLFLVTLNRLGIEVTFVENPDDPE 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305 115 KLEAAITPRTKAIIPVSLYGQCAD-LD--AINAVAERHGIPVIEDAAQSYGATYKGRK-SCNLSAISCTSFFPSKPLGCY 190
Cdd:PRK05613  147 SWQAAVQPNTKAFFGETFANPQADvLDipAVAEVAHRNQVPLIVDNTIATAALVRPLElGADVVVASLTKFYTGNGSGLG 226


                  ....*..
gi 1419359305 191 G---DGG 194
Cdd:PRK05613  227 GvliDGG 233
tyr_nico_aTase TIGR01265
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ...
 56-156 3.95e-03

tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley.


Pssm-ID: 188123  Cd Length: 403  Bit Score: 38.86  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  56 CANGTDALQIVQMALGIgPGDEVITP--GF-NYIATAEsvvllgakpvYVDVDPRTCNLDPAK--------LEAAITPRT 124
Cdd:TIGR01265 102 TSGCSQAIEICIEALAN-PGANILVPrpGFpLYDTRAA----------FSGLEVRLYDLLPEKdweidldgLESLADEKT 170

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1419359305 125 KAIIPVSLYGQCAD------LDAINAVAERHGIPVIED 156
Cdd:TIGR01265 171 VAIVVINPSNPCGSvfsrdhLQKIAEVAEKLGIPIIAD 208
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 18-162 5.27e-03

2-amino-3-ketobutyrate coenzyme A ligase; Provisional


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 38.64  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  18 IDAGIQRVLAHG------QFILGPEV--AELEQKLAAYAGTEFCISCANGTDALQIVQMALgIGPGDEVITPGFNYIATA 89
Cdd:PRK06939   62 IAAAKAALDSHGfgmasvRFICGTQDlhKELEEKLAKFLGTEDAILYSSCFDANGGLFETL-LGKEDAIISDALNHASII 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419359305  90 ESVVLLGAKPVyvdvdpRTCNLDPAKLEA------AITPRTKAIIP---VSLYGQCADLDAINAVAERHGIPVIEDAAQS 160
Cdd:PRK06939  141 DGVRLCKAKRY------RYANNDMADLEAqlkeakEAGARHKLIATdgvFSMDGDIAPLPEICDLADKYDALVMVDDSHA 214


                  ..
gi 1419359305 161 YG 162
Cdd:PRK06939  215 VG 216
SelA COG1921
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis];
116-158 8.12e-03

Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441524  Cd Length: 399  Bit Score: 37.79  E-value: 8.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1419359305 116 LEAAITPRTKAIIPV--SLYGQC-----ADLDAINAVAERHGIPVIEDAA 158
Cdd:COG1921   147 YEAAITENTAALLKVhtSNYRIVgfteeVSLAELAELAHEHGLPVIVDLG 196
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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