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Conserved domains on  [gi|17557272|ref|NP_505372|]
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Sphingosine Phosphate Lyase [Caenorhabditis elegans]

Protein Classification

aspartate aminotransferase family protein( domain architecture ID 10157828)

aspartate aminotransferase family protein is a pyridoxal phosphate (PLP)-dependent enzyme similar to cysteine sulfinic acid decarboxylase that catalyzes the decarboxylation of L-aspartate, 3-sulfino-L-alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine, and taurine, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 130-493 6.13e-106

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: 321.07  E-value: 6.13e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 130 RVSGAVFNREDDKDEREMyeEVFGKFAWTNPlwPKLFPGVRIMEAEVVRMCCNMMNGDSET-CGTMSTGGSISILLACLA 208
Cdd:cd06450   1 FLAGFVTTMDPPALLLEM--LTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPSEDaDGVFTSGGSESNLLALLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 209 HRNRLLKR-------GEKYTEMIVPSSVHAAFFKAAECFRIKVRKIPVDPvTFKVDLVKMKAAINK------RTCMLVGS 275
Cdd:cd06450  77 ARDRARKRlkagggrGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDE-DGRMDPEALEAAIDEdkaeglNPIMVVAT 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 276 APNFPFGTVDDIEAIGQLGLEYDIPVHVDACLGGFLLPFLEEDeiRYDFRVPGVSSISADSHKYGLAPKGSSVVLYRnke 355
Cdd:cd06450 156 AGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPR--HLDFGIERVDSISVDPHKYGLVPLGCSAVLVR--- 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 356 llhnqyfcdadwqggiyasatmegsraghnIALCWAAMLYHAQEGYKANARKIVDTTRKIRNGLSNIKGIKLQGPSDVCI 435
Cdd:cd06450 231 ------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLSL 280

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17557272 436 VSWTTNDGVEL----YRFHNFMKEK-HWQLNGLQF--PAGVHIMVTMNHTHPGLAEAFVADCRAA 493
Cdd:cd06450 281 VCFRLKPSVKLdelnYDLSDRLNERgGWHVPATTLggPNVLRFVVTNPLTTRDDADALLEDIERA 345
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 130-493 6.13e-106

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: 321.07  E-value: 6.13e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 130 RVSGAVFNREDDKDEREMyeEVFGKFAWTNPlwPKLFPGVRIMEAEVVRMCCNMMNGDSET-CGTMSTGGSISILLACLA 208
Cdd:cd06450   1 FLAGFVTTMDPPALLLEM--LTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPSEDaDGVFTSGGSESNLLALLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 209 HRNRLLKR-------GEKYTEMIVPSSVHAAFFKAAECFRIKVRKIPVDPvTFKVDLVKMKAAINK------RTCMLVGS 275
Cdd:cd06450  77 ARDRARKRlkagggrGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDE-DGRMDPEALEAAIDEdkaeglNPIMVVAT 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 276 APNFPFGTVDDIEAIGQLGLEYDIPVHVDACLGGFLLPFLEEDeiRYDFRVPGVSSISADSHKYGLAPKGSSVVLYRnke 355
Cdd:cd06450 156 AGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPR--HLDFGIERVDSISVDPHKYGLVPLGCSAVLVR--- 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 356 llhnqyfcdadwqggiyasatmegsraghnIALCWAAMLYHAQEGYKANARKIVDTTRKIRNGLSNIKGIKLQGPSDVCI 435
Cdd:cd06450 231 ------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLSL 280

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17557272 436 VSWTTNDGVEL----YRFHNFMKEK-HWQLNGLQF--PAGVHIMVTMNHTHPGLAEAFVADCRAA 493
Cdd:cd06450 281 VCFRLKPSVKLdelnYDLSDRLNERgGWHVPATTLggPNVLRFVVTNPLTTRDDADALLEDIERA 345
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 158-495 5.27e-73

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 439846 [Multi-domain]  Cd Length: 460  Bit Score: 239.73  E-value: 5.27e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 158 TNPLWPKLFPGVRIMEAEVVRMCCNMMNGDSETCGTMSTGGSISILLACLAHRNRLLKRGEKYT--------EMIVPSSV 229
Cdd:COG0076  94 QNMGDWDTSPAATELEREVVRWLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARRVRAEglpgaprpRIVVSEEA 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 230 HAAFFKAAECFRIK---VRKIPVDPvTFKVDLVKMKAAI------NKRTCMLVGSAPNFPFGTVDDIEAIGQLGLEYDIP 300
Cdd:COG0076 174 HSSVDKAARLLGLGrdaLRKVPVDE-DGRMDPDALEAAIdedraaGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLW 252

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 301 VHVDACLGGFLLPfleEDEIRYDF-RVPGVSSISADSHKYGLAPKGSSVVLYRNKELLHNQYFCDAD-----WQGGI-YA 373
Cdd:COG0076 253 LHVDAAYGGFALP---SPELRHLLdGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASylgpaDDGVPnLG 329

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 374 SATMEGSRAGhNIALCWAAMLYHAQEGYKANARKIVDTTRKIRNGLSNIKGIKLQGPSDVCIVSWTTNDGVE------LY 447
Cdd:COG0076 330 DYTLELSRRF-RALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCFRYKPAGLdeedalNY 408

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17557272 448 RFHNFMKEKhwqlnGLQFPAGVHI-------MVTMNH-THPGLAEAFVADCRAAVE 495
Cdd:COG0076 409 ALRDRLRAR-----GRAFLSPTKLdgrvvlrLVVLNPrTTEDDVDALLDDLREAAA 459
tyr_de_CO2_Arch TIGR03812
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of ...
 150-489 1.96e-68

tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of tyrosine decarboxylase, and are involved in methanofuran biosynthesis. Members show clear homology to the Enterococcus form, Tdc, that is involved in tyrosine decarboxylation for resistance to acidic conditions. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274796  Cd Length: 373  Bit Score: 224.92  E-value: 1.96e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   150 EVFGKFAWTNPLWPKLFPGVRIMEAEVVRMCCNMMNgDSETCGTMSTGGSISILLACLAHRNrLLKRGEKYTEMIVPSSV 229
Cdd:TIGR03812  38 KAYDMFIETNLGDPGLFPGTKKIEEEVVGSLGNLLH-LPDAYGYIVSGGTEANIQAVRAAKN-LAREEKRTPNIIVPESA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   230 HAAFFKAAECFRIKVRKIPVDPvTFKVDLVKMKAAINKRTCMLVGSAPNFPFGTVDDIEAIGQLGLEYDIPVHVDACLGG 309
Cdd:TIGR03812 116 HFSFEKAAEMLGLELRYAPLDE-DYTVDVKDVEDLIDDNTIGIVGIAGTTELGQIDDIEELSKIALENGIYLHVDAAFGG 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   310 FLLPFLEEDE--IRYDFRVPGVSSISADSHKYGLAPKGSSVVLYRNKELLH----NQYFCDADWQggiyasATMEGSRAG 383
Cdd:TIGR03812 195 FVIPFLKKGYnpPPFDFSLPGVQSITIDPHKMGLSPIPAGGILFRSKSYLKylsvDAPYLTVKKQ------ATITGTRSG 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   384 HNIALCWAAMLYHAQEGYKANARKIVDTTRKIRNGLSNIKGIKLQGPSdVCIVSWTTNDGVELYRfhnFMKEKHWQLNGL 463
Cdd:TIGR03812 269 ASAAATYAVIKYLGREGYRKIVAECMENTRYLVEELKKIGFEPVIEPV-LNIVAFEVDDPEEVRK---KLRDRGWYVSVT 344

                         330       340
                  ....*....|....*....|....*.
gi 17557272   464 QFPAGVHIMVtMNHTHPGLAEAFVAD 489
Cdd:TIGR03812 345 RCPKALRIVV-MPHVTREHIEEFLED 369
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
172-421 7.73e-19

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 88.24  E-value: 7.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   172 MEAEVVRMCCNMMN-----GDSETCGTMSTGGSISILLACLAHRNRLLKR----GEKYTEMIVP--------SSVHAAFF 234
Cdd:pfam00282  80 LENVVMNWLGEMLGlpaefLGQEGGGVLQPGSSESNLLALLAARTKWIKRmkaaGKPADSSGILaklvaytsDQAHSSIE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   235 KAAECFRIKVRKIPVDPvTFKV---DLVKMKAAINKRTCMLVGSAPNFP---FGTVDDIEAIGQLGLEYDIPVHVDACLG 308
Cdd:pfam00282 160 KAALYGGVKLREIPSDD-NGKMrgmDLEKAIEEDKENGLIPFFVVATLGttgSGAFDDLQELGDICAKHNLWLHVDAAYG 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   309 G--FLLPfleedEIR-YDFRVPGVSSISADSHKYGLAPKGSSVVLYRNKELLHNQYFCDADWQGGIYASA-----TMEGS 380
Cdd:pfam00282 239 GsaFICP-----EFRhWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDSAYdtghkQIPLS 313

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 17557272   381 RaGHNIALCWAAMLYHAQEGYKANARKIVDTTRKIRNGLSN 421
Cdd:pfam00282 314 R-RFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRK 353
PRK02769 PRK02769
histidine decarboxylase; Provisional
 189-489 1.36e-11

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 66.22  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  189 ETCGTMSTGGSISILLACLAHRNRllkrgekYTEMIVPSS--VHAAFFKAAECFRIKVRKIP--------VDPVTFKVDL 258
Cdd:PRK02769  84 ESWGYITNGGTEGNLYGCYLAREL-------FPDGTLYYSkdTHYSVSKIARLLRIKSRVITslpngeidYDDLISKIKE 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  259 VKMKAAI---NKRTCMLvgsapnfpfGTVDDIEAI----GQLGLEyDIPVHVDACLGGFLLPFLEeDEIRYDFRvPGVSS 331
Cdd:PRK02769 157 NKNQPPIifaNIGTTMT---------GAIDNIKEIqeilKKIGID-DYYIHADAALSGMILPFVN-NPPPFSFA-DGIDS 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  332 ISADSHKYGLAPKGSSVVLYRNKELLHNQYFCDadwqggiYASA---TMEGSRAGHNIALCWAAMLYHAQEGYKANARKI 408
Cdd:PRK02769 225 IAISGHKFIGSPMPCGIVLAKKKYVERISVDVD-------YIGSrdqTISGSRNGHTALLLWAAIRSLGSKGLRQRVQHC 297

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  409 VDTTRKIRNGLSNIkGIK-LQGPSDVCIVSWTTNDGVelyrfhnfmkEKHWQLNGLQFPAgvHIMVTMNHTHP---GLAE 484
Cdd:PRK02769 298 LDMAQYAVDRLQAN-GIPaWRNPNSITVVFPCPSERI----------WKKWHLATSGNQA--HIITMPHHNKQqidSLID 364


                 ....*
gi 17557272  485 AFVAD 489
Cdd:PRK02769 365 ELIFD 369
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 130-493 6.13e-106

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: 321.07  E-value: 6.13e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 130 RVSGAVFNREDDKDEREMyeEVFGKFAWTNPlwPKLFPGVRIMEAEVVRMCCNMMNGDSET-CGTMSTGGSISILLACLA 208
Cdd:cd06450   1 FLAGFVTTMDPPALLLEM--LTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPSEDaDGVFTSGGSESNLLALLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 209 HRNRLLKR-------GEKYTEMIVPSSVHAAFFKAAECFRIKVRKIPVDPvTFKVDLVKMKAAINK------RTCMLVGS 275
Cdd:cd06450  77 ARDRARKRlkagggrGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDE-DGRMDPEALEAAIDEdkaeglNPIMVVAT 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 276 APNFPFGTVDDIEAIGQLGLEYDIPVHVDACLGGFLLPFLEEDeiRYDFRVPGVSSISADSHKYGLAPKGSSVVLYRnke 355
Cdd:cd06450 156 AGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPR--HLDFGIERVDSISVDPHKYGLVPLGCSAVLVR--- 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 356 llhnqyfcdadwqggiyasatmegsraghnIALCWAAMLYHAQEGYKANARKIVDTTRKIRNGLSNIKGIKLQGPSDVCI 435
Cdd:cd06450 231 ------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLSL 280

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17557272 436 VSWTTNDGVEL----YRFHNFMKEK-HWQLNGLQF--PAGVHIMVTMNHTHPGLAEAFVADCRAA 493
Cdd:cd06450 281 VCFRLKPSVKLdelnYDLSDRLNERgGWHVPATTLggPNVLRFVVTNPLTTRDDADALLEDIERA 345
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 158-495 5.27e-73

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 439846 [Multi-domain]  Cd Length: 460  Bit Score: 239.73  E-value: 5.27e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 158 TNPLWPKLFPGVRIMEAEVVRMCCNMMNGDSETCGTMSTGGSISILLACLAHRNRLLKRGEKYT--------EMIVPSSV 229
Cdd:COG0076  94 QNMGDWDTSPAATELEREVVRWLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARRVRAEglpgaprpRIVVSEEA 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 230 HAAFFKAAECFRIK---VRKIPVDPvTFKVDLVKMKAAI------NKRTCMLVGSAPNFPFGTVDDIEAIGQLGLEYDIP 300
Cdd:COG0076 174 HSSVDKAARLLGLGrdaLRKVPVDE-DGRMDPDALEAAIdedraaGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLW 252

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 301 VHVDACLGGFLLPfleEDEIRYDF-RVPGVSSISADSHKYGLAPKGSSVVLYRNKELLHNQYFCDAD-----WQGGI-YA 373
Cdd:COG0076 253 LHVDAAYGGFALP---SPELRHLLdGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASylgpaDDGVPnLG 329

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 374 SATMEGSRAGhNIALCWAAMLYHAQEGYKANARKIVDTTRKIRNGLSNIKGIKLQGPSDVCIVSWTTNDGVE------LY 447
Cdd:COG0076 330 DYTLELSRRF-RALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCFRYKPAGLdeedalNY 408

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17557272 448 RFHNFMKEKhwqlnGLQFPAGVHI-------MVTMNH-THPGLAEAFVADCRAAVE 495
Cdd:COG0076 409 ALRDRLRAR-----GRAFLSPTKLdgrvvlrLVVLNPrTTEDDVDALLDDLREAAA 459
tyr_de_CO2_Arch TIGR03812
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of ...
 150-489 1.96e-68

tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of tyrosine decarboxylase, and are involved in methanofuran biosynthesis. Members show clear homology to the Enterococcus form, Tdc, that is involved in tyrosine decarboxylation for resistance to acidic conditions. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274796  Cd Length: 373  Bit Score: 224.92  E-value: 1.96e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   150 EVFGKFAWTNPLWPKLFPGVRIMEAEVVRMCCNMMNgDSETCGTMSTGGSISILLACLAHRNrLLKRGEKYTEMIVPSSV 229
Cdd:TIGR03812  38 KAYDMFIETNLGDPGLFPGTKKIEEEVVGSLGNLLH-LPDAYGYIVSGGTEANIQAVRAAKN-LAREEKRTPNIIVPESA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   230 HAAFFKAAECFRIKVRKIPVDPvTFKVDLVKMKAAINKRTCMLVGSAPNFPFGTVDDIEAIGQLGLEYDIPVHVDACLGG 309
Cdd:TIGR03812 116 HFSFEKAAEMLGLELRYAPLDE-DYTVDVKDVEDLIDDNTIGIVGIAGTTELGQIDDIEELSKIALENGIYLHVDAAFGG 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   310 FLLPFLEEDE--IRYDFRVPGVSSISADSHKYGLAPKGSSVVLYRNKELLH----NQYFCDADWQggiyasATMEGSRAG 383
Cdd:TIGR03812 195 FVIPFLKKGYnpPPFDFSLPGVQSITIDPHKMGLSPIPAGGILFRSKSYLKylsvDAPYLTVKKQ------ATITGTRSG 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   384 HNIALCWAAMLYHAQEGYKANARKIVDTTRKIRNGLSNIKGIKLQGPSdVCIVSWTTNDGVELYRfhnFMKEKHWQLNGL 463
Cdd:TIGR03812 269 ASAAATYAVIKYLGREGYRKIVAECMENTRYLVEELKKIGFEPVIEPV-LNIVAFEVDDPEEVRK---KLRDRGWYVSVT 344

                         330       340
                  ....*....|....*....|....*.
gi 17557272   464 QFPAGVHIMVtMNHTHPGLAEAFVAD 489
Cdd:TIGR03812 345 RCPKALRIVV-MPHVTREHIEEFLED 369
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
172-421 7.73e-19

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 88.24  E-value: 7.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   172 MEAEVVRMCCNMMN-----GDSETCGTMSTGGSISILLACLAHRNRLLKR----GEKYTEMIVP--------SSVHAAFF 234
Cdd:pfam00282  80 LENVVMNWLGEMLGlpaefLGQEGGGVLQPGSSESNLLALLAARTKWIKRmkaaGKPADSSGILaklvaytsDQAHSSIE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   235 KAAECFRIKVRKIPVDPvTFKV---DLVKMKAAINKRTCMLVGSAPNFP---FGTVDDIEAIGQLGLEYDIPVHVDACLG 308
Cdd:pfam00282 160 KAALYGGVKLREIPSDD-NGKMrgmDLEKAIEEDKENGLIPFFVVATLGttgSGAFDDLQELGDICAKHNLWLHVDAAYG 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   309 G--FLLPfleedEIR-YDFRVPGVSSISADSHKYGLAPKGSSVVLYRNKELLHNQYFCDADWQGGIYASA-----TMEGS 380
Cdd:pfam00282 239 GsaFICP-----EFRhWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDSAYdtghkQIPLS 313

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 17557272   381 RaGHNIALCWAAMLYHAQEGYKANARKIVDTTRKIRNGLSN 421
Cdd:pfam00282 314 R-RFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRK 353
PRK02769 PRK02769
histidine decarboxylase; Provisional
 189-489 1.36e-11

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 66.22  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  189 ETCGTMSTGGSISILLACLAHRNRllkrgekYTEMIVPSS--VHAAFFKAAECFRIKVRKIP--------VDPVTFKVDL 258
Cdd:PRK02769  84 ESWGYITNGGTEGNLYGCYLAREL-------FPDGTLYYSkdTHYSVSKIARLLRIKSRVITslpngeidYDDLISKIKE 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  259 VKMKAAI---NKRTCMLvgsapnfpfGTVDDIEAI----GQLGLEyDIPVHVDACLGGFLLPFLEeDEIRYDFRvPGVSS 331
Cdd:PRK02769 157 NKNQPPIifaNIGTTMT---------GAIDNIKEIqeilKKIGID-DYYIHADAALSGMILPFVN-NPPPFSFA-DGIDS 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  332 ISADSHKYGLAPKGSSVVLYRNKELLHNQYFCDadwqggiYASA---TMEGSRAGHNIALCWAAMLYHAQEGYKANARKI 408
Cdd:PRK02769 225 IAISGHKFIGSPMPCGIVLAKKKYVERISVDVD-------YIGSrdqTISGSRNGHTALLLWAAIRSLGSKGLRQRVQHC 297

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  409 VDTTRKIRNGLSNIkGIK-LQGPSDVCIVSWTTNDGVelyrfhnfmkEKHWQLNGLQFPAgvHIMVTMNHTHP---GLAE 484
Cdd:PRK02769 298 LDMAQYAVDRLQAN-GIPaWRNPNSITVVFPCPSERI----------WKKWHLATSGNQA--HIITMPHHNKQqidSLID 364


                 ....*
gi 17557272  485 AFVAD 489
Cdd:PRK02769 365 ELIFD 369
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
193-432 3.58e-11

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 65.16  E-value: 3.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 193 TMSTGGSISILLACLAHrnrlLKRGEK--YTEM-----IVPssvhaaFFKAAECFRIKVRKIPVDPvTFKVDLVKMKAAI 265
Cdd:COG0520  83 TRGTTEAINLVAYGLGR----LKPGDEilITEMehhsnIVP------WQELAERTGAEVRVIPLDE-DGELDLEALEALL 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 266 NKRTCML-VGSAPNFpFGTVDDIEAIGQLGLEYDIPVHVDACLGGFLLPF-LEEDEIryDFrvpgvssISADSHK-YGla 342
Cdd:COG0520 152 TPRTKLVaVTHVSNV-TGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVdVQALGC--DF-------YAFSGHKlYG-- 219

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 343 PKGSSVvLYRNKELLHNQ--YFCDadwqGGIYASATMEGSR---------AG-HNIALCW---AAMLYHAQEGYKANARK 407
Cdd:COG0520 220 PTGIGV-LYGKRELLEALppFLGG----GGMIEWVSFDGTTyadlprrfeAGtPNIAGAIglgAAIDYLEAIGMEAIEAR 294

                       250       260
                ....*....|....*....|....*
gi 17557272 408 IVDTTRKIRNGLSNIKGIKLQGPSD 432
Cdd:COG0520 295 ERELTAYALEGLAAIPGVRILGPAD 319
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 195-301 9.99e-09

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 57.44  E-value: 9.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  195 STGGSISILLACLAhrnrLLKRGEkytEMIVPS----SvHAAFFKAAECfriKVRKIPVDPVT-FKVDLVKMKAAINKRT 269
Cdd:PRK05764  97 TTGAKQALYNAFMA----LLDPGD---EVIIPApywvS-YPEMVKLAGG---VPVFVPTGEENgFKLTVEQLEAAITPKT 165

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 17557272  270 CMLVGSAPNFPFGTV---DDIEAIGQLGLEYDIPV 301
Cdd:PRK05764 166 KALILNSPSNPTGAVyspEELEAIADVAVEHDIWV 200
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 194-310 8.64e-08

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: 54.27  E-value: 8.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 194 MSTGGSISILLACLAhrnrLLKRGEkytEMIVPSSVHAAFFKAAECFRIKVRKIPVDPV-TFKVDLVKMKAAINKRTCML 272
Cdd:cd00609  64 VTNGAQEALSLLLRA----LLNPGD---EVLVPDPTYPGYEAAARLAGAEVVPVPLDEEgGFLLDLELLEAAKTPKTKLL 136

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17557272 273 VGSAPNFPFGTV---DDIEAIGQLGLEYDIPVHVDACLGGF 310
Cdd:cd00609 137 YLNNPNNPTGAVlseEELEELAELAKKHGILIISDEAYAEL 177
PLN03032 PLN03032
serine decarboxylase; Provisional
 213-419 1.12e-07

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 54.06  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  213 LLKRgEKYTEMIVPSS--VHAAFFKAAECFRIKVRKIPVDPVTfKVDLVKMKAAINK---RTCMLVGSAPNFPFGTVDDI 287
Cdd:PLN03032 103 LVGR-EVFPDGILYASreSHYSVFKAARMYRMEAVKVPTLPSG-EIDYDDLERALAKnrdKPAILNVNIGTTVKGAVDDL 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  288 EAIGQLGLEYDIP-----VHVDACLGGFLLPFLEEDEiRYDFRVPgVSSISADSHKYGLAPKGSSVVLYRNKELL----H 358
Cdd:PLN03032 181 DRILRILKELGYTedrfyIHCDGALFGLMMPFVSRAP-EVTFRKP-IGSVSVSGHKFLGCPMPCGVALTRKKHVKalsqN 258

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17557272  359 NQYFCDADwqggiyasATMEGSRAGHNIALCWAAMLYHAQEGYKANARKIVDTTRKIRNGL 419
Cdd:PLN03032 259 VEYLNSRD--------ATIMGSRNGHAPLYLWYTLRRKGYRGIKRDVQHCMRNAHYLKDRL 311
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 242-439 1.52e-07

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: 53.62  E-value: 1.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 242 IKVRKIPVDPvTFKVDLVKMKAAINKRTCML-VGSAPNFpFGTVDDIEAIGQLGLEYDIPVHVDACLGGFLLPfLEEDEI 320
Cdd:cd06453 114 AKLKVVPVDD-DGQLDLEALEKLLTERTKLVaVTHVSNV-LGTINPVKEIGEIAHEAGVPVLVDGAQSAGHMP-VDVQDL 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 321 RYDFRV-PGvssisadsHKyGLAPKGSSvVLYRNKELLhnqyfcdAD---WQGGIYASATMEGSR-----------AG-H 384
Cdd:cd06453 191 GCDFLAfSG--------HK-MLGPTGIG-VLYGKEELL-------EEmppYGGGGEMIEEVSFEEttyadlphkfeAGtP 253

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17557272 385 NIA----LCwAAMLYHAQEGYKANARKIVDTTRKIRNGLSNIKGIKLQGPSD--VCIVSWT 439
Cdd:cd06453 254 NIAgaigLG-AAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEdrAGVVSFN 313
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 170-430 4.51e-07

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: 52.25  E-value: 4.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   170 RIMEA--EVVRmccNMMNGDS--ETCGTMSTGGSISILLACLAHRnrlLKRGekyTEMIVPSSVHAAFF----KAAECFR 241
Cdd:pfam00266  43 QAYEEarEKVA---EFINAPSndEIIFTSGTTEAINLVALSLGRS---LKPG---DEIVITEMEHHANLvpwqELAKRTG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   242 IKVRKIPVDPvTFKVDLVKMKAAINKRTCMLVGSAPNFPFGTVDDIEAIGQLGLEYDIPVHVDAC--LGGfllpfleede 319
Cdd:pfam00266 114 ARVRVLPLDE-DGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAqaIGH---------- 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   320 IRYDFRVPGVSSISADSHKYgLAPKGSSvVLYRNKELLHN--------QYFCDADWQGGIYASATMeGSRAGH-NIA--- 387
Cdd:pfam00266 183 RPIDVQKLGVDFLAFSGHKL-YGPTGIG-VLYGRRDLLEKmppllgggGMIETVSLQESTFADAPW-KFEAGTpNIAgii 259

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 17557272   388 LCWAAMLYHAQEGYKANARKIVDTTRKIRNGLSNIKGIKLQGP 430
Cdd:pfam00266 260 GLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGP 302
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 193-301 7.56e-07

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: 51.28  E-value: 7.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 193 TMSTGGSISILLACLAhrnrLLKRGEkytEMIVPS---SVHAAFFKAAECfriKVRKIPVDPVT-FKVDLVKMKAAINKR 268
Cdd:COG0436  94 LVTNGAKEALALALLA----LLNPGD---EVLVPDpgyPSYRAAVRLAGG---KPVPVPLDEENgFLPDPEALEAAITPR 163

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 17557272 269 TCMLVGSAPNFPFGTV---DDIEAIGQLGLEYDIPV 301
Cdd:COG0436 164 TKAIVLNSPNNPTGAVysrEELEALAELAREHDLLV 199
PLN02651 PLN02651
cysteine desulfurase
 247-432 9.96e-07

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 50.81  E-value: 9.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  247 IPVDPvTFKVDLVKMKAAINKRTCMLVGSAPNFPFGTVDDIEAIGQLGLEYDIPVHVDAC--LGgfllpfleedEIRYDF 324
Cdd:PLN02651 118 LPVKS-DGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAAqaVG----------KIPVDV 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  325 RVPGVSSISADSHKYGlAPKGSSVVLYRNKELLH-NQYFCDADWQGGIyasatmegsRAG-HNIALC----WAAMLyhAQ 398
Cdd:PLN02651 187 DDLGVDLMSISGHKIY-GPKGVGALYVRRRPRVRlEPLMSGGGQERGR---------RSGtENTPLVvglgAACEL--AM 254

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 17557272  399 EGYKANARKIVDTTRKIRNGLSN-IKGIKLQGPSD 432
Cdd:PLN02651 255 KEMDYDEKHMKALRERLLNGLRAkLGGVRVNGPRD 289
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
187-304 4.75e-06

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 48.84  E-value: 4.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   187 DSETCGTMSTGGSISILLACLAhrnrllkrgEKYTEMIVPSSVHAAFFKAAECFRIKVRKIPV-DPVTFKVDLVKMKAAI 265
Cdd:pfam00155  63 EAAVVFGSGAGANIEALIFLLA---------NPGDAILVPAPTYASYIRIARLAGGEVVRYPLyDSNDFHLDFDALEAAL 133

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 17557272   266 NKRTCMLVGSAPNFPFGTV---DDIEAIGQLGLEYDIPVHVD 304
Cdd:pfam00155 134 KEKPKVVLHTSPHNPTGTVatlEELEKLLDLAKEHNILLLVD 175
PLN02263 PLN02263
serine decarboxylase
 230-407 5.04e-06

serine decarboxylase


Pssm-ID: 177904 [Multi-domain]  Cd Length: 470  Bit Score: 49.04  E-value: 5.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  230 HAAFFKAAECFRIKVRKI------PVDPVTFKVDLVKMK---AAINKRTCMLVGsapnfpfGTVDD----IEAIGQLGLE 296
Cdd:PLN02263 188 HYSVFKAARMYRMECVKVdtlvsgEIDCADFKAKLLANKdkpAIINVNIGTTVK-------GAVDDldlvIKTLEECGFS 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  297 YD-IPVHVDACLGGFLLPFLEEDEiRYDFRVPgVSSISADSHKYGLAPKGSSVVLYRNKE---LLHN-QYFCDADwqggi 371
Cdd:PLN02263 261 QDrFYIHCDGALFGLMMPFVKRAP-KVTFKKP-IGSVSVSGHKFVGCPMPCGVQITRMEHinvLSSNvEYLASRD----- 333

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 17557272  372 yasATMEGSRAGHNIALCWAAMLYHAQEGYKANARK 407
Cdd:PLN02263 334 ---ATIMGSRNGHAPIFLWYTLNRKGYRGFQKEVQK 366
PRK00451 PRK00451
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
205-293 1.08e-05

aminomethyl-transferring glycine dehydrogenase subunit GcvPA;


Pssm-ID: 234769 [Multi-domain]  Cd Length: 447  Bit Score: 47.83  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  205 ACLAHRNRllKRgekyTEMIVPSSVHAAFFKAAECF----RIKVRKIPVDPVTfkVDLVKMKAAINKRTCMLVGSAPNFp 280
Cdd:PRK00451 145 ALMAVRIT--KR----KKVLVSGAVHPEYREVLKTYlkgqGIEVVEVPYEDGV--TDLEALEAAVDDDTAAVVVQYPNF- 215

                         90
                 ....*....|...
gi 17557272  281 FGTVDDIEAIGQL 293
Cdd:PRK00451 216 FGVIEDLEEIAEI 228
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
190-303 1.21e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 47.49  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  190 TCGTmstGGSISILLaclahrNRLLKRGEkytEMIVPssvhAAFFKA----AECFRIKVRKIPVDPVTFKVDLVKMKAAI 265
Cdd:PRK06836 102 TCGA---AGALNVAL------KAILNPGD---EVIVF----APYFVEyrfyVDNHGGKLVVVPTDTDTFQPDLDALEAAI 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 17557272  266 NKRTCMLVGSAPNFPFGTV---DDIEAIGQL----GLEYDIPVHV 303
Cdd:PRK06836 166 TPKTKAVIINSPNNPTGVVyseETLKALAALleekSKEYGRPIYL 210
PRK07777 PRK07777
putative succinyldiaminopimelate transaminase DapC;
230-304 1.22e-04

putative succinyldiaminopimelate transaminase DapC;


Pssm-ID: 236095 [Multi-domain]  Cd Length: 387  Bit Score: 44.64  E-value: 1.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17557272  230 HAAFFKAAECFRIKVRKIPVDPvTFKVDLVKMKAAINKRTCMLVGSAPNFPFGTV---DDIEAIGQLGLEYDIPVHVD 304
Cdd:PRK07777 122 YAAVIAMAGAHRVPVPLVPDGR-GFALDLDALRAAVTPRTRALIVNSPHNPTGTVltaAELAAIAELAVEHDLLVITD 198
GDC-P cd00613
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ...
 204-305 2.24e-04

Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalysed by this protein is: Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2. Alpha-beta-type dimers associate to form an alpha(2)beta(2) tetramer, where the alpha- and beta-subunits are structurally similar and appear to have arisen by gene duplication and subsequent divergence with a loss of one active site. The members of this CD are widely dispersed among all three forms of cellular life.


Pssm-ID: 99737 [Multi-domain]  Cd Length: 398  Bit Score: 43.76  E-value: 2.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 204 LACLAHRNRLLKRgekyTEMIVPSSVH------AAFfkAAECFRIKVRKIPVDPVTfKVDLVKMKAAINKRTCMLVGSAP 277
Cdd:cd00613  96 AAGLAAIRAYHKR----NKVLVPDSAHptnpavART--RGEPLGIEVVEVPSDEGG-TVDLEALKEEVSEEVAALMVQYP 168

                        90       100
                ....*....|....*....|....*....
gi 17557272 278 NFpFGTV-DDIEAIGQLGLEYDIPVHVDA 305
Cdd:cd00613 169 NT-LGVFeDLIKEIADIAHSAGALVYVDG 196
PRK09082 PRK09082
methionine aminotransferase; Validated
 187-299 3.33e-04

methionine aminotransferase; Validated


Pssm-ID: 181642 [Multi-domain]  Cd Length: 386  Bit Score: 42.98  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  187 DSETCGTMSTGGSISILLACLAhrnrLLKRGEkytEMIVPSSVHAAFFKAAECFRIKVRKIPVDPVTFKVDLVKMKAAIN 266
Cdd:PRK09082  89 DADSEITVTAGATEALFAAILA----LVRPGD---EVIVFDPSYDSYAPAIELAGGRAVRVALQPPDFRVDWQRFAAAIS 161

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 17557272  267 KRTCMLVGSAPNFPFGTV---DDIEAIGQLGLEYDI 299
Cdd:PRK09082 162 PRTRLIILNTPHNPSGTVwsaADMRALWQLIAGTDI 197
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 221-306 3.43e-04

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: 43.04  E-value: 3.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272   221 TEMIVPSsvhAAFFKAAECFrIKVRKIPV----DPVTFKVDLVKMKAAINKRTCMLVgsaPNFPFGTVDDIEAIGQLGLE 296
Cdd:pfam01041  65 DEVITPS---FTFVATANAA-LRLGAKPVfvdiDPDTYNIDPEAIEAAITPRTKAII---PVHLYGQPADMDAIRAIAAR 137

                          90
                  ....*....|
gi 17557272   297 YDIPVHVDAC 306
Cdd:pfam01041 138 HGLPVIEDAA 147
PRK14012 PRK14012
IscS subfamily cysteine desulfurase;
256-345 7.98e-04

IscS subfamily cysteine desulfurase;


Pssm-ID: 184450 [Multi-domain]  Cd Length: 404  Bit Score: 41.85  E-value: 7.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  256 VDLVKMKAAINKRTCMLVGSAPNFPFGTVDDIEAIGQLGLEYDIPVHVDACLGGFLLPFleedeiryDFRVPGVSSISAD 335
Cdd:PRK14012 132 IDLEKLEAAMRDDTILVSIMHVNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPI--------DLSKLKVDLMSFS 203

                         90
                 ....*....|.
gi 17557272  336 SHK-YGlaPKG 345
Cdd:PRK14012 204 AHKiYG--PKG 212
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 283-492 2.27e-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: 40.39  E-value: 2.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 283 TVDDIEAIGQLGLEYDIPVHVD--------ACLGGFLLPFLEedeirydfrvpGVSSISADSHKYGLAPKGSSVVLyrNK 354
Cdd:cd06502 144 PLDELKAISALAKENGLPLHLDgarlanaaAALGVALKTYKS-----------GVDSVSFCLSKGGGAPVGAVVVG--NR 210

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272 355 ELL-HNQYFCDAdwQGGiyasatmeGSRAGHNIALCWAAMLyhAQEGYKANARKIVDTTRKIRNGLSNIKGIKLQGPSDV 433
Cdd:cd06502 211 DFIaRARRRRKQ--AGG--------GMRQSGFLAAAGLAAL--ENDLWLRRLRHDHEMARRLAEALEELGGLESEVQTNI 278

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17557272 434 CIVSWTTNDGV--ELYRFHNFMKEKHWQLNGlqFPAGVHIMVTMNHTHPGLAEAFVADCRA 492
Cdd:cd06502 279 VLLDPVEANAVfvELSKEAIERRGEGVLFYA--WGEGGVRFVTHWDTTEEDVDELLSALKA 337
PRK08361 PRK08361
aspartate aminotransferase; Provisional
 213-299 2.64e-03

aspartate aminotransferase; Provisional


Pssm-ID: 236248 [Multi-domain]  Cd Length: 391  Bit Score: 40.25  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  213 LLKRGEkytEMIVPSSVHAAFFKAAECFRIKVRKIPV-DPVTFKVDLVKMKAAINKRTCMLVGSAPNFPFGTVDDIE--- 288
Cdd:PRK08361 113 LLEEGD---EVIIPDPAFVCYVEDAKIAEAKPIRIPLrEENEFQPDPDELLELITKRTRMIVINYPNNPTGATLDKEvak 189

                         90
                 ....*....|.
gi 17557272  289 AIGQLGLEYDI 299
Cdd:PRK08361 190 AIADIAEDYNI 200
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
254-310 3.35e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 40.09  E-value: 3.35e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557272  254 FKVDLVKMKAAINKRTCMLVGSAPNFPFGTV---DDIEAIGQLGLEYDIPVHVDACLGGF 310
Cdd:PRK06348 148 FQINVKKLEALITSKTKAIILNSPNNPTGAVfskETLEEIAKIAIEYDLFIISDEVYDGF 207
 
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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