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Conserved domains on  [gi|74275346|ref|NP_001625|]
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S-adenosylmethionine decarboxylase proenzyme isoform 1 [Homo sapiens]

Protein Classification

S-adenosylmethionine decarboxylase proenzyme( domain architecture ID 10479824)

S-adenosylmethionine decarboxylase proenzyme is cleaved to form the alpha and beta chains of the active enzyme that catalyzes the conversion of S-adenosyl-L-methionine to decarboxylated S-adenosylmethionine, which is essential for biosynthesis of the polyamines spermidine and spermine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SAM_decarbox pfam01536
Adenosylmethionine decarboxylase; This is a family of S-adenosylmethionine decarboxylase ...
4-325 0e+00

Adenosylmethionine decarboxylase; This is a family of S-adenosylmethionine decarboxylase (SAMDC) proenzymes. In the biosynthesis of polyamines SAMDC produces decarboxylated S-adenosylmethionine, which serves as the aminopropyl moiety necessary for spermidine and spermine biosynthesis from putrescine. The Pfam alignment contains both the alpha and beta chains that are cleaved to form the active enzyme.


:

Pssm-ID: 460243  Cd Length: 331  Bit Score: 513.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346     4 AHFFEGTEKLLEVWFSRQQPDA-NQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTC 82
Cdd:pfam01536   1 TIAFEGPEKLLEIWFSPSSGFIpSGDEGGLRSIPREKWEEILDLVKCEILSVKSNDKVDAYVLSESSLFVYPHKIILKTC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346    83 GTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTL 162
Cdd:pfam01536  81 GTTTLLLCLPPLLELAKEELGFLEVYKVFYSRKNFMFPEKQPSPHRSFSEEVAYLDKFFPNGKAYVVGRMNSDHWHLYTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346   163 DFPESRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYWTI 242
Cdd:pfam01536 161 SDPESLSSPEPDQTLEILMTGLDPEKAKQFYKDGHVSGAEMTKASGIDDILPGSIIDDFAFDPCGYSMNGIEGDGAYSTI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346   243 HITPEPEFSYVSFETNLSQ---TSYDDLIRKVVEVFKPGKFVTTLFVNQSSK-----CRTVLASPQKIEGFKRLDCQSAM 314
Cdd:pfam01536 241 HVTPEDGFSYASFETNVPYdpeVDYSDLIRKVLKVFKPGKFSVTLFANSSSPswakcLKLDVSKLQKLGGYKRLDRIVYE 320
                         330
                  ....*....|.
gi 74275346   315 FNDYNFVFTSF 325
Cdd:pfam01536 321 LDGYSLVYQSF 331
 
Name Accession Description Interval E-value
SAM_decarbox pfam01536
Adenosylmethionine decarboxylase; This is a family of S-adenosylmethionine decarboxylase ...
4-325 0e+00

Adenosylmethionine decarboxylase; This is a family of S-adenosylmethionine decarboxylase (SAMDC) proenzymes. In the biosynthesis of polyamines SAMDC produces decarboxylated S-adenosylmethionine, which serves as the aminopropyl moiety necessary for spermidine and spermine biosynthesis from putrescine. The Pfam alignment contains both the alpha and beta chains that are cleaved to form the active enzyme.


Pssm-ID: 460243  Cd Length: 331  Bit Score: 513.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346     4 AHFFEGTEKLLEVWFSRQQPDA-NQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTC 82
Cdd:pfam01536   1 TIAFEGPEKLLEIWFSPSSGFIpSGDEGGLRSIPREKWEEILDLVKCEILSVKSNDKVDAYVLSESSLFVYPHKIILKTC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346    83 GTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTL 162
Cdd:pfam01536  81 GTTTLLLCLPPLLELAKEELGFLEVYKVFYSRKNFMFPEKQPSPHRSFSEEVAYLDKFFPNGKAYVVGRMNSDHWHLYTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346   163 DFPESRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYWTI 242
Cdd:pfam01536 161 SDPESLSSPEPDQTLEILMTGLDPEKAKQFYKDGHVSGAEMTKASGIDDILPGSIIDDFAFDPCGYSMNGIEGDGAYSTI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346   243 HITPEPEFSYVSFETNLSQ---TSYDDLIRKVVEVFKPGKFVTTLFVNQSSK-----CRTVLASPQKIEGFKRLDCQSAM 314
Cdd:pfam01536 241 HVTPEDGFSYASFETNVPYdpeVDYSDLIRKVLKVFKPGKFSVTLFANSSSPswakcLKLDVSKLQKLGGYKRLDRIVYE 320
                         330
                  ....*....|.
gi 74275346   315 FNDYNFVFTSF 325
Cdd:pfam01536 321 LDGYSLVYQSF 331
SAM_DCase TIGR00535
S-adenosylmethionine decarboxylase proenzyme, eukaryotic form; This enzyme is a key regulatory ...
7-328 8.89e-89

S-adenosylmethionine decarboxylase proenzyme, eukaryotic form; This enzyme is a key regulatory enzyme of the polyamine synthetic pathway. This protein is a pyruvoyl-dependent enzyme. The proenzyme is cleaved at a Ser residue that becomes a pyruvoyl group active site. [Central intermediary metabolism, Polyamine biosynthesis]


Pssm-ID: 273124  Cd Length: 334  Bit Score: 269.41  E-value: 8.89e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346     7 FEGTEKLLEVWFSRQQPDANQGSGdLRTIPRSEWDILLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTL 86
Cdd:TIGR00535   1 FEGPEKLLEIWFFEHKKFIDEGKG-LRAIGRAQIDEILDLARCTILSSKKNKSLDSYVLSESSLFIYDHKIIIKTCGTTK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346    87 LLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDC-WYLYTLDF- 164
Cdd:TIGR00535  80 LLFALPKILQLAEQLSSWYKVFSVFYSRGCFLFPCAQPAIHRNFSEEVAYLNKFFGNGKAYVVGDPAKPQkWHLYVAETe 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346   165 PESRVISQPDQTLEILMSELDPAVMDQFYMKDGVT----AKDVTRESGIRDLIP-GSVIDATMFNPCGYSMNGMKSDGTY 239
Cdd:TIGR00535 160 RETPKIEDPDETLEMLMTGLDKEKASKFFKGPAASthnlGYQMTKNSGIDKIIPnSAQICDFDFEPCGYSMNAILGEKAY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346   240 WTIHITPEPEFSYVSFETN---LSQTSYDDLIRKVVEVFKPGKFVTTLFVN--QSSKCRTVLASPQKIEGFKRLDCQSAM 314
Cdd:TIGR00535 240 STIHVTPEKGFSYASFESNgidQGKQDYLDLVLRVLNCFQPSEFSMTVFAKnyQNQSFQKLLSINESLPDYIKLDKQELD 319
                         330
                  ....*....|....
gi 74275346   315 FNDYNFVFTSFAKK 328
Cdd:TIGR00535 320 LGDYHLFYQKFQKK 333
PLN02524 PLN02524
S-adenosylmethionine decarboxylase
7-287 2.22e-82

S-adenosylmethionine decarboxylase


Pssm-ID: 215287  Cd Length: 355  Bit Score: 253.78  E-value: 2.22e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346    7 FEGTEKLLEVWFSRQQPDANQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTL 86
Cdd:PLN02524   8 FEGFEKRLEITFFEPPVFADPNGRGLRALTRSQLDEILRPAECTIVSSLSNDQFDSYVLSESSLFVYPYKIIIKTCGTTK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346   87 LLKALVPLLKLARDYSgfDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPN----GAAYCMG-RMNSDCWYLYT 161
Cdd:PLN02524  88 LLLSIPPLLELAARLS--LSVRSVKYTRGSFIFPGAQPFPHRSFSEEVSVLDGHFGKlglgGKAYVMGdPDKGQKWHVYS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346  162 LDFPESRVISQPDQTLEILMSELDPAVMDQFYMK-DGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGtYW 240
Cdd:PLN02524 166 ASAHNSSNSNEPVYTLEMCMTGLDREKASVFFKDsSLSSAEEMTKASGIRKILPESEICDFAFDPCGYSMNGIEGDA-IS 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 74275346  241 TIHITPEPEFSYVSFET---NLSQTSYDDLIRKVVEVFKPGKFVTTLFVN 287
Cdd:PLN02524 245 TIHVTPEDGFSYASFEAmgyDPGDLDLSQLVERVLACFKPKEFSVAVHAN 294
 
Name Accession Description Interval E-value
SAM_decarbox pfam01536
Adenosylmethionine decarboxylase; This is a family of S-adenosylmethionine decarboxylase ...
4-325 0e+00

Adenosylmethionine decarboxylase; This is a family of S-adenosylmethionine decarboxylase (SAMDC) proenzymes. In the biosynthesis of polyamines SAMDC produces decarboxylated S-adenosylmethionine, which serves as the aminopropyl moiety necessary for spermidine and spermine biosynthesis from putrescine. The Pfam alignment contains both the alpha and beta chains that are cleaved to form the active enzyme.


Pssm-ID: 460243  Cd Length: 331  Bit Score: 513.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346     4 AHFFEGTEKLLEVWFSRQQPDA-NQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTC 82
Cdd:pfam01536   1 TIAFEGPEKLLEIWFSPSSGFIpSGDEGGLRSIPREKWEEILDLVKCEILSVKSNDKVDAYVLSESSLFVYPHKIILKTC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346    83 GTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTL 162
Cdd:pfam01536  81 GTTTLLLCLPPLLELAKEELGFLEVYKVFYSRKNFMFPEKQPSPHRSFSEEVAYLDKFFPNGKAYVVGRMNSDHWHLYTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346   163 DFPESRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYWTI 242
Cdd:pfam01536 161 SDPESLSSPEPDQTLEILMTGLDPEKAKQFYKDGHVSGAEMTKASGIDDILPGSIIDDFAFDPCGYSMNGIEGDGAYSTI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346   243 HITPEPEFSYVSFETNLSQ---TSYDDLIRKVVEVFKPGKFVTTLFVNQSSK-----CRTVLASPQKIEGFKRLDCQSAM 314
Cdd:pfam01536 241 HVTPEDGFSYASFETNVPYdpeVDYSDLIRKVLKVFKPGKFSVTLFANSSSPswakcLKLDVSKLQKLGGYKRLDRIVYE 320
                         330
                  ....*....|.
gi 74275346   315 FNDYNFVFTSF 325
Cdd:pfam01536 321 LDGYSLVYQSF 331
SAM_DCase TIGR00535
S-adenosylmethionine decarboxylase proenzyme, eukaryotic form; This enzyme is a key regulatory ...
7-328 8.89e-89

S-adenosylmethionine decarboxylase proenzyme, eukaryotic form; This enzyme is a key regulatory enzyme of the polyamine synthetic pathway. This protein is a pyruvoyl-dependent enzyme. The proenzyme is cleaved at a Ser residue that becomes a pyruvoyl group active site. [Central intermediary metabolism, Polyamine biosynthesis]


Pssm-ID: 273124  Cd Length: 334  Bit Score: 269.41  E-value: 8.89e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346     7 FEGTEKLLEVWFSRQQPDANQGSGdLRTIPRSEWDILLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTL 86
Cdd:TIGR00535   1 FEGPEKLLEIWFFEHKKFIDEGKG-LRAIGRAQIDEILDLARCTILSSKKNKSLDSYVLSESSLFIYDHKIIIKTCGTTK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346    87 LLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDC-WYLYTLDF- 164
Cdd:TIGR00535  80 LLFALPKILQLAEQLSSWYKVFSVFYSRGCFLFPCAQPAIHRNFSEEVAYLNKFFGNGKAYVVGDPAKPQkWHLYVAETe 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346   165 PESRVISQPDQTLEILMSELDPAVMDQFYMKDGVT----AKDVTRESGIRDLIP-GSVIDATMFNPCGYSMNGMKSDGTY 239
Cdd:TIGR00535 160 RETPKIEDPDETLEMLMTGLDKEKASKFFKGPAASthnlGYQMTKNSGIDKIIPnSAQICDFDFEPCGYSMNAILGEKAY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346   240 WTIHITPEPEFSYVSFETN---LSQTSYDDLIRKVVEVFKPGKFVTTLFVN--QSSKCRTVLASPQKIEGFKRLDCQSAM 314
Cdd:TIGR00535 240 STIHVTPEKGFSYASFESNgidQGKQDYLDLVLRVLNCFQPSEFSMTVFAKnyQNQSFQKLLSINESLPDYIKLDKQELD 319
                         330
                  ....*....|....
gi 74275346   315 FNDYNFVFTSFAKK 328
Cdd:TIGR00535 320 LGDYHLFYQKFQKK 333
PLN02524 PLN02524
S-adenosylmethionine decarboxylase
7-287 2.22e-82

S-adenosylmethionine decarboxylase


Pssm-ID: 215287  Cd Length: 355  Bit Score: 253.78  E-value: 2.22e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346    7 FEGTEKLLEVWFSRQQPDANQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTL 86
Cdd:PLN02524   8 FEGFEKRLEITFFEPPVFADPNGRGLRALTRSQLDEILRPAECTIVSSLSNDQFDSYVLSESSLFVYPYKIIIKTCGTTK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346   87 LLKALVPLLKLARDYSgfDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPN----GAAYCMG-RMNSDCWYLYT 161
Cdd:PLN02524  88 LLLSIPPLLELAARLS--LSVRSVKYTRGSFIFPGAQPFPHRSFSEEVSVLDGHFGKlglgGKAYVMGdPDKGQKWHVYS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74275346  162 LDFPESRVISQPDQTLEILMSELDPAVMDQFYMK-DGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGtYW 240
Cdd:PLN02524 166 ASAHNSSNSNEPVYTLEMCMTGLDREKASVFFKDsSLSSAEEMTKASGIRKILPESEICDFAFDPCGYSMNGIEGDA-IS 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 74275346  241 TIHITPEPEFSYVSFET---NLSQTSYDDLIRKVVEVFKPGKFVTTLFVN 287
Cdd:PLN02524 245 TIHVTPEDGFSYASFEAmgyDPGDLDLSQLVERVLACFKPKEFSVAVHAN 294
 
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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