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Conserved domains on  [gi|1981092575|ref|NP_001380336|]
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S-adenosylmethionine decarboxylase proenzyme isoform 6 [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 ...
1-208 1.62e-120

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: 344.90  E-value: 1.62e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981092575   1 MKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYMKDG 80
Cdd:pfam01536 116 MFPEKQPSPHRSFSEEVAYLDKFFPNGKAYVVGRMNSDHWHLYTASDPESLSSPEPDQTLEILMTGLDPEKAKQFYKDGH 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981092575  81 VTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQ---TSYDDLIRKVVEV 157
Cdd:pfam01536 196 VSGAEMTKASGIDDILPGSIIDDFAFDPCGYSMNGIEGDGAYSTIHVTPEDGFSYASFETNVPYdpeVDYSDLIRKVLKV 275
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1981092575 158 FKPGKFVTTLFVNQSSK-----CRTVLASPQKIEGFKRLDCQSAMFNDYNFVFTSF 208
Cdd:pfam01536 276 FKPGKFSVTLFANSSSPswakcLKLDVSKLQKLGGYKRLDRIVYELDGYSLVYQSF 331
 
Name Accession Description Interval E-value
SAM_decarbox pfam01536
Adenosylmethionine decarboxylase; This is a family of S-adenosylmethionine decarboxylase ...
1-208 1.62e-120

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: 344.90  E-value: 1.62e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981092575   1 MKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYMKDG 80
Cdd:pfam01536 116 MFPEKQPSPHRSFSEEVAYLDKFFPNGKAYVVGRMNSDHWHLYTASDPESLSSPEPDQTLEILMTGLDPEKAKQFYKDGH 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981092575  81 VTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQ---TSYDDLIRKVVEV 157
Cdd:pfam01536 196 VSGAEMTKASGIDDILPGSIIDDFAFDPCGYSMNGIEGDGAYSTIHVTPEDGFSYASFETNVPYdpeVDYSDLIRKVLKV 275
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1981092575 158 FKPGKFVTTLFVNQSSK-----CRTVLASPQKIEGFKRLDCQSAMFNDYNFVFTSF 208
Cdd:pfam01536 276 FKPGKFSVTLFANSSSPswakcLKLDVSKLQKLGGYKRLDRIVYELDGYSLVYQSF 331
PLN02524 PLN02524
S-adenosylmethionine decarboxylase
3-170 2.38e-52

S-adenosylmethionine decarboxylase


Pssm-ID: 215287  Cd Length: 355  Bit Score: 172.11  E-value: 2.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981092575   3 PSHQGYPHRNFQEEIEFLNAIFPN----GAAYCMG-RMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYM 77
Cdd:PLN02524  119 PGAQPFPHRSFSEEVSVLDGHFGKlglgGKAYVMGdPDKGQKWHVYSASAHNSSNSNEPVYTLEMCMTGLDREKASVFFK 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981092575  78 K-DGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGtYWTIHITPEPEFSYVSFET---NLSQTSYDDLIRK 153
Cdd:PLN02524  199 DsSLSSAEEMTKASGIRKILPESEICDFAFDPCGYSMNGIEGDA-ISTIHVTPEDGFSYASFEAmgyDPGDLDLSQLVER 277
                         170
                  ....*....|....*..
gi 1981092575 154 VVEVFKPGKFVTTLFVN 170
Cdd:PLN02524  278 VLACFKPKEFSVAVHAN 294
SAM_DCase TIGR00535
S-adenosylmethionine decarboxylase proenzyme, eukaryotic form; This enzyme is a key regulatory ...
3-211 2.99e-50

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: 166.18  E-value: 2.99e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981092575   3 PSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDC-WYLYTLDF-PESRVISQPDQTLEILMSELDPAVMDQFYMKDG 80
Cdd:TIGR00535 113 PCAQPAIHRNFSEEVAYLNKFFGNGKAYVVGDPAKPQkWHLYVAETeRETPKIEDPDETLEMLMTGLDKEKASKFFKGPA 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981092575  81 VT----AKDVTRESGIRDLIP-GSVIDATMFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETN---LSQTSYDDLIR 152
Cdd:TIGR00535 193 ASthnlGYQMTKNSGIDKIIPnSAQICDFDFEPCGYSMNAILGEKAYSTIHVTPEKGFSYASFESNgidQGKQDYLDLVL 272
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1981092575 153 KVVEVFKPGKFVTTLFVN--QSSKCRTVLASPQKIEGFKRLDCQSAMFNDYNFVFTSFAKK 211
Cdd:TIGR00535 273 RVLNCFQPSEFSMTVFAKnyQNQSFQKLLSINESLPDYIKLDKQELDLGDYHLFYQKFQKK 333
 
Name Accession Description Interval E-value
SAM_decarbox pfam01536
Adenosylmethionine decarboxylase; This is a family of S-adenosylmethionine decarboxylase ...
1-208 1.62e-120

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: 344.90  E-value: 1.62e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981092575   1 MKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYMKDG 80
Cdd:pfam01536 116 MFPEKQPSPHRSFSEEVAYLDKFFPNGKAYVVGRMNSDHWHLYTASDPESLSSPEPDQTLEILMTGLDPEKAKQFYKDGH 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981092575  81 VTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQ---TSYDDLIRKVVEV 157
Cdd:pfam01536 196 VSGAEMTKASGIDDILPGSIIDDFAFDPCGYSMNGIEGDGAYSTIHVTPEDGFSYASFETNVPYdpeVDYSDLIRKVLKV 275
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1981092575 158 FKPGKFVTTLFVNQSSK-----CRTVLASPQKIEGFKRLDCQSAMFNDYNFVFTSF 208
Cdd:pfam01536 276 FKPGKFSVTLFANSSSPswakcLKLDVSKLQKLGGYKRLDRIVYELDGYSLVYQSF 331
PLN02524 PLN02524
S-adenosylmethionine decarboxylase
3-170 2.38e-52

S-adenosylmethionine decarboxylase


Pssm-ID: 215287  Cd Length: 355  Bit Score: 172.11  E-value: 2.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981092575   3 PSHQGYPHRNFQEEIEFLNAIFPN----GAAYCMG-RMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYM 77
Cdd:PLN02524  119 PGAQPFPHRSFSEEVSVLDGHFGKlglgGKAYVMGdPDKGQKWHVYSASAHNSSNSNEPVYTLEMCMTGLDREKASVFFK 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981092575  78 K-DGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGtYWTIHITPEPEFSYVSFET---NLSQTSYDDLIRK 153
Cdd:PLN02524  199 DsSLSSAEEMTKASGIRKILPESEICDFAFDPCGYSMNGIEGDA-ISTIHVTPEDGFSYASFEAmgyDPGDLDLSQLVER 277
                         170
                  ....*....|....*..
gi 1981092575 154 VVEVFKPGKFVTTLFVN 170
Cdd:PLN02524  278 VLACFKPKEFSVAVHAN 294
SAM_DCase TIGR00535
S-adenosylmethionine decarboxylase proenzyme, eukaryotic form; This enzyme is a key regulatory ...
3-211 2.99e-50

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: 166.18  E-value: 2.99e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981092575   3 PSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDC-WYLYTLDF-PESRVISQPDQTLEILMSELDPAVMDQFYMKDG 80
Cdd:TIGR00535 113 PCAQPAIHRNFSEEVAYLNKFFGNGKAYVVGDPAKPQkWHLYVAETeRETPKIEDPDETLEMLMTGLDKEKASKFFKGPA 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981092575  81 VT----AKDVTRESGIRDLIP-GSVIDATMFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETN---LSQTSYDDLIR 152
Cdd:TIGR00535 193 ASthnlGYQMTKNSGIDKIIPnSAQICDFDFEPCGYSMNAILGEKAYSTIHVTPEKGFSYASFESNgidQGKQDYLDLVL 272
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1981092575 153 KVVEVFKPGKFVTTLFVN--QSSKCRTVLASPQKIEGFKRLDCQSAMFNDYNFVFTSFAKK 211
Cdd:TIGR00535 273 RVLNCFQPSEFSMTVFAKnyQNQSFQKLLSINESLPDYIKLDKQELDLGDYHLFYQKFQKK 333
 
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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