Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A4XJ25

- SPEH_CALS8

UniProt

A4XJ25 - SPEH_CALS8

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

speH

Organism
Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.UniRule annotation

Catalytic activityi

S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2.UniRule annotation

Cofactori

Pyruvoyl group.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei62 – 632Cleavage (non-hydrolytic); by autolysisUniRule annotation
Active sitei63 – 631Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
Active sitei68 – 681Proton acceptor; for processing activityUniRule annotation
Active sitei83 – 831Proton donor; for catalytic activityUniRule annotation

GO - Molecular functioni

  1. adenosylmethionine decarboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. S-adenosylmethioninamine biosynthetic process Source: UniProtKB-HAMAP
  2. spermidine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Pyruvate, S-adenosyl-L-methionine, Schiff base

Enzyme and pathway databases

BioCyciCSAC351627:GJ17-1341-MONOMER.
UniPathwayiUPA00331; UER00451.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine decarboxylase proenzymeUniRule annotation (EC:4.1.1.50UniRule annotation)
Short name:
AdoMetDCUniRule annotation
Short name:
SAMDCUniRule annotation
Cleaved into the following 2 chains:
S-adenosylmethionine decarboxylase beta chainUniRule annotation
S-adenosylmethionine decarboxylase alpha chainUniRule annotation
Gene namesi
Name:speHUniRule annotation
Ordered Locus Names:Csac_1308
OrganismiCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903)
Taxonomic identifieri351627 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor
ProteomesiUP000000256: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6262S-adenosylmethionine decarboxylase beta chainUniRule annotationPRO_1000013670Add
BLAST
Chaini63 – 12462S-adenosylmethionine decarboxylase alpha chainUniRule annotationPRO_0000315023Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei63 – 631Pyruvic acid (Ser); by autocatalysisUniRule annotation

Post-translational modificationi

Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.UniRule annotation

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.UniRule annotation

Protein-protein interaction databases

STRINGi351627.Csac_1308.

Structurei

3D structure databases

ProteinModelPortaliA4XJ25.
SMRiA4XJ25. Positions 3-117.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000216579.
KOiK01611.
OMAiHIANMHL.
OrthoDBiEOG6358J6.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
HAMAPiMF_00464. AdoMetDC_1.
InterProiIPR003826. AdoMetDC_fam_prok.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view]
PfamiPF02675. AdoMet_dc. 1 hit.
[Graphical view]
SUPFAMiSSF56276. SSF56276. 1 hit.
TIGRFAMsiTIGR03330. SAM_DCase_Bsu. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A4XJ25-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHALGRHIIA ELYGCDKEVL NNRELIEKIM VESALKAGAE VREVAFHKFS
60 70 80 90 100
PQGVSGVVVI SESHLTIHTW PELGYAAVDV FTCGERVDPW QACNYITEML
110 120
KASHMTTTEV KRGLFEQPVK VANL
Length:124
Mass (Da):13,837
Last modified:May 29, 2007 - v1
Checksum:i4EA13C00427B88B4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000679 Genomic DNA. Translation: ABP66910.1.
RefSeqiYP_001180101.1. NC_009437.1.

Genome annotation databases

EnsemblBacteriaiABP66910; ABP66910; Csac_1308.
GeneIDi5088248.
KEGGicsc:Csac_1308.
PATRICi21252290. VBICalSac56748_1456.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000679 Genomic DNA. Translation: ABP66910.1 .
RefSeqi YP_001180101.1. NC_009437.1.

3D structure databases

ProteinModelPortali A4XJ25.
SMRi A4XJ25. Positions 3-117.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 351627.Csac_1308.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABP66910 ; ABP66910 ; Csac_1308 .
GeneIDi 5088248.
KEGGi csc:Csac_1308.
PATRICi 21252290. VBICalSac56748_1456.

Phylogenomic databases

eggNOGi COG1586.
HOGENOMi HOG000216579.
KOi K01611.
OMAi HIANMHL.
OrthoDBi EOG6358J6.

Enzyme and pathway databases

UniPathwayi UPA00331 ; UER00451 .
BioCyci CSAC351627:GJ17-1341-MONOMER.

Family and domain databases

Gene3Di 3.60.90.10. 1 hit.
HAMAPi MF_00464. AdoMetDC_1.
InterProi IPR003826. AdoMetDC_fam_prok.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view ]
Pfami PF02675. AdoMet_dc. 1 hit.
[Graphical view ]
SUPFAMi SSF56276. SSF56276. 1 hit.
TIGRFAMsi TIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43494 / DSM 8903.

Entry informationi

Entry nameiSPEH_CALS8
AccessioniPrimary (citable) accession number: A4XJ25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: October 1, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3