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Q2JWR6

- Q2JWR6_SYNJA

UniProt

Q2JWR6 - Q2JWR6_SYNJA

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Protein
S-adenosylmethionine decarboxylase proenzyme
Gene
speH, CYA_0574
Organism
Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime)
Status
Unreviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Pyruvoyl group By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei75 – 762Cleavage (non-hydrolytic); by autolysis By similarityUniRule annotation
Active sitei76 – 761Schiff-base intermediate with substrate; via pyruvic acid By similarityUniRule annotation
Active sitei81 – 811Proton acceptor; for processing activity By similarityUniRule annotation
Active sitei96 – 961Proton donor; for catalytic activity By similarityUniRule annotation

GO - Molecular functioni

  1. adenosylmethionine decarboxylase activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

DecarboxylaseUniRule annotation, Lyase

Keywords - Biological processi

Polyamine biosynthesisUniRule annotation, Spermidine biosynthesisUniRule annotationSAAS annotations

Keywords - Ligandi

PyruvateUniRule annotation, S-adenosyl-L-methionineUniRule annotationSAAS annotations, Schiff baseUniRule annotation

Enzyme and pathway databases

BioCyciSSP321327:GHFX-570-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
Gene namesi
Name:speHUniRule annotation
Ordered Locus Names:CYA_0574Imported
OrganismiSynechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime)Imported
Taxonomic identifieri321327 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000008818: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 761Pyruvic acid (Ser); by autocatalysis By similarityUniRule 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 By similarity.UniRule annotation

Keywords - PTMi

Autocatalytic cleavageUniRule annotation, ZymogenUniRule annotation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi321327.CYA_0574.

Structurei

3D structure databases

ProteinModelPortaliQ2JWR6.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000216579.
KOiK01611.
OMAiGNLYGCN.
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.

Q2JWR6-1 [UniParc]FASTAAdd to Basket

« Hide

MLHTLSGQLG DRSLALIGIH CILELYDCPA KLLDDVSLVQ QALREAARRS    50
NSTLLGELCH PFEPQGITAL ALLGESHISI HTWPEAGYAA VDVFTCGRHT 100
RPEAACEYLI QVFQARRYSL RKLPRRTTDA APIEEMADFP KALSCETAGR 150
RR 152
Length:152
Mass (Da):16,870
Last modified:March 7, 2006 - v1
Checksum:i8A9D3D82BB8AF51A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000239 Genomic DNA. Translation: ABC98790.1.
RefSeqiWP_011429477.1. NC_007775.1.
YP_474053.1. NC_007775.1.

Genome annotation databases

EnsemblBacteriaiABC98790; ABC98790; CYA_0574.
GeneIDi3897371.
KEGGicya:CYA_0574.
PATRICi23809415. VBISynSp90045_0572.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000239 Genomic DNA. Translation: ABC98790.1 .
RefSeqi WP_011429477.1. NC_007775.1.
YP_474053.1. NC_007775.1.

3D structure databases

ProteinModelPortali Q2JWR6.
ModBasei Search...

Protein-protein interaction databases

STRINGi 321327.CYA_0574.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABC98790 ; ABC98790 ; CYA_0574 .
GeneIDi 3897371.
KEGGi cya:CYA_0574.
PATRICi 23809415. VBISynSp90045_0572.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00331 ; UER00451 .
BioCyci SSP321327:GHFX-570-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. "Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
    Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
    ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JA-3-3AbImported.

Entry informationi

Entry nameiQ2JWR6_SYNJA
AccessioniPrimary (citable) accession number: Q2JWR6
Entry historyi
Integrated into UniProtKB/TrEMBL: March 7, 2006
Last sequence update: March 7, 2006
Last modified: September 3, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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