SubmitCancel

Skip Header

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

A8ALG9

- SPED_CITK8

UniProt

A8ALG9 - SPED_CITK8

(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
speD, CKO_03248
Organism
Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Pyruvoyl group By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei111 – 1122Cleavage (non-hydrolytic); by autolysis By similarity
Active sitei112 – 1121Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active sitei117 – 1171Proton acceptor; for processing activity By similarity
Active sitei140 – 1401Proton donor; for catalytic activity By similarity

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

BioCyciCKOS290338:GJ8L-3241-MONOMER.
UniPathwayiUPA00331; UER00451.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine decarboxylase proenzyme (EC:4.1.1.50)
Short name:
AdoMetDC
Short name:
SAMDC
Cleaved into the following 2 chains:
Gene namesi
Name:speD
Ordered Locus Names:CKO_03248
OrganismiCitrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
Taxonomic identifieri290338 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacter
ProteomesiUP000008148: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 111111S-adenosylmethionine decarboxylase beta chain By similarity
PRO_1000013688Add
BLAST
Chaini112 – 264153S-adenosylmethionine decarboxylase alpha chain By similarity
PRO_0000315014Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei112 – 1121Pyruvic acid (Ser); by autocatalysis By similarity

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 cleavage, Zymogen

Proteomic databases

PRIDEiA8ALG9.

Interactioni

Subunit structurei

Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers By similarity.

Protein-protein interaction databases

STRINGi290338.CKO_03248.

Structurei

3D structure databases

ProteinModelPortaliA8ALG9.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000116821.
KOiK01611.
OMAiVKHYIDH.
OrthoDBiEOG68Q0SQ.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
HAMAPiMF_00465. AdoMetDC_2.
InterProiIPR003826. AdoMetDC_fam_prok.
IPR009165. S-AdoMet_deCO2ase_bac.
IPR016067. S-AdoMet_deCO2ase_core.
[Graphical view]
PfamiPF02675. AdoMet_dc. 1 hit.
[Graphical view]
PIRSFiPIRSF001356. SAM_decarboxylas. 1 hit.
SUPFAMiSSF56276. SSF56276. 2 hits.
TIGRFAMsiTIGR03331. SAM_DCase_Eco. 1 hit.

Sequencei

Sequence statusi: Complete.

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

A8ALG9-1 [UniParc]FASTAAdd to Basket

« Hide

MKKLKLHGFN NLTKSLSFCI YDICYAKTAE ERDGYIAYID ELYNANRLTE    50
ILSETCSIIG ANILNIARQD YEPQGASVTI LVSEEPVDPQ LIDKTEHPGP 100
LPEAVVAHLD KSHICVHTYP ESHPEGGLCT FRADIEVSTC GVISPLKALN 150
YLIHQLESDI VTIDYRVRGF TRDVNGMKHF IDHEINSIQN FMSDDMKSLY 200
DMVDVNVYQE NIFHTKMLLK EFDLKHYMFH TKPEDLTETE RKEITAALWK 250
EMREIYYGRN IPAV 264
Length:264
Mass (Da):30,367
Last modified:October 23, 2007 - v1
Checksum:iEFA8ACA5EE924EA1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000822 Genomic DNA. Translation: ABV14332.1.
RefSeqiWP_012134037.1. NC_009792.1.
YP_001454768.1. NC_009792.1.

Genome annotation databases

EnsemblBacteriaiABV14332; ABV14332; CKO_03248.
GeneIDi5583015.
KEGGicko:CKO_03248.
PATRICi20389092. VBICitKos71230_2724.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000822 Genomic DNA. Translation: ABV14332.1 .
RefSeqi WP_012134037.1. NC_009792.1.
YP_001454768.1. NC_009792.1.

3D structure databases

ProteinModelPortali A8ALG9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 290338.CKO_03248.

Proteomic databases

PRIDEi A8ALG9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABV14332 ; ABV14332 ; CKO_03248 .
GeneIDi 5583015.
KEGGi cko:CKO_03248.
PATRICi 20389092. VBICitKos71230_2724.

Phylogenomic databases

eggNOGi COG1586.
HOGENOMi HOG000116821.
KOi K01611.
OMAi VKHYIDH.
OrthoDBi EOG68Q0SQ.

Enzyme and pathway databases

UniPathwayi UPA00331 ; UER00451 .
BioCyci CKOS290338:GJ8L-3241-MONOMER.

Family and domain databases

Gene3Di 3.60.90.10. 1 hit.
HAMAPi MF_00465. AdoMetDC_2.
InterProi IPR003826. AdoMetDC_fam_prok.
IPR009165. S-AdoMet_deCO2ase_bac.
IPR016067. S-AdoMet_deCO2ase_core.
[Graphical view ]
Pfami PF02675. AdoMet_dc. 1 hit.
[Graphical view ]
PIRSFi PIRSF001356. SAM_decarboxylas. 1 hit.
SUPFAMi SSF56276. SSF56276. 2 hits.
TIGRFAMsi TIGR03331. SAM_DCase_Eco. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-895 / CDC 4225-83 / SGSC4696.

Entry informationi

Entry nameiSPED_CITK8
AccessioniPrimary (citable) accession number: A8ALG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: September 3, 2014
This is version 39 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

Documents

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

External Data

Dasty 3

Similar proteinsi