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A1VYP3 (A1VYP3_CAMJJ) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Succinyl-CoA ligase [ADP-forming] subunit alpha RuleBase RU000699
EC=6.2.1.5 RuleBase RU000699
Gene names
Name:sucD EMBL EAQ72982.1
Ordered Locus Names:CJJ81176_0559 EMBL EAQ72982.1
OrganismCampylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) [Complete proteome] [HAMAP] EMBL EAQ72982.1
Taxonomic identifier354242 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter ›

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. RuleBase RU000699

Subunit structure

Heterotetramer of two alpha and two beta subunits By similarity. RuleBase RU000699

Sequence similarities

Belongs to the succinate/malate CoA ligase alpha subunit family. RuleBase RU000677

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site2471Tele-phosphohistidine intermediate By similarity PIRSR PIRSR001553-1

Sequences

Sequence LengthMass (Da)Tools
A1VYP3 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 05FDA005D3FCF3A2

FASTA28930,007
        10         20         30         40         50         60 
MSILVNKNTK VIVQGFTGKE ATFHAEQCMA YGTNIVGGVT PHKGGQTHLG KPVFDTVADA 

        70         80         90        100        110        120 
VKATKADVSL IFVPAFAVGD SVIEAADAGI KLAVVITEHT PVKDMMFAKQ YANKKGMKII 

       130        140        150        160        170        180 
GPNCPGIITS EECKLGIMPG FIFKKGCVGL ISKSGTLTYE AANQVVQGGY GISTAVGIGG 

       190        200        210        220        230        240 
DPIIGLAYKE LLSEFQKDDE TKAIVMIGEI GGSLEVEAAK FIKENISKPV VAFIAGATAP 

       250        260        270        280 
KGKRMGHAGA IVGSADESAA AKKEALKSYG IHVVDSPALI GEEIQKILG

« Hide

References

[1]Fouts D.E., Nelson K.E., Sebastian Y.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 81-176.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000538 Genomic DNA. Translation: EAQ72982.1.
RefSeqYP_001000234.1. NC_008787.1.

3D structure databases

ProteinModelPortalA1VYP3.
SMRA1VYP3. Positions 2-285.
ModBaseSearch...

Protein-protein interaction databases

STRING354242.CJJ81176_0559.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEAQ72982; EAQ72982; CJJ81176_0559.
GeneID4682288.
KEGGcjj:CJJ81176_0559.
PATRIC20051071. VBICamJej103413_0567.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0074.
HOGENOMHOG000239685.
KOK01902.
OMADAGIKYC.
ProtClustDBCLSK878826.

Enzyme and pathway databases

BioCycCJEJ354242:GC51-532-MONOMER.

Family and domain databases

Gene3D3.40.50.261. 1 hit.
3.40.50.720. 1 hit.
InterProIPR017440. Cit_synth/succinyl-CoA_lig_AS.
IPR003781. CoA-bd.
IPR005810. CoA_lig_alpha.
IPR005811. CoA_ligase.
IPR016040. NAD(P)-bd_dom.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PfamPF02629. CoA_binding. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFPIRSF001553. SucCS_alpha. 1 hit.
PRINTSPR01798. SCOASYNTHASE.
SMARTSM00881. CoA_binding. 1 hit.
[Graphical view]
SUPFAMSSF52210. CoA_ligase. 1 hit.
TIGRFAMsTIGR01019. sucCoAalpha. 1 hit.
PROSITEPS01216. SUCCINYL_COA_LIG_1. 1 hit.
PS00399. SUCCINYL_COA_LIG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA1VYP3_CAMJJ
AccessionPrimary (citable) accession number: A1VYP3
Entry history
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: May 29, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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