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O31550 (ACOC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system

EC=2.3.1.12
Alternative name(s):
Acetoin dehydrogenase E2 component
Dihydrolipoamide acetyltransferase component of acetoin cleaving system
Gene names
Name:acoC
Synonyms:yfjI
Ordered Locus Names:BSU08080
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactor

Binds 1 lipoyl cofactor covalently By similarity.

Pathway

Ketone degradation; acetoin degradation.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Ontologies

Keywords
   Biological processAcetoin catabolism
   DomainLipoyl
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacetoin catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functiondihydrolipoyllysine-residue acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 398398Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system
PRO_0000162306

Regions

Domain1 – 7676Lipoyl-binding

Sites

Active site3711 Potential
Active site3751 Potential

Amino acid modifications

Modified residue431N6-lipoyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O31550 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 559564C27C1C64F6

FASTA39842,886
        10         20         30         40         50         60 
MAVKVVMPKL GMAMKQGEVS IWNKKVGDPV EKGESIASIQ SEKIEMEIEA PEKGTLIDIK 

        70         80         90        100        110        120 
VKEGEEVPPG TAICYIGDAN ESVQEEAGAP VAEDNMPQAV QPVKQENKPA ASKKDRMKIS 

       130        140        150        160        170        180 
PVARKIAEKA GLDLKQLKGT GPGGRIVKDD VTKALAEQKK DQAKPVSEQK AQEIPVTGMR 

       190        200        210        220        230        240 
KVIAARMQES LANSAQLTIT MKADITKLAT LQKQLSPTAE ERYGTKLTIT HFVSRAAVLA 

       250        260        270        280        290        300 
LQAHPVLNSF YQNERIITHP HVHLGMAVAL ENGLVVPVIR HAEKLSLIEL AQSISENAKK 

       310        320        330        340        350        360 
AREGRAGSEE LQGSTFSITN LGAFGVEHFT PILNPPETGI LGIGASYDTP VYQGEEIVRS 

       370        380        390 
TILPLSLTFD HRACDGAPAA AFLKAMKTYL EEPAALIL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76 degrees region of the Bacillus subtilis chromosome containing genes for trehalose metabolism and acetoin utilization."
Yamamoto H., Uchiyama S., Sekiguchi J.
Microbiology 142:3057-3065(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / AC327.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D78509 Genomic DNA. Translation: BAA24294.1.
AL009126 Genomic DNA. Translation: CAB12637.1.
PIRF69581.
RefSeqNP_388689.1. NC_000964.3.

3D structure databases

ProteinModelPortalO31550.
SMRO31550. Positions 16-77, 118-155, 162-398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO31550. 4 interactions.
STRING224308.BSU08080.

Proteomic databases

PaxDbO31550.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12637; CAB12637; BSU08080.
GeneID936147.
KEGGbsu:BSU08080.
PATRIC18973266. VBIBacSub10457_0847.

Organism-specific databases

GenoListBSU08080. [Micado]

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281566.
KOK00627.
OMAKSTRISV.
OrthoDBEOG610413.
ProtClustDBPRK11856.

Enzyme and pathway databases

BioCycBSUB:BSU08080-MONOMER.
UniPathwayUPA00040.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACOC_BACSU
AccessionPrimary (citable) accession number: O31550
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList