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Reviewed, UniProtKB/Swiss-Prot O31550 (ACOC_BACSU)

Last modified November 25, 2008. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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Ontologies

Keywords

   Biological processAcetoin catabolism
   DomainLipoyl
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processacetoin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiondihydrolipoyllysine-residue acetyltransferase activity

Inferred from electronic annotation. Source: EC

lipoic acid binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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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
Binding site431Lipoyl (covalent) By similarity

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Sequences

Sequence LengthMass (Da)Tools
O31550-1 [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

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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: 8969503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 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: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

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Cross-references

Sequence databases

D78509 Genomic DNA. Translation: BAA24294.1.
Z99108 Genomic DNA. Translation: CAB12637.1.
PIRF69581.
RefSeqNP_388689.1.

3D structure databases

HSSPHSSP built from PDB template 1BBL based on UniProtKB P07016.
ModBaseSearch...

Genome annotation databases

GeneID936147.
GenomeReviewsGene locus BSU08080 in contig AL009126_GR.
KEGGbsu:BSU08080.
NMPDRfig|224308.1.peg.808.

Organism-specific databases

SubtiListBG12560. acoC. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMO31550.

Enzyme and pathway databases

BioCycBSUB224308:BSU0808-MON.

Family and domain databases

InterProIPR003016. 2-oxoA_DHase_lipoyl-BS.
IPR001078. 2Oxoacid_DHase.
IPR000089. Biotin_lipoyl.
IPR004167. E3_bd.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
ProDomPD001115. 2Oxoacid_dh. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. False negative.
[Graphical view]
ProtoNetSearch...

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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: November 25, 2008
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents