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Protein

Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system

Gene

acoC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei371 – 3711Sequence Analysis
Active sitei375 – 3751Sequence Analysis

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. acetoin catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Acetoin catabolism

Enzyme and pathway databases

BioCyciBSUB:BSU08080-MONOMER.
UniPathwayiUPA00040.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:acoC
Synonyms:yfjI
Ordered Locus Names:BSU08080
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU08080. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 398398Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving systemPRO_0000162306Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431N6-lipoyllysinePROSITE-ProRule annotationBy similarity

Proteomic databases

PaxDbiO31550.

Interactioni

Protein-protein interaction databases

IntActiO31550. 6 interactions.
STRINGi224308.BSU08080.

Structurei

3D structure databases

ProteinModelPortaliO31550.
SMRiO31550. Positions 16-77, 118-155, 162-398.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7776Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
InParanoidiO31550.
KOiK00627.
OMAiVESCIIT.
OrthoDBiEOG610413.
PhylomeDBiO31550.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O31550-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVKVVMPKL GMAMKQGEVS IWNKKVGDPV EKGESIASIQ SEKIEMEIEA
60 70 80 90 100
PEKGTLIDIK VKEGEEVPPG TAICYIGDAN ESVQEEAGAP VAEDNMPQAV
110 120 130 140 150
QPVKQENKPA ASKKDRMKIS PVARKIAEKA GLDLKQLKGT GPGGRIVKDD
160 170 180 190 200
VTKALAEQKK DQAKPVSEQK AQEIPVTGMR KVIAARMQES LANSAQLTIT
210 220 230 240 250
MKADITKLAT LQKQLSPTAE ERYGTKLTIT HFVSRAAVLA LQAHPVLNSF
260 270 280 290 300
YQNERIITHP HVHLGMAVAL ENGLVVPVIR HAEKLSLIEL AQSISENAKK
310 320 330 340 350
AREGRAGSEE LQGSTFSITN LGAFGVEHFT PILNPPETGI LGIGASYDTP
360 370 380 390
VYQGEEIVRS TILPLSLTFD HRACDGAPAA AFLKAMKTYL EEPAALIL
Length:398
Mass (Da):42,886
Last modified:January 1, 1998 - v1
Checksum:i559564C27C1C64F6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78509 Genomic DNA. Translation: BAA24294.1.
AL009126 Genomic DNA. Translation: CAB12637.1.
PIRiF69581.
RefSeqiNP_388689.1. NC_000964.3.
WP_003244059.1. NZ_JNCM01000032.1.

Genome annotation databases

EnsemblBacteriaiCAB12637; CAB12637; BSU08080.
GeneIDi936147.
KEGGibsu:BSU08080.
PATRICi18973266. VBIBacSub10457_0847.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78509 Genomic DNA. Translation: BAA24294.1.
AL009126 Genomic DNA. Translation: CAB12637.1.
PIRiF69581.
RefSeqiNP_388689.1. NC_000964.3.
WP_003244059.1. NZ_JNCM01000032.1.

3D structure databases

ProteinModelPortaliO31550.
SMRiO31550. Positions 16-77, 118-155, 162-398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO31550. 6 interactions.
STRINGi224308.BSU08080.

Proteomic databases

PaxDbiO31550.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12637; CAB12637; BSU08080.
GeneIDi936147.
KEGGibsu:BSU08080.
PATRICi18973266. VBIBacSub10457_0847.

Organism-specific databases

GenoListiBSU08080. [Micado]

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
InParanoidiO31550.
KOiK00627.
OMAiVESCIIT.
OrthoDBiEOG610413.
PhylomeDBiO31550.

Enzyme and pathway databases

UniPathwayiUPA00040.
BioCyciBSUB:BSU08080-MONOMER.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiACOC_BACSU
AccessioniPrimary (citable) accession number: O31550
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 113 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, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.