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O31550

- ACOC_BACSU

UniProt

O31550 - ACOC_BACSU

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Protein

Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system

Gene

acoC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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

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: 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-lipoyllysineBy similarity

Proteomic databases

PaxDbiO31550.

Interactioni

Protein-protein interaction databases

IntActiO31550. 4 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
Domaini1 – 7676Lipoyl-bindingAdd
BLAST

Sequence similaritiesi

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

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:
EMBL
GenBank
DDBJ
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_CM000487.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D78509 Genomic DNA. Translation: BAA24294.1 .
AL009126 Genomic DNA. Translation: CAB12637.1 .
PIRi F69581.
RefSeqi NP_388689.1. NC_000964.3.
WP_003244059.1. NZ_CM000487.1.

3D structure databases

ProteinModelPortali O31550.
SMRi O31550. Positions 16-77, 118-155, 162-398.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O31550. 4 interactions.
STRINGi 224308.BSU08080.

Proteomic databases

PaxDbi O31550.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12637 ; CAB12637 ; BSU08080 .
GeneIDi 936147.
KEGGi bsu:BSU08080.
PATRICi 18973266. VBIBacSub10457_0847.

Organism-specific databases

GenoListi BSU08080. [Micado ]

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281566.
InParanoidi O31550.
KOi K00627.
OMAi VESCIIT.
OrthoDBi EOG610413.
PhylomeDBi O31550.

Enzyme and pathway databases

UniPathwayi UPA00040 .
BioCyci BSUB:BSU08080-MONOMER.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 111 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