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Protein

Biotin carboxylase 1

Gene

accC1

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.By similarity

Catalytic activityi

ATP + biotin-[carboxyl-carrier-protein] + HCO3- = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].
ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.

Pathway: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.
Proteins known to be involved in this subpathway in this organism are:
  1. Biotin carboxylase 2 (accC2), Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (accD), Biotin carboxylase 1 (accC1), Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA)
This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161ATPBy similarity
Binding sitei200 – 2001ATPBy similarity
Active sitei293 – 2931By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Biotin, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU24340-MONOMER.
UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin carboxylase 1 (EC:6.3.4.14)
Alternative name(s):
Acetyl-CoA carboxylase subunit A 1 (EC:6.4.1.2)
Short name:
ACC 1
Gene namesi
Name:accC1
Synonyms:accC, yqhX
Ordered Locus Names:BSU24340
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU24340. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Biotin carboxylase 1PRO_0000146789Add
BLAST

Proteomic databases

PaxDbiP49787.

Interactioni

Subunit structurei

Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl carrier protein, biotin carboxylase and the two subunits of carboxyl transferase in a 2:2 complex.By similarity

Protein-protein interaction databases

IntActiP49787. 1 interaction.
MINTiMINT-8365265.
STRINGi224308.Bsubs1_010100013351.

Structurei

3D structure databases

ProteinModelPortaliP49787.
SMRiP49787. Positions 3-448.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 447447Biotin carboxylationAdd
BLAST
Domaini120 – 318199ATP-graspPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
Contains 1 biotin carboxylation domain.Curated

Phylogenomic databases

eggNOGiCOG0439.
HOGENOMiHOG000008988.
InParanoidiP49787.
KOiK01961.
OMAiKDFYFME.
OrthoDBiEOG6CVV6Z.
PhylomeDBiP49787.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR004549. Acetyl_CoA_COase_biotin_COase.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR00514. accC. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P49787-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKKLLIANR GEIAVRIIRA CRELGIETVA VYSEADKDAL HVQMADEAFC
60 70 80 90 100
IGPKASKDSY LNVTNIVSVA KLTGTDAIHP GYGFLAENAD FAELCEEVNV
110 120 130 140 150
TFVGPSADAI SKMGTKDVAR ETMKQAGVPI VPGSQGIIEN VEEAVSLANE
160 170 180 190 200
IGYPVIIKAT AGGGGKGIRV ARTEEELING IKITQQEAAT AFGNPGVYIE
210 220 230 240 250
KYIEDFRHVE IQVLADNYGN TIHLGERDCS IQRRLQKLLE ESPSPALDSE
260 270 280 290 300
IREQMGDAAV KAAKAVGYTG AGTVEFIYDY NEQRYYFMEM NTRIQVEHPV
310 320 330 340 350
TEMVTGTDLI KEQIKVASGM ELSLKQEDVE FEGWAIECRI NAENPSKNFM
360 370 380 390 400
PSPGEIKMYL PPGGLGVRVD SAAYPGYSIP PYYDSMIAKV ITYGKTRDEA
410 420 430 440 450
IARMKRALSE FVIEGIETTI PFHLKLLEHE TFVSGEFNTK FLETYDVMGS
Length:450
Mass (Da):49,452
Last modified:July 7, 2009 - v3
Checksum:i2F93B3E793478334
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071A → P in BAA12569 (PubMed:8969508).Curated
Sequence conflicti193 – 1931G → R in BAA12569 (PubMed:8969508).Curated
Sequence conflicti240 – 2401E → G in AAB00183 (PubMed:7592499).Curated
Sequence conflicti248 – 2481D → G in AAB00183 (PubMed:7592499).Curated
Sequence conflicti344 – 3485NPSKN → TQVK in AAB00183 (PubMed:7592499).Curated
Sequence conflicti357 – 3626KMYLPP → NVPAS in AAB00183 (PubMed:7592499).Curated
Sequence conflicti409 – 4102SE → QQ in AAB00183 (PubMed:7592499).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36245 Genomic DNA. Translation: AAB00183.1.
D84432 Genomic DNA. Translation: BAA12569.1.
AL009126 Genomic DNA. Translation: CAB14365.2.
PIRiA69581.
RefSeqiNP_390314.2. NC_000964.3.
WP_003230253.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14365; CAB14365; BSU24340.
GeneIDi938588.
KEGGibsu:BSU24340.
PATRICi18976702. VBIBacSub10457_2541.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36245 Genomic DNA. Translation: AAB00183.1.
D84432 Genomic DNA. Translation: BAA12569.1.
AL009126 Genomic DNA. Translation: CAB14365.2.
PIRiA69581.
RefSeqiNP_390314.2. NC_000964.3.
WP_003230253.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliP49787.
SMRiP49787. Positions 3-448.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP49787. 1 interaction.
MINTiMINT-8365265.
STRINGi224308.Bsubs1_010100013351.

Proteomic databases

PaxDbiP49787.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14365; CAB14365; BSU24340.
GeneIDi938588.
KEGGibsu:BSU24340.
PATRICi18976702. VBIBacSub10457_2541.

Organism-specific databases

GenoListiBSU24340. [Micado]

Phylogenomic databases

eggNOGiCOG0439.
HOGENOMiHOG000008988.
InParanoidiP49787.
KOiK01961.
OMAiKDFYFME.
OrthoDBiEOG6CVV6Z.
PhylomeDBiP49787.

Enzyme and pathway databases

UniPathwayiUPA00655; UER00711.
BioCyciBSUB:BSU24340-MONOMER.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR004549. Acetyl_CoA_COase_biotin_COase.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR00514. accC. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genes encoding the biotin carboxyl carrier protein and biotin carboxylase subunits of Bacillus subtilis acetyl coenzyme A carboxylase, the first enzyme of fatty acid synthesis."
    Marini P.E., Li S.J., Gardiol D., Cronan J.E. Jr., de Mendoza D.
    J. Bacteriol. 177:7003-7006(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
    Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
    Microbiology 142:3103-3111(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / JH642.
  3. "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.
  4. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 107 AND 193.

Entry informationi

Entry nameiACCC1_BACSU
AccessioniPrimary (citable) accession number: P49787
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 7, 2009
Last modified: June 24, 2015
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Leu-235 is present instead of the conserved His which is expected to bind ATP.Curated

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.