Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P49787 (ACCC1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. 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:
Biotin carboxylase 1

EC=6.3.4.14
Alternative name(s):
Acetyl-CoA carboxylase subunit A 1
Short name=ACC 1
EC=6.4.1.2
Gene names
Name:accC1
Synonyms:accC, yqhX
Ordered Locus Names:BSU24340
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.

Pathway

Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.

Subunit structure

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.

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Biotin carboxylase 1
PRO_0000146789

Regions

Domain1 – 447447Biotin carboxylation
Domain120 – 318199ATP-grasp

Sites

Active site2931 By similarity
Binding site1161ATP By similarity
Binding site2001ATP By similarity

Experimental info

Sequence conflict1071A → P in BAA12569. Ref.2
Sequence conflict1931G → R in BAA12569. Ref.2
Sequence conflict2401E → G in AAB00183. Ref.1
Sequence conflict2481D → G in AAB00183. Ref.1
Sequence conflict344 – 3485NPSKN → TQVK in AAB00183. Ref.1
Sequence conflict357 – 3626KMYLPP → NVPAS in AAB00183. Ref.1
Sequence conflict409 – 4102SE → QQ in AAB00183. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49787 [UniParc].

Last modified July 7, 2009. Version 3.
Checksum: 2F93B3E793478334

FASTA45049,452
        10         20         30         40         50         60 
MIKKLLIANR GEIAVRIIRA CRELGIETVA VYSEADKDAL HVQMADEAFC IGPKASKDSY 

        70         80         90        100        110        120 
LNVTNIVSVA KLTGTDAIHP GYGFLAENAD FAELCEEVNV TFVGPSADAI SKMGTKDVAR 

       130        140        150        160        170        180 
ETMKQAGVPI VPGSQGIIEN VEEAVSLANE IGYPVIIKAT AGGGGKGIRV ARTEEELING 

       190        200        210        220        230        240 
IKITQQEAAT AFGNPGVYIE KYIEDFRHVE IQVLADNYGN TIHLGERDCS IQRRLQKLLE 

       250        260        270        280        290        300 
ESPSPALDSE IREQMGDAAV KAAKAVGYTG AGTVEFIYDY NEQRYYFMEM NTRIQVEHPV 

       310        320        330        340        350        360 
TEMVTGTDLI KEQIKVASGM ELSLKQEDVE FEGWAIECRI NAENPSKNFM PSPGEIKMYL 

       370        380        390        400        410        420 
PPGGLGVRVD SAAYPGYSIP PYYDSMIAKV ITYGKTRDEA IARMKRALSE FVIEGIETTI 

       430        440        450 
PFHLKLLEHE TFVSGEFNTK FLETYDVMGS 

« Hide

References

« Hide 'large scale' references
[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. 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.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U36245 Genomic DNA. Translation: AAB00183.1.
D84432 Genomic DNA. Translation: BAA12569.1.
AL009126 Genomic DNA. Translation: CAB14365.2.
PIRA69581.
RefSeqNP_390314.2. NC_000964.3.

3D structure databases

ProteinModelPortalP49787.
SMRP49787. Positions 3-448.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP49787. 1 interaction.
MINTMINT-8365265.
STRING224308.BSU24340.

Proteomic databases

PaxDbP49787.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14365; CAB14365; BSU24340.
GeneID938588.
KEGGbsu:BSU24340.
PATRIC18976702. VBIBacSub10457_2541.

Organism-specific databases

GenoListBSU24340. [Micado]

Phylogenomic databases

eggNOGCOG0439.
HOGENOMHOG000008988.
KOK01961.
OrthoDBEOG6CVV6Z.
PhylomeDBP49787.

Enzyme and pathway databases

BioCycBSUB:BSU24340-MONOMER.
UniPathwayUPA00655; UER00711.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProIPR004549. 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]
PfamPF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR00514. accC. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACCC1_BACSU
AccessionPrimary (citable) accession number: P49787
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 7, 2009
Last modified: July 9, 2014
This is version 120 of the entry and version 3 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