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Protein

Biotin carboxylase

Gene

accC

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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. Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (accD), Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA), Biotin carboxylase (accC)
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 sitei201 – 2011ATPBy similarity
Binding sitei236 – 2361ATPBy similarity
Active sitei292 – 2921Sequence Analysis

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

UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin carboxylase (EC:6.3.4.14)
Alternative name(s):
Acetyl-CoA carboxylase subunit A (EC:6.4.1.2)
Short name:
ACC
Gene namesi
Name:accC
Ordered Locus Names:HI_0972
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000000579 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Biotin carboxylasePRO_0000146793Add
BLAST

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

STRINGi71421.HI0972.

Structurei

Secondary structure

1
448
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Helixi11 – 2414Combined sources
Beta strandi27 – 337Combined sources
Helixi34 – 363Combined sources
Helixi40 – 445Combined sources
Beta strandi45 – 5511Combined sources
Helixi56 – 583Combined sources
Turni59 – 613Combined sources
Helixi63 – 7311Combined sources
Beta strandi76 – 794Combined sources
Turni84 – 874Combined sources
Helixi89 – 979Combined sources
Beta strandi101 – 1044Combined sources
Helixi107 – 1148Combined sources
Helixi116 – 12611Combined sources
Helixi142 – 15211Combined sources
Beta strandi154 – 1607Combined sources
Beta strandi169 – 1724Combined sources
Helixi175 – 19218Combined sources
Beta strandi198 – 2025Combined sources
Beta strandi208 – 2169Combined sources
Beta strandi222 – 23413Combined sources
Beta strandi237 – 2448Combined sources
Helixi250 – 26718Combined sources
Beta strandi271 – 28010Combined sources
Beta strandi283 – 2908Combined sources
Helixi297 – 3048Combined sources
Helixi308 – 3169Combined sources
Helixi325 – 3273Combined sources
Beta strandi332 – 34211Combined sources
Turni344 – 3463Combined sources
Beta strandi356 – 3583Combined sources
Beta strandi365 – 3684Combined sources
Beta strandi379 – 3813Combined sources
Beta strandi384 – 39411Combined sources
Helixi395 – 40814Combined sources
Beta strandi410 – 4145Combined sources
Helixi418 – 4258Combined sources
Helixi428 – 4325Combined sources
Helixi439 – 4446Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MV1X-ray1.91A1-448[»]
4MV3X-ray1.69A1-448[»]
4MV4X-ray1.61A1-448[»]
4MV6X-ray1.77A1-448[»]
4MV7X-ray1.73A1-448[»]
4MV8X-ray2.06A1-448[»]
4MV9X-ray1.98A1-448[»]
ProteinModelPortaliP43873.
SMRiP43873. Positions 1-446.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 445445Biotin carboxylationAdd
BLAST
Domaini120 – 317198ATP-graspPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0439.
KOiK01961.
OMAiERCANAC.
OrthoDBiEOG6CVV6Z.
PhylomeDBiP43873.

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.

P43873-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEKVVIANR GEIALRILRA CKELGIKTVA VHSTADRDLK HVLLADETIC
60 70 80 90 100
IGPAPSAKSY LNIPAIIAAA EVTGADAIHP GYGFLSENAD FAEQVERSGF
110 120 130 140 150
TFIGPTADVI RLMGDKVSAI KAMKKAGVPC VPGSDGPVSN DIAKNKEIAK
160 170 180 190 200
RIGYPIIIKA SGGGGGRGMR VVRSEDALEE SIAMTKAEAK AAFNNDMVYM
210 220 230 240 250
EKYLENPRHV EIQVLADTHG NAVYLAERDC SMQRRHQKVV EEAPAPGITE
260 270 280 290 300
EVRRDIGSRC ANACVEIGYR GAGTFEFLYE NGEFYFIEMN TRIQVEHPVT
310 320 330 340 350
EMITGVDLVK EQLRIAAGLP ISFKQEDIKV KGHAMECRIN AEDPKTFLPS
360 370 380 390 400
PGKVNHLHSP GGLGVRWDSH VYGGYTVPPH YDSMIAKLIT YGDTREVAIR
410 420 430 440
RMQNALSETI IDGIKTNIPL HELILEDENF QKGGTNIHYL EKKLGMNE
Length:448
Mass (Da):49,108
Last modified:November 1, 1995 - v1
Checksum:i2B497E2A31ED96D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22632.1.
PIRiF64105.
RefSeqiNP_439133.1. NC_000907.1.
WP_005655956.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC22632; AAC22632; HI_0972.
GeneIDi949398.
KEGGihin:HI0972.
PATRICi20190601. VBIHaeInf48452_1013.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22632.1.
PIRiF64105.
RefSeqiNP_439133.1. NC_000907.1.
WP_005655956.1. NC_000907.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MV1X-ray1.91A1-448[»]
4MV3X-ray1.69A1-448[»]
4MV4X-ray1.61A1-448[»]
4MV6X-ray1.77A1-448[»]
4MV7X-ray1.73A1-448[»]
4MV8X-ray2.06A1-448[»]
4MV9X-ray1.98A1-448[»]
ProteinModelPortaliP43873.
SMRiP43873. Positions 1-446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi71421.HI0972.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC22632; AAC22632; HI_0972.
GeneIDi949398.
KEGGihin:HI0972.
PATRICi20190601. VBIHaeInf48452_1013.

Phylogenomic databases

eggNOGiCOG0439.
KOiK01961.
OMAiERCANAC.
OrthoDBiEOG6CVV6Z.
PhylomeDBiP43873.

Enzyme and pathway databases

UniPathwayiUPA00655; UER00711.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Entry informationi

Entry nameiACCC_HAEIN
AccessioniPrimary (citable) accession number: P43873
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 27, 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.