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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.

Pathwayi: 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)DescriptionActionsGraphical viewLength
Binding sitei116ATPBy similarity1
Binding sitei201ATPBy similarity1
Binding sitei236ATPBy similarity1
Active sitei292Sequence analysis1

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
Proteomesi
  • UP000000579 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001467931 – 448Biotin carboxylaseAdd BLAST448

Proteomic databases

PRIDEiP43873.

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

1448
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Helixi11 – 24Combined sources14
Beta strandi27 – 33Combined sources7
Helixi34 – 36Combined sources3
Helixi40 – 44Combined sources5
Beta strandi45 – 55Combined sources11
Helixi56 – 58Combined sources3
Turni59 – 61Combined sources3
Helixi63 – 73Combined sources11
Beta strandi76 – 79Combined sources4
Turni84 – 87Combined sources4
Helixi89 – 97Combined sources9
Beta strandi101 – 104Combined sources4
Helixi107 – 114Combined sources8
Helixi116 – 126Combined sources11
Helixi142 – 152Combined sources11
Beta strandi154 – 160Combined sources7
Beta strandi169 – 172Combined sources4
Helixi175 – 192Combined sources18
Beta strandi198 – 202Combined sources5
Beta strandi208 – 216Combined sources9
Beta strandi222 – 234Combined sources13
Beta strandi237 – 244Combined sources8
Helixi250 – 267Combined sources18
Beta strandi271 – 280Combined sources10
Beta strandi283 – 290Combined sources8
Helixi297 – 304Combined sources8
Helixi308 – 316Combined sources9
Helixi325 – 327Combined sources3
Beta strandi332 – 342Combined sources11
Turni344 – 346Combined sources3
Beta strandi356 – 358Combined sources3
Beta strandi365 – 368Combined sources4
Beta strandi379 – 381Combined sources3
Beta strandi384 – 394Combined sources11
Helixi395 – 408Combined sources14
Beta strandi410 – 414Combined sources5
Helixi418 – 425Combined sources8
Helixi428 – 432Combined sources5
Helixi439 – 444Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4RZQX-ray1.98A1-448[»]
ProteinModelPortaliP43873.
SMRiP43873.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 445Biotin carboxylationAdd BLAST445
Domaini120 – 317ATP-graspPROSITE-ProRule annotationAdd BLAST198

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CER. Bacteria.
COG0439. LUCA.
KOiK01961.
OMAiKGHAVEC.
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.
IPR005481. BC-like_N.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. Biotin_carb_N. 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
PDB 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[»]
4RZQX-ray1.98A1-448[»]
ProteinModelPortaliP43873.
SMRiP43873.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi71421.HI0972.

Proteomic databases

PRIDEiP43873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105CER. Bacteria.
COG0439. LUCA.
KOiK01961.
OMAiKGHAVEC.
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.
IPR005481. BC-like_N.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. Biotin_carb_N. 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...

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: November 2, 2016
This is version 121 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

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 one 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.