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Protein

Biotin carboxylase

Gene

accC

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: -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]-biotin-N6-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N6-L-lysine.
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

Keywordsi

Molecular functionLigase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Biotin, Nucleotide-binding

Enzyme and pathway databases

BioCyciHINF71421:G1GJ1-1013-MONOMER
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

Phylogenomic databases

eggNOGiENOG4105CER Bacteria
COG0439 LUCA
KOiK01961
OMAiFVEICSH
PhylomeDBiP43873

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
InterProiView protein in InterPro
IPR004549 Acetyl_CoA_COase_biotin_COase
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR005481 BC-like_N
IPR011764 Biotin_carboxylation_dom
IPR005482 Biotin_COase_C
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR016185 PreATP-grasp_dom_sf
IPR011054 Rudment_hybrid_motif
PfamiView protein in Pfam
PF02785 Biotin_carb_C, 1 hit
PF00289 Biotin_carb_N, 1 hit
PF02786 CPSase_L_D2, 1 hit
SMARTiView protein in SMART
SM00878 Biotin_carb_C, 1 hit
SUPFAMiSSF51246 SSF51246, 1 hit
SSF52440 SSF52440, 1 hit
TIGRFAMsiTIGR00514 accC, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS50979 BC, 1 hit
PS00866 CPSASE_1, 1 hit
PS00867 CPSASE_2, 1 hit

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
PATRICifig|71421.8.peg.1013

Similar proteinsi

Entry informationi

Entry nameiACCC_HAEIN
AccessioniPrimary (citable) accession number: P43873
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 25, 2018
This is version 129 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health