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Database: UniProt
Entry: A5UIB3_HAEIG
LinkDB: A5UIB3_HAEIG
Original site: A5UIB3_HAEIG 
ID   A5UIB3_HAEIG            Unreviewed;       155 AA.
AC   A5UIB3;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562, ECO:0000256|RuleBase:RU364072};
GN   OrderedLocusNames=CGSHiGG_08435 {ECO:0000313|EMBL:ABR00519.1};
OS   Haemophilus influenzae (strain PittGG).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374931 {ECO:0000313|EMBL:ABR00519.1, ECO:0000313|Proteomes:UP000001990};
RN   [1] {ECO:0000313|EMBL:ABR00519.1, ECO:0000313|Proteomes:UP000001990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittGG {ECO:0000313|EMBL:ABR00519.1,
RC   ECO:0000313|Proteomes:UP000001990};
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
CC   -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC       carboxylase complex; first, biotin carboxylase catalyzes the
CC       carboxylation of the carrier protein and then the transcarboxylase
CC       transfers the carboxyl group to form malonyl-CoA.
CC       {ECO:0000256|ARBA:ARBA00003761, ECO:0000256|RuleBase:RU364072}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194, ECO:0000256|RuleBase:RU364072}.
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DR   EMBL; CP000672; ABR00519.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5UIB3; -.
DR   KEGG; hiq:CGSHiGG_08435; -.
DR   HOGENOM; CLU_016733_3_1_6; -.
DR   OMA; IKSPIIG; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001990; Chromosome.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   InterPro; IPR001249; AcCoA_biotinCC.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR00531; BCCP; 1.
DR   PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   PRINTS; PR01071; ACOABIOTINCC.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE   4: Predicted;
KW   Biotin {ECO:0000256|ARBA:ARBA00023267, ECO:0000256|RuleBase:RU364072};
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU364072};
KW   Ligase {ECO:0000313|EMBL:ABR00519.1};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU364072}.
FT   DOMAIN          72..155
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   155 AA;  16245 MW;  3230BE0B7D4BC9BB CRC64;
     MDIRKIKKLI ELVEESGITE LEVQEEEGTV RISRAAPVIA PAAVQYAAAP VVAPTPTAAP
     AQAPAAATPA PAASDELSGH LVRSPMVGTF YRSPSPEAKA FVEVGQSVKV GDALCIVEAM
     KMMNRIEADK AGVVKAILIN DGNAVEFDEP LIVIE
//
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