ID E8QH09_HELP7 Unreviewed; 156 AA.
AC E8QH09;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562, ECO:0000256|RuleBase:RU364072};
GN OrderedLocusNames=HPIN_05345 {ECO:0000313|EMBL:ADU80271.1};
OS Helicobacter pylori (strain India7).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=907238 {ECO:0000313|EMBL:ADU80271.1, ECO:0000313|Proteomes:UP000009059};
RN [1] {ECO:0000313|Proteomes:UP000009059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=India7 {ECO:0000313|Proteomes:UP000009059};
RA Kersulyte D., Mukhopadhyay A., Choudhury A., Nair G.B., Berg D.E.;
RT "Genome sequence of Helicobacter pylori strain India7.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU364072}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|RuleBase:RU364072}.
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DR EMBL; CP002331; ADU80271.1; -; Genomic_DNA.
DR RefSeq; WP_001053826.1; NC_017372.1.
DR AlphaFoldDB; E8QH09; -.
DR KEGG; hpn:HPIN_05345; -.
DR PATRIC; fig|907238.3.peg.1066; -.
DR HOGENOM; CLU_016733_3_0_7; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000009059; 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; 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; PS50968; BIOTINYL_LIPOYL; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|RuleBase:RU364072};
KW Fatty acid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU364072};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW Lipid metabolism {ECO:0000256|RuleBase:RU364072}.
FT DOMAIN 78..154
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 156 AA; 17204 MW; 983B8F8D888026C2 CRC64;
MNLSEIEELI KEFKASDLGH LKLKHEHFEL VLDKESAYTK KNALNPAHSP APIMVEASMP
SVQTPVPMVC TPIVDKKEDF VLSPMVGTFY HAPSPGAEPY VKAGDTLKKG QIVGIVEAMK
IMNEIEVEYP CKVLSVEVGD AQPVEYGTKL IKVEKL
//
