ID F8KRQ3_HELBC Unreviewed; 453 AA.
AC F8KRQ3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Biotin carboxylase of acetyl-CoA carboxylase {ECO:0000313|EMBL:CCB79440.1};
DE EC=6.3.4.14 {ECO:0000313|EMBL:CCB79440.1};
GN OrderedLocusNames=HBZC1_04540 {ECO:0000313|EMBL:CCB79440.1};
OS Helicobacter bizzozeronii (strain CIII-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1002804 {ECO:0000313|EMBL:CCB79440.1, ECO:0000313|Proteomes:UP000008387};
RN [1] {ECO:0000313|EMBL:CCB79440.1, ECO:0000313|Proteomes:UP000008387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIII-1 {ECO:0000313|EMBL:CCB79440.1,
RC ECO:0000313|Proteomes:UP000008387};
RX PubMed=21705603; DOI=10.1128/JB.05439-11;
RA Schott T., Rossi M., Hanninen M.L.;
RT "Genome sequence of Helicobacter bizzozeronii strain CIII-1, an isolate
RT from human gastric mucosa.";
RL J. Bacteriol. 193:4565-4566(2011).
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DR EMBL; FR871757; CCB79440.1; -; Genomic_DNA.
DR RefSeq; WP_013889927.1; NC_015674.1.
DR AlphaFoldDB; F8KRQ3; -.
DR STRING; 1002804.HBZC1_04540; -.
DR KEGG; hbi:HBZC1_04540; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_000395_3_2_7; -.
DR Proteomes; UP000008387; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CCB79440.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000008387}.
FT DOMAIN 7..451
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 127..322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 453 AA; 49875 MW; B436E93A6B1D6F33 CRC64;
MGYKPQKIKK VLVANRGEIA VRIIQAAHEL NMKAVAIYTD ADQGNLASQL ADEAYRVGEN
LAHKSYLNID KVLEIAKQAQ VDAIHPGYGF LSENPKFAAR VEEAGIIFVG PSSALIEMMG
DKAKALQQAK KSQVPTMPNS PVLQNVDQAL QEASKIGYPL LIKAIAGGGG KGIRLVANEG
DLKTQFEIAT AEARAAFGNG GVYLEKYLQG AKHIEVQVLG DGQRVIHLYD RECSLQRRRQ
KVLEEAPSPS LDCQTREALC ASAARMAGDV GYKGAGTLEF LYDTQSKGFY FLEMNTRIQV
EHAITEMVTG IDLVRQMLRI ADGEALTYKQ EDISLRGHSI EVRINAEDPS NNFFPSPGEI
TKLQCPTGSG VRLDSMLFNG RIIPPFYDSL IAKLIVYDQN REFALSKLKR ALNELKIEGV
KTTIGLFKEL VENPHVQRGD YDINFLESYK LGG
//
