ID A0A1L7D558_9CORY Unreviewed; 591 AA.
AC A0A1L7D558;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=CPHO_09795 {ECO:0000313|EMBL:APT93133.1};
OS Corynebacterium phocae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=161895 {ECO:0000313|EMBL:APT93133.1, ECO:0000313|Proteomes:UP000185491};
RN [1] {ECO:0000313|EMBL:APT93133.1, ECO:0000313|Proteomes:UP000185491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M408/89/1 {ECO:0000313|EMBL:APT93133.1,
RC ECO:0000313|Proteomes:UP000185491};
RA Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium phocae M408/89/1(T)(=DSM
RT 44612(T)), isolated from the common seal (Phoca vitulina).";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000256|ARBA:ARBA00024172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502;
CC Evidence={ECO:0000256|ARBA:ARBA00024172};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP009249; APT93133.1; -; Genomic_DNA.
DR RefSeq; WP_075735363.1; NZ_VXKJ01000046.1.
DR AlphaFoldDB; A0A1L7D558; -.
DR STRING; 161895.CPHO_09795; -.
DR KEGG; cpho:CPHO_09795; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000185491; 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 CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000185491}.
FT DOMAIN 7..451
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 126..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 515..591
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 591 AA; 63749 MW; 91C9D3A4EF07EE3A CRC64;
MSVETKTITK VLIANRGEIA VRVIRAARDA GIASVAVYAE PDATAQFVEL ADEAFALGGS
TSADSYLDMT KVLDAAKKSG ADAIHPGYGF LSENAEFAQA VMDAGLIWIG PSPQAIRDLG
DKVTARHIAE RADAPMAPGT PNPVADATEV EAFADEYGLP IAIKAAFGGG GRGMKVAYKR
EEVAELFESA TREATTAFGR GECFVERYLD KARHVEAQVL ADQHGNVVVM GTRDCSLQRR
FQKLVEEAPA PFLTDEQRRS IHDSAKRICR EAGYYGAGTV EYLVGSDGLI SFLEVNTRLQ
VEHPVTEETT GYDLVREQFR IAEGRELSIS EDPTPFGHAI EFRINGEDAQ AGFMPAPGTV
VKYSEPSGPG IRMDSGVREG SVIGGQFDSM LAKLIVWGPD RQTAIERSRR ALDEFTVEGL
PTVIPFDKAI VNNPAFTAED GSFDIYTKWI EEEWVNDLEP YVDSDAADAE DSEPARKFVV
EIDNRRVEVA LPSNLLMGGI NAVRKKAKKR RGGGGGKSAV SGDAVVAPMQ GTVIKVNVEE
GQEVAEGDVV VVLEAMKMEN PVKAHKSGKV TDLKVETGGQ INKGEPILEI K
//
