ID U3GVX9_9CORY Unreviewed; 593 AA.
AC U3GVX9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=CARG_07740 {ECO:0000313|EMBL:AGU15665.1};
OS Corynebacterium argentoratense DSM 44202.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1348662 {ECO:0000313|EMBL:AGU15665.1, ECO:0000313|Proteomes:UP000016943};
RN [1] {ECO:0000313|EMBL:AGU15665.1, ECO:0000313|Proteomes:UP000016943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44202 {ECO:0000313|EMBL:AGU15665.1};
RX PubMed=24092787;
RA Bomholt C., Glaub A., Gravermann K., Albersmeier A., Brinkrolf K.,
RA Ruckert C., Tauch A.;
RT "Whole-Genome Sequence of the Clinical Strain Corynebacterium
RT argentoratense DSM 44202, Isolated from a Human Throat Specimen.";
RL Genome Announc. 1:e00793-13(2013).
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; CP006365; AGU15665.1; -; Genomic_DNA.
DR RefSeq; WP_021012055.1; NC_022198.1.
DR AlphaFoldDB; U3GVX9; -.
DR STRING; 1348662.CARG_07740; -.
DR GeneID; 78250297; -.
DR KEGG; caz:CARG_07740; -.
DR PATRIC; fig|1348662.3.peg.1529; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_11; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000016943; 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:UP000016943}.
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 517..593
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 593 AA; 63540 MW; D9E8821A21C5D686 CRC64;
MSVETKKITK VLVANRGEIA IRVIRAARDA GIASVAVYAE PDADAPFVSM ADEAFALGGQ
NSAESYLVFD KILDAAKKSG ADAIHPGYGF LSENGDFAQA VIDAGLIWIG PSPQSIRDLG
DKVTARHIAM RANAPMAPGS KEPVKDAAEV RAFAEEHGLP IAIKAAFGGG GRGMKVAYEM
DEVEDLYESA TREAVAAFGR GECFVERYLD KARHVECQVV ADMHGNVVVA GTRDCSLQRR
FQKLVEEAPA PFLTDEQRTR LHESAKAICK EAGYYGAGTV EYLVGSDGLI SFLEVNTRLQ
VEHPVTEVTT GLDLVREQFR IAEGRELHIK EDPTPRGHAF EFRINGEDAG SNFMPAPGKI
TKYIEPAGPG VRMDSGIVEG SVIGGQFDSM LAKLIVFGES REEALQRARR ALSEYVIEGM
PTVLPFHAHI VENPAFVGDG EKFDVYTKWI EEEWDNPIPA YVDPADVEEE EEATPKQKVV
VEIDGRRVEI ALPGDLALAG GGASGAKKKA KKRRAGGGKK AVSGDAVAAP MQGTVIKVNV
EEGQEVNEGD TVVVLEAMKM ENPVKAHKSG VVTGLSAAAG EGVTKGAVLM EIK
//
