ID A0A2Z3YR81_9CORY Unreviewed; 605 AA.
AC A0A2Z3YR81;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN Name=accA1_1 {ECO:0000313|EMBL:AWT25560.1};
GN ORFNames=Csp1_07510 {ECO:0000313|EMBL:AWT25560.1};
OS Corynebacterium provencense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1737425 {ECO:0000313|EMBL:AWT25560.1, ECO:0000313|Proteomes:UP000247696};
RN [1] {ECO:0000313|Proteomes:UP000247696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17KM38 {ECO:0000313|Proteomes:UP000247696};
RA Kittl S., Brodard I., Rychener L., Jores J., Roosje P., Gobeli Brawand S.;
RT "Otitis media/interna in a cat caused by the recently described species
RT Corynebacterium provencense.";
RL Submitted (NOV-2017) 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; CP024988; AWT25560.1; -; Genomic_DNA.
DR RefSeq; WP_066583741.1; NZ_CP024988.1.
DR AlphaFoldDB; A0A2Z3YR81; -.
DR STRING; 1737425.GCA_900049755_00542; -.
DR KEGG; cpre:Csp1_07510; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000247696; 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:UP000247696}.
FT DOMAIN 11..455
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 130..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 529..605
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 517..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 65087 MW; 91BE2B6D836AFE70 CRC64;
MPAEHRNDPR KIRKVLVANR GEIAVRVIRA ARDEGISSVA VYAVPDADAP FVRLADEAFA
LGGQTSAESY LDIVKIVDAA VRSGADAVHP GYGFLSENAD FARAVIDAGL TWIGPSPRTI
GELGDKVTAR RYAEQVSAPM APGTPEPVTD AQEIIDFATE YGLPVAVKAS FGGGGRGMKV
ARTLEEIPAL FESATREAEK AFGRGECFVE RYLDRARHVE CQVVADTHGN VVVASTRDCT
LQRRFQKLIE EAPAPFLTPE QDARLREASR AVMRAADYTG VGTVEYLVGD DGLISFLEVN
TRLQVEHPVT EQVTGWDLVR EQFRIAEGRE LSRTTDPEIR GHAFEFRING EDAASGFMPS
PGTLTTYREP AGPGVRVDSG VEQGSVIGDQ FDSMLAKLIV TGEDRAHALR RAARALDEYT
VEGIPTVLPF HRAVVRDPAF APELAGDSAA DAAADPLTVD HFDVYTRWIE EEWRNTVEPD
ESPAADGDVP SRRTIPVEVD GRRVEVSVPG DLFATGAPVR RPARRSAGGS AASASGDDVL
APMQGTVVSV LVEEGQEVTE GEPVLLLEAM KMENAVRAHK NGTVSGLSVS AGDGVKKSQL
MLQLL
//
