ID A0A1X0JMY8_9MYCO Unreviewed; 644 AA.
AC A0A1X0JMY8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Acetyl/propionyl-CoA carboxylase subuit alpha {ECO:0000313|EMBL:ORB64172.1};
GN ORFNames=BST47_16385 {ECO:0000313|EMBL:ORB64172.1};
OS Mycolicibacterium tusciae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=75922 {ECO:0000313|EMBL:ORB64172.1, ECO:0000313|Proteomes:UP000192411};
RN [1] {ECO:0000313|EMBL:ORB64172.1, ECO:0000313|Proteomes:UP000192411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44153 {ECO:0000313|Proteomes:UP000192411};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (FEB-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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORB64172.1}.
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DR EMBL; MVIM01000008; ORB64172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0JMY8; -.
DR STRING; 75922.BST47_16385; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000192411; Unassembled WGS sequence.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
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:SF126; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 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}.
FT DOMAIN 1..436
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 94..311
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 561..642
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 644 AA; 67781 MW; B52B1C20880D85D2 CRC64;
MITRVLVANR GEIARRVFDT CRKLGIGTVA VYTDPDAASP HVAEADARVR LEGTKGYLDA
AQLIAAAQAA GADAIHPGYG FLSENAEFAA AVIDAGLTWI GPPVAAVAAM GSKIEAKKML
AAAGVPVLEE LDPDTVTADQ LPVLIKASAG GGGRGMRIVD ELSSLPDQVE AARREAQSAF
GDPTVFCERY LATGHHVEVQ VMADQHGTVW AVGERECSIQ RRHQKIIEEA PSPLVERTEG
MRAKLFDAAR LAAEAIGYAG AGTVEFMAGP DGPGAGDFYF LEMNTRLQVE HPVTEATTGL
DLVELQLHVA DGGQLDPEPP PSRGSSIEAR LYAEDPAKNW QPQAGTVHRF EVPQTVRVDT
GIQDGSEVSI FYDPMLAKVI SYAPTRRQAA AVLADALTRT RLHGIRTNRD LLVNVLRHPA
FLDGATDTAF FDTHGLDRLS TPLGDDRAAA LSAVAAALAD AAQNRDSATV FAAAPSGWRN
LASGFQTKSY GDASGGEHVV RYRCTRDSVH LPDLDGVGLV SSAADRVVLS IAGVERAFDV
ARYGADVYVD SSLGPVHLVA LPRFGDPDTA VAQGSLLAPM PGSVLRIGAA VGDSVAAGQP
LVWLEAMKME HTVTSPGDGV LAELNVEVGQ QVDVGAVLAR VDNP
//
