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Database: UniProt
Entry: A0A1A2GGX1_9MYCO
LinkDB: A0A1A2GGX1_9MYCO
Original site: A0A1A2GGX1_9MYCO 
ID   A0A1A2GGX1_9MYCO        Unreviewed;       523 AA.
AC   A0A1A2GGX1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Methylcrotonoyl-CoA carboxylase {ECO:0000313|EMBL:OBG28359.1};
GN   ORFNames=A5764_25570 {ECO:0000313|EMBL:OBG28359.1};
OS   Mycobacterium sp. 852002-51057_SCH5723018.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834094 {ECO:0000313|EMBL:OBG28359.1, ECO:0000313|Proteomes:UP000092171};
RN   [1] {ECO:0000313|Proteomes:UP000092171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=852002-51057_SCH5723018 {ECO:0000313|Proteomes:UP000092171};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Mehaffy C., Tameris M.,
RA   Hatherill M., Hanekom W., Mahomed H., Mcshane H.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC       {ECO:0000256|ARBA:ARBA00006102}.
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:OBG28359.1}.
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DR   EMBL; LZIR01000027; OBG28359.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A2GGX1; -.
DR   STRING; 1834094.A5764_25570; -.
DR   Proteomes; UP000092171; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR045190; MCCB/AccD1-like.
DR   PANTHER; PTHR22855; ACETYL, PROPIONYL, PYRUVATE, AND GLUTACONYL CARBOXYLASE-RELATED; 1.
DR   PANTHER; PTHR22855:SF13; METHYLCROTONOYL-COA CARBOXYLASE BETA CHAIN, MITOCHONDRIAL; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   3: Inferred from homology;
FT   DOMAIN          10..266
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          272..515
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   523 AA;  56579 MW;  5AF576601C0FA6DF CRC64;
     MTAPSFADEH RRLVRELNAK LAAAALGGSE RARERHVSRG KLLPRERVDR LLDPGSPFLE
     LSPLAANGMY DDESPGAGVI TGIGRVSERE CVIVVNDATV KGGTYYPMTV KKHLRAQEVA
     LQNRLPCIYL VDSGGAFLPR QDEVFPDREH FGRIFYNQAT MSAKGIPQVA AVLGSCTAGG
     AYVPAMSDEA VIVREQGTIF LGGPPLVKAA TGEIVSAEEL GGGDLHSRVS GVTDHLAEDD
     EHALRIVRSI VATFGPREPG QWEVRRSVEP KHAQTELYDV VPPDPRVPYD VHEVIVRLVD
     GSEFGEFKAN YGKTLVTAFA RIHGHPVGII ANNGVLFSES ALKGAHFIEL CDKRNIPLLF
     LQNIAGFMVG RDYEAGGIAK HGAKMVTAVA CARVPKLTVV IGGSYGAGNY SMCGRAYSPR
     FLWMWPNARI SVMGGEQAAS VLATVRGEQL ATAGKPWSAD EEEAFKAPIR EQYEDQGNPY
     YSTARLWDDG IIDPADTRTC VGLALSACVH APLEPVSYGV FRM
//
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