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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//