ID A0A0D5A9Z8_9NOCA Unreviewed; 546 AA.
AC A0A0D5A9Z8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Methylcrotonyl-CoA carboxylase carboxyl transferase subunit {ECO:0000313|EMBL:AJW39730.1};
GN ORFNames=NY08_1700 {ECO:0000313|EMBL:AJW39730.1};
OS Rhodococcus sp. B7740.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1564114 {ECO:0000313|EMBL:AJW39730.1, ECO:0000313|Proteomes:UP000032410};
RN [1] {ECO:0000313|EMBL:AJW39730.1, ECO:0000313|Proteomes:UP000032410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7740 {ECO:0000313|EMBL:AJW39730.1};
RX PubMed=25931596;
RA Zhang D., Li L., Zhu S., Zhang N., Yang J., Ma X., Chen J.;
RT "Complete Genome Sequence of Rhodococcus sp. B7740, a Carotenoid-Producing
RT Bacterium Isolated from the Arctic Sea.";
RL Genome Announc. 3:0-0(2015).
CC -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC {ECO:0000256|ARBA:ARBA00006102}.
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DR EMBL; CP010797; AJW39730.1; -; Genomic_DNA.
DR RefSeq; WP_032397648.1; NZ_CP010797.1.
DR AlphaFoldDB; A0A0D5A9Z8; -.
DR STRING; 1564114.NY08_1700; -.
DR KEGG; rhb:NY08_1700; -.
DR PATRIC; fig|1564114.4.peg.1668; -.
DR HOGENOM; CLU_018822_6_2_11; -.
DR Proteomes; UP000032410; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 PANTHER; PTHR43842:SF2; BIOTIN-DEPENDENT ACETYL-_PROPIONYL-COENZYME A CARBOXYLASE BETA5 SUBUNIT; 1.
DR PANTHER; PTHR43842; PROPIONYL-COA CARBOXYLASE BETA CHAIN; 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;
KW Transferase {ECO:0000313|EMBL:AJW39730.1}.
FT DOMAIN 21..277
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 292..540
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 58392 MW; 296C9AA888DDCFB6 CRC64;
MTSVQDSTAH GSAEAPDIHT TAGKLADLRK RLAVAEIPSG EAAVDKVHAK GKLTARERIT
ALLDEGSFVE LDALARHRSQ NFGLGENRPF GDGVVTGYGT VDGRDVCVFS QDATVFGGSL
GEIYGEKIVK VMDLAVKTGR PLVGINEGAG ARIQEGVVSL GLYGEIFHRN VRASGVIPQI
SVIMGPAAGG HVYSPALTDF VVMVDGTSQM FVTGPDVIKT VTGENVTMEE LGGAHTHMEK
SGVAHYVASG EQDALDYVRD LLSYLPSNNR ADAPRTAPSD PVVGSIEDSL TAEDLELDTL
IPDSPNTPYD MHEVIRRILD DDEFLEVQEG RARNIIVGFG RIDGRSVGIV ANQPTQFAGT
LDIDASEKAA RFVRTCDCFN VPIITLVDVP GFLPGTGQEY NGIIRRGAKL LYAYGEATVG
KITVITRKAY GGAYDVMGSK HMGADVNLAW PTAQIAVMGA SGAVGFVYRK QLLEAAKNGD
DVDALRLTLQ QEYEDTLVNP YIAAERGYLD AVIPPSHTRG QIVTALRLLE RKQVTLPPKK
HGNIPL
//
