ID R7WQC1_9NOCA Unreviewed; 536 AA.
AC R7WQC1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Fatty acid CoA carboxylase B subunit {ECO:0000313|EMBL:EOM77517.1};
GN ORFNames=Rrhod_1194 {ECO:0000313|EMBL:EOM77517.1};
OS Rhodococcus rhodnii LMG 5362.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM77517.1, ECO:0000313|Proteomes:UP000013525};
RN [1] {ECO:0000313|EMBL:EOM77517.1, ECO:0000313|Proteomes:UP000013525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM77517.1,
RC ECO:0000313|Proteomes:UP000013525};
RX PubMed=23788540;
RA Pachebat J.A., van Keulen G., Whitten M.M., Girdwood S., Del Sol R.,
RA Dyson P.J., Facey P.D.;
RT "Draft Genome Sequence of Rhodococcus rhodnii Strain LMG5362, a Symbiont of
RT Rhodnius prolixus (Hemiptera, Reduviidae, Triatominae), the Principle
RT Vector of Trypanosoma cruzi.";
RL Genome Announc. 1:e00329-13(2013).
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:EOM77517.1}.
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; APMY01000039; EOM77517.1; -; Genomic_DNA.
DR RefSeq; WP_010837260.1; NZ_APMY01000039.1.
DR AlphaFoldDB; R7WQC1; -.
DR STRING; 38312.GCA_000720375_00935; -.
DR PATRIC; fig|1273125.3.peg.1156; -.
DR eggNOG; COG4799; Bacteria.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000013525; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000013525}.
FT DOMAIN 23..279
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 283..528
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 57416 MW; DED32488BF5AB82D CRC64;
MTSDVQSGID GENRHTETPR DAHVSLVAKL RTALAAAALG GSERSRERHV ARGKLLPRER
VDALLDPGSP FLEIAPLAAH GMYDDESPGA GIITGIGRVE GRECVVVAND ATVKGGTYYP
MTVKKHLRAQ EIALQNRLPC IYLVDSGGAF LPRQDEVFPD RDHFGRIFYN QATMSAQGIA
QIAAVMGSCT AGGAYVPAMS DEAVIVRGQG TIFLGGPPLV KAATGEVVTA EELGGGELHS
RISGVTDHLA DDDLDALRIV REIVRTLGPR EPVPWRTEPA LAALGDPHEL YDVVPVDSRT
PFDVHEVIDR IVDGGRFQEF KAEYGRTLVT GFAHIDGHPV GIVANNGVLF GESAVKGAHF
IELCDRRSTP LVFLQNITGF MVGRDYEAGG IAKHGAKMVT AVACARVPKL TVVIGGSHGA
GNYSMCGRAY SPRFLWMWSN ARISVMGGEQ AAKVLSTVRG DQRAAAGEPW SEADAEAVEA
PVREQYERQG NPYYSTARLW DDGIIDPAET RTVLGLALAA CANAPLEPVS YGVFRM
//
