ID C1B458_RHOOB Unreviewed; 502 AA.
AC C1B458;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Putative acetyl-CoA carboxylase beta chain {ECO:0000313|EMBL:BAH50906.1};
DE EC=6.4.1.2 {ECO:0000313|EMBL:BAH50906.1};
GN Name=accD {ECO:0000313|EMBL:BAH50906.1};
GN OrderedLocusNames=ROP_26590 {ECO:0000313|EMBL:BAH50906.1};
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH50906.1, ECO:0000313|Proteomes:UP000002212};
RN [1] {ECO:0000313|EMBL:BAH50906.1, ECO:0000313|Proteomes:UP000002212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:BAH50906.1,
RC ECO:0000313|Proteomes:UP000002212};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC {ECO:0000256|ARBA:ARBA00006102}.
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DR EMBL; AP011115; BAH50906.1; -; Genomic_DNA.
DR RefSeq; WP_012689862.1; NC_012522.1.
DR AlphaFoldDB; C1B458; -.
DR STRING; 632772.ROP_26590; -.
DR KEGG; rop:ROP_26590; -.
DR PATRIC; fig|632772.20.peg.2780; -.
DR HOGENOM; CLU_015486_2_1_11; -.
DR OrthoDB; 9772975at2; -.
DR Proteomes; UP000002212; Chromosome.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR PANTHER; PTHR42995; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR PANTHER; PTHR42995:SF5; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR PRINTS; PR01070; ACCCTRFRASEB.
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 Ligase {ECO:0000313|EMBL:BAH50906.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..236
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 235..486
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 502 AA; 53129 MW; 5912F7F69D87095F CRC64;
MARLTAPELL DLVVDAGTWE SWDTAPIPVA ADSEYADELL RAQEKTGLDE AVLTGLATIR
GRRTAILVCE FGFLGGSIGV AAGERLVAAI RRATHERLPL LALPTSGGTR MQEGTTAFLQ
MVKITAAVIK HKEAHLPYLV YLRSPTTGGV FASWGSLGHV TIAEPGALVG FLGPRVYEAL
YDAPFPSGVQ TAENLHAHGL IDAVRPPDQL AEIVDRALRI ITSSRGGRPA PAEPAVRESL
RDVPAWESVL ASRREDRPGV RDVMFHSASD VLPLNGTGQG EIDPGLILAL VRFGDMPCVL
LGQDRRGQTT RSPLGPAALR EARRGMRLAA ELNLPLVTVI DTAGAALSKE AEEGGLAGEI
ARCIADMVSL DVPTISLLLG QGTGGGALAL IPADRVLAAE HGWLSPLPPE GASAILHHDI
EHAPDMAARQ GIRSSDLLMS GIVDEVIPEF PDAAEESTAF CTRVGAVLHR ELALLDAADT
TQRLSERAAR FDRIGLLQPA PA
//
