ID C0ZVA0_RHOE4 Unreviewed; 503 AA.
AC C0ZVA0;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Putative acetyl-CoA carboxylase beta chain {ECO:0000313|EMBL:BAH36594.1};
DE EC=6.4.1.2 {ECO:0000313|EMBL:BAH36594.1};
GN Name=accD {ECO:0000313|EMBL:BAH36594.1};
GN OrderedLocusNames=RER_58860 {ECO:0000313|EMBL:BAH36594.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH36594.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
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-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH36594.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT strain PR4.";
RL Environ. Microbiol. 8:334-346(2006).
CC -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC {ECO:0000256|ARBA:ARBA00006102}.
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DR EMBL; AP008957; BAH36594.1; -; Genomic_DNA.
DR RefSeq; WP_020909751.1; NC_012490.1.
DR AlphaFoldDB; C0ZVA0; -.
DR GeneID; 57484229; -.
DR KEGG; rer:RER_58860; -.
DR PATRIC; fig|234621.6.peg.6475; -.
DR eggNOG; COG0777; Bacteria.
DR eggNOG; COG0825; Bacteria.
DR HOGENOM; CLU_015486_2_1_11; -.
DR Proteomes; UP000002204; 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:BAH36594.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..236
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 216..477
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 503 AA; 53454 MW; 747F937E8F7830C6 CRC64;
MNRLTARDLL DLVIDAGTWE SWDTPPIPVA TDSDYAEALL RAQEKTGLDE SVLTGSASVR
GRRVAIIVCE FGFLGGSIGV AAGERLVVAI RRATQEQLPL LALPTSGGTR MQEGTTAFLQ
MVKITAALIK HKEAHLPYIV YLRNPTTGGV FASWGSLGHV TIAEPGALVG FLGPRVFEAL
YNSPFPVGVQ TAENLHEHGL IDAVRPPDQL AEIVDRALRI ITSRRRGYSL PSDPCSYDCP
PDTSAWESVV ASRREDRPGI REVLLNSASD MLPLNGTGQG ENDPGIMLAL VRFGDMPCVL
LGQDRRGQTA HSPLGPGALR EARRGMRLAA ELDLPLVTII DTAGAALSKE AEEGGLAGEI
ARCIADMISL EVPTISLLLG QGTGGGALAL IPADRVLAAR HGWLSPLPPE GASAIMFHDI
THAPEMAAGQ GIRSFDLLTG GIVDRVIPEF PDAADESAAF CTRVGAVLHY ELSVLSATDA
TERLITRTER IDRIGLVEAS TAV
//