ID K8XXZ5_RHOOP Unreviewed; 502 AA.
AC K8XXZ5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Acetyl-CoA carboxylase carboxyl transferase subunit {ECO:0000313|EMBL:EKT82055.1};
GN ORFNames=WSS_A14049 {ECO:0000313|EMBL:EKT82055.1};
OS Rhodococcus opacus M213.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1129896 {ECO:0000313|EMBL:EKT82055.1, ECO:0000313|Proteomes:UP000005951};
RN [1] {ECO:0000313|EMBL:EKT82055.1, ECO:0000313|Proteomes:UP000005951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M213 {ECO:0000313|EMBL:EKT82055.1,
RC ECO:0000313|Proteomes:UP000005951};
RX PubMed=23409266;
RA Pathak A., Green S.J., Ogram A., Chauhan A.;
RT "Draft Genome Sequence of Rhodococcus opacus Strain M213 Shows a Diverse
RT Catabolic Potential.";
RL Genome Announc. 1:E00144-12(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:EKT82055.1}.
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DR EMBL; AJYC02000042; EKT82055.1; -; Genomic_DNA.
DR RefSeq; WP_005256596.1; NZ_AJYC02000042.1.
DR AlphaFoldDB; K8XXZ5; -.
DR Proteomes; UP000005951; Unassembled WGS sequence.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKT82055.1}.
FT DOMAIN 1..236
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 245..474
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 502 AA; 53109 MW; 82DF70A6C8FB16C3 CRC64;
MARLTAPELL DLVVDAGTWE SWDTPPIQVA ADSEYADELL RAQEKTGLDE AVLTGVATIR
GRRTAILVCE FGFLGGSIGV AAGERLVAGI RRATRERLPL LALPTSGGTR MQEGTTAFLQ
MVKITAAVIK HKEAHLPYLV YLRSPTTGGV FASWGSLGHV TIAEPGALVG FLGPRVFEAL
YESPFPAGVQ TAENLHAHGL IDAVRPPDQL AEIVDRALRI ITSGRGGRPS LADAPVHESL
PDVPAWDSVV ASRREDRPGV REVMFHSASD VLPLNGTGQG EVDPGLILAL VRFGDMPCVL
LGQDRRGQTT RSPLGPGALR EARRGMRLAA ELNLPLVTVI DTAGAALSKE AEEGGLAGEI
ARCIADMVSL DVPTISLLLG QGTGGGALAL IPADRVLAAQ HGWLSPLPPE GASAILHHDI
AHAPDMAARQ GIRSSDLLAT GIVDEVIREF PDAAEESTAF CIRVGAVLHR ELSLLDAADT
TQRLSDRAER FDRIGLLQPA HA
//
