ID A0PKW2_MYCUA Unreviewed; 493 AA.
AC A0PKW2;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Acetyl-coenzyme a carboxylase carboxyl transferase (Subunit beta) AccD3 {ECO:0000313|EMBL:ABL02981.1};
GN Name=accD3 {ECO:0000313|EMBL:ABL02981.1};
GN OrderedLocusNames=MUL_0237 {ECO:0000313|EMBL:ABL02981.1};
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL02981.1, ECO:0000313|Proteomes:UP000000765};
RN [1] {ECO:0000313|EMBL:ABL02981.1, ECO:0000313|Proteomes:UP000000765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99 {ECO:0000313|EMBL:ABL02981.1,
RC ECO:0000313|Proteomes:UP000000765};
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D., Davies J.K., Jenkin G.A., Small P.L., Jones L.M., Tekaia F.,
RA Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
CC -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC {ECO:0000256|ARBA:ARBA00006102}.
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DR EMBL; CP000325; ABL02981.1; -; Genomic_DNA.
DR RefSeq; WP_011738606.1; NC_008611.1.
DR AlphaFoldDB; A0PKW2; -.
DR KEGG; mul:MUL_0237; -.
DR eggNOG; COG0777; Bacteria.
DR eggNOG; COG0825; Bacteria.
DR HOGENOM; CLU_015486_2_1_11; -.
DR Proteomes; UP000000765; Chromosome.
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:ABL02981.1}.
FT DOMAIN 1..236
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 213..467
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 493 AA; 51513 MW; 627F333E01B7469B CRC64;
MSRITTDQLR DAVLDEDSFI SWDTPPLEVP ISESYARDLA DVRAATGRDE SVLTGEGRVL
GRRVAVVACE FDFLAGSIGV AAAERITAAM ERATSQRLPL LASPSSGGTR MQEGTVAFLQ
MVKIAAAVRL HKQAHLPYLV YLRHPTTGGV FASWGSLGHV TVAEPGALIG FLGPRVYELL
YDEPFPAGVQ TAENLQRHGV IDGVVTLDEL RRTLDRALTV LTDAPAPAPA APAPPAIPDV
AAWTSVLASR RPDRPGVEHL LRYGATDRVL LSGTGYGDAA TTLLALARMA GQPMVVLGQQ
GIGGGIIGPA SLREARRGMA LAAELRLPLV LVIDTAGPAL SADAEQGGLA GQIAQCLAEL
VTLGTPTVSV LLGQGSGGPA LAMVPADRVL AAQHGWLAPL PPEGASAIVF RDTTHAAELA
AAQGIRSADL LAAGIVDVIV PELPDAAAEP VEFAQRLSIA IATEVAALRE IPDAQRMTAR
LARYRSIGLP RDR
//
