ID F6EMA7_HOYSD Unreviewed; 496 AA.
AC F6EMA7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase alpha and beta subunits {ECO:0000313|EMBL:AEF39313.1};
GN OrderedLocusNames=AS9A_0861 {ECO:0000313|EMBL:AEF39313.1};
OS Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS (Amycolicicoccus subflavus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC Hoyosella.
OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF39313.1, ECO:0000313|Proteomes:UP000009235};
RN [1] {ECO:0000313|EMBL:AEF39313.1, ECO:0000313|Proteomes:UP000009235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX PubMed=21725023; DOI=10.1128/JB.05388-11;
RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA Wu X.L.;
RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT actinomycete isolated from crude oil-polluted soil.";
RL J. Bacteriol. 193:4538-4539(2011).
CC -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC {ECO:0000256|ARBA:ARBA00006102}.
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DR EMBL; CP002786; AEF39313.1; -; Genomic_DNA.
DR RefSeq; WP_013805662.1; NC_015564.1.
DR AlphaFoldDB; F6EMA7; -.
DR STRING; 443218.AS9A_0861; -.
DR KEGG; asd:AS9A_0861; -.
DR eggNOG; COG0777; Bacteria.
DR eggNOG; COG0825; Bacteria.
DR HOGENOM; CLU_015486_2_1_11; -.
DR OrthoDB; 9772975at2; -.
DR Proteomes; UP000009235; 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 Reference proteome {ECO:0000313|Proteomes:UP000009235};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEF39313.1}.
FT DOMAIN 1..235
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 244..473
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 496 AA; 52840 MW; B61518CC4B13854F CRC64;
MPTTAQELFD RVLDQDSYIS WDTAPIDLPA HELYSTDLAA ARSKAGTDES VITGEGRIRG
RRVAVIACEF RFLAGSVGVA AAERIVSTIE RATAEQLPLL ASPTSGGTRM QEGTVAFLQM
VKIAAAIKHH KDAHLPYLVY LRHPTTGGVF ASWGSLGHVT VAEPGALIGF LGPRVYESLY
GEKFPEGVQT AENLYQHGVI DGVVPVRWLR PILDRVLRVV CGTIGAPSDL EPAPTLSQVP
DILAWDSVVA SRNPVRPGAR HVLRHGATTL TPLSGTGQGE ADRSMLLYLA RIRGTPCVVL
AHDRALTVES GAFGPAALRE ARRGMHLANE LRLPLVLIID TVGAALSKDA EERGLAGEIA
RCLADLVTLQ CPTVSVLLGQ GTGGGALAVL PADRVLCTQN GWLAPLPPEG AAAIVYRDTS
RAAEIAAAQG IRSRDLLESG IVDAIIPECP DASEEPIPFS QRVASAIARE IRELALIPAP
KRYAARLNRY RTLGLP
//
