ID A0A1V0PYP7_9RHOB Unreviewed; 391 AA.
AC A0A1V0PYP7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acetyl-CoA acetyltransferase of ethylmalonyl-CoA pathway {ECO:0000313|EMBL:ARE41272.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:ARE41272.1};
GN ORFNames=RGUI_3131 {ECO:0000313|EMBL:ARE41272.1};
OS Rhodovulum sp. P5.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=1564506 {ECO:0000313|EMBL:ARE41272.1, ECO:0000313|Proteomes:UP000191808};
RN [1] {ECO:0000313|EMBL:ARE41272.1, ECO:0000313|Proteomes:UP000191808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P5 {ECO:0000313|EMBL:ARE41272.1,
RC ECO:0000313|Proteomes:UP000191808};
RA Tang K.;
RT "Shallow-sea hydrothermal system.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; CP015039; ARE41272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0PYP7; -.
DR STRING; 1564506.RGUI_3131; -.
DR KEGG; rhc:RGUI_3131; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000191808; Chromosome.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:ARE41272.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000191808};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ARE41272.1}.
FT DOMAIN 4..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..390
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 391 AA; 40938 MW; ED51FE62724BA32E CRC64;
MTNVVIVSAA RTPVGSFNGS FATVPAHDLG KVMLEALVER AGIDKSEVSE TILGQVLTAG
QGQNPARQAH INAGLPIESA AWSINQVCGS GLRSVALAAQ HIMLGDAAIV AAGGQENMTL
CPHVAHLRAG HKMGDVKFID AMIKDGLWDA FNGYHMGQTA ENVAEQWQIS REQQDEFALA
SQNKAEAAQK AGKFQDEIVS VTVPNRKGDI VVDADEYIRH GATIENMQKL RPAFAKDGSV
TAGNASGIND GAAGALLMSA EEAEKRGLEP LARIVSYATA GLDPSIMGTG PIPASRKALE
KAGWKAEDLD LVEANEAFAA QACAVNKDMG WNPEVVNVNG GAIAIGHPIG ASGARILNTL
LFEMKRRDAK KGLATLCIGG GMGVAMCLER P
//
