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Database: UniProt
Entry: A0A124IN01_9FIRM
LinkDB: A0A124IN01_9FIRM
Original site: A0A124IN01_9FIRM 
ID   A0A124IN01_9FIRM        Unreviewed;       384 AA.
AC   A0A124IN01;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Propanoyl-CoA acyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=APF81_25835 {ECO:0000313|EMBL:KUO70654.1};
OS   Desulfosporosinus sp. BRH_c37.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1734396 {ECO:0000313|EMBL:KUO70654.1, ECO:0000313|Proteomes:UP000053148};
RN   [1] {ECO:0000313|EMBL:KUO70654.1, ECO:0000313|Proteomes:UP000053148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c37 {ECO:0000313|EMBL:KUO70654.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|RuleBase:RU003557}.
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:KUO70654.1}.
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DR   EMBL; LOEW01000288; KUO70654.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124IN01; -.
DR   Proteomes; UP000053148; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd00829; SCP-x_thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020616; Thiolase_N.
DR   PANTHER; PTHR42870; ACETYL-COA C-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR42870:SF1; NON-SPECIFIC LIPID-TRANSFER PROTEIN-LIKE 2; 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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Transferase {ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          4..186
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          256..352
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
SQ   SEQUENCE   384 AA;  40626 MW;  E299A0CC65FCD3B0 CRC64;
     MRDVYVVGVG MTDYYRKSPI PGADLGRKAI LYALRDAGIT PQQVQSVYQG EMPGLSGSIC
     FGQRVACTMG MGGVSIMNVE SACSSGALAV NLAMKDVANG VTDISMAVGV QNISAARTAG
     TAFSPDANDP EGIQGITMPG IYAMRAKRYM HEFGATPEDL AKVAVKNRRH AMNNPRSQFH
     EPITVEQIVN ARSISDPLTL LMSCPNVDAG AAVILTTKEK AMQLGSKLVK ILASEVTSGI
     FTNGFRDMTS MEITVRGSKE AYEIAGVGPE DIDMVECHDA FAINEHLYTE AMGFCGHGEA
     VEFIRSGGND YGGKVVFSPR GGLMSCGHPT GCTGAAQVVE ATWQLRNEAG AMQIPDCKVA
     LTHVTGGGIY GLDNAVCTIH ILSR
//
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