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Database: UniProt
Entry: A0A0F2RKE2_9PROT
LinkDB: A0A0F2RKE2_9PROT
Original site: A0A0F2RKE2_9PROT 
ID   A0A0F2RKE2_9PROT        Unreviewed;       381 AA.
AC   A0A0F2RKE2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   13-SEP-2023, entry version 21.
DE   RecName: Full=Thiolase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=VR70_08735 {ECO:0000313|EMBL:KJS39134.1};
OS   Rhodospirillaceae bacterium BRH_c57.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae.
OX   NCBI_TaxID=1629718 {ECO:0000313|EMBL:KJS39134.1, ECO:0000313|Proteomes:UP000033468};
RN   [1] {ECO:0000313|EMBL:KJS39134.1, ECO:0000313|Proteomes:UP000033468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c57 {ECO:0000313|EMBL:KJS39134.1};
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 (MAR-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:KJS39134.1}.
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DR   EMBL; LAEA01000120; KJS39134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2RKE2; -.
DR   STRING; 1629718.VR70_08735; -.
DR   Proteomes; UP000033468; 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; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Transferase {ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          4..217
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          259..352
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
SQ   SEQUENCE   381 AA;  38883 MW;  12A19CA837A2FAA3 CRC64;
     MTGVWIAGTG VTPFGRHADL DVVALGARAA RDALAASGLA ASQITMGVFA NALAGRLMGA
     LTLGQNVLAE VGISRIPVVN VENACTSGST ALHLAWTAIR AGEADAVLVV GAEKMCVPQM
     GLIDSGETQI DTLLGMVTPA SFALRAMRHV HEFGTTPLQL AAVSVKNRAN AAHNPIAMFR
     APVSLPEVLD APLIADPLTR LQCCPIADGA AAVVLVNDRL ARRLGATVQV AASVLTSGGY
     DSDGDLVRWE TDSRTAALAY DKAGVGPGDL DLVECHDAFT IAEILHYEGL GLCPTGEGGR
     FVESGAASIG GRIPVNPSGG LIGRGHPVGA TGVAQVVEIA EQLLGRAGGR QVEGARLGLA
     HCMGGDKDGD AKSCTIAILK R
//
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