ID A0A150UDP0_9BRAD Unreviewed; 393 AA.
AC A0A150UDP0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=propanoyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00012352};
DE EC=2.3.1.176 {ECO:0000256|ARBA:ARBA00012352};
DE AltName: Full=Propanoyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00032316};
GN ORFNames=SE92_21095 {ECO:0000313|EMBL:KYG22408.1};
OS Bradyrhizobium sp. AT1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=574934 {ECO:0000313|EMBL:KYG22408.1, ECO:0000313|Proteomes:UP000075342};
RN [1] {ECO:0000313|EMBL:KYG22408.1, ECO:0000313|Proteomes:UP000075342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT1 {ECO:0000313|EMBL:KYG22408.1,
RC ECO:0000313|Proteomes:UP000075342};
RA Okubo T., Minamisawa K.;
RT "Evolution of nitrogen fixation genes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, 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:KYG22408.1}.
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DR EMBL; JXDL01000001; KYG22408.1; -; Genomic_DNA.
DR RefSeq; WP_063198032.1; NZ_JXDL01000001.1.
DR AlphaFoldDB; A0A150UDP0; -.
DR STRING; 574934.SE92_21095; -.
DR PATRIC; fig|574934.3.peg.4465; -.
DR OrthoDB; 9790314at2; -.
DR Proteomes; UP000075342; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
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; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
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.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Transferase {ECO:0000256|RuleBase:RU003557};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 4..191
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..362
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 393 AA; 41271 MW; F9A2554BB86A7A5D CRC64;
MSDVIVAGVG MIPFAKPGAS APYHEMGTEA VKLALADAGL GYDEVEQAYV GYVYGDSTCG
QRALYPVGMT GIPIVNVNNN CSTGSTALFM ARQMIASGAL DCVLAVGFEQ MKPGALGSVY
TDRPSAFEEF DAAADELIDA PGIPLALRYF GGAGLSHMKK YGTPLDAFAK VRAKASRHAK
NNPLALFRKE VTADDVMNDQ VIWPGVMTRL MACPPTCGGA AAVLVSERFA DKHGIGKQVR
ITAQAMTTDT PSTFKAGDMM QLVGYDMAKE AASRVYESAG IGPDDLDVVE LHDCFAHNEL
ITYEALGLCG EGEAGKFIND GDNTYGGRIV TNPSGGLLSK GHPLGATGLA QCYELTRQLR
GTAGATQVEG AKVALQHNLG LGGACVVTLY KRH
//
