ID A0A1G5PXB2_9MICC Unreviewed; 412 AA.
AC A0A1G5PXB2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=SAMN02799638_01460 {ECO:0000313|EMBL:SCZ54295.1};
OS Arthrobacter sp. UNCCL28.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1502752 {ECO:0000313|EMBL:SCZ54295.1, ECO:0000313|Proteomes:UP000199526};
RN [1] {ECO:0000313|EMBL:SCZ54295.1, ECO:0000313|Proteomes:UP000199526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNCCL28 {ECO:0000313|EMBL:SCZ54295.1,
RC ECO:0000313|Proteomes:UP000199526};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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; FMWE01000002; SCZ54295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5PXB2; -.
DR STRING; 1502752.SAMN02799638_01460; -.
DR OrthoDB; 1402717at2; -.
DR Proteomes; UP000199526; 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 CDD; cd00751; 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; 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; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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 Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SCZ54295.1}.
FT DOMAIN 5..280
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 289..410
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 95
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 367
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 397
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 412 AA; 42747 MW; 1085667577C07C2E CRC64;
MTEAVIVSTA RSPIGRAFKG SLKDERPDDL ATAMVQAALA KIPAFDPGSE DGRGLDDLLL
GCAEPSGEAG SNMARVVAVL AGMDRVPAAT VNRFCASSLQ TLRMAFHAIK AGEAQAIVSA
GVESVSRYQN WAGAGETDTA NHNPLFAAAA QRTASRAASN IPWTDPRMGG RLPDIYISMG
QTAENVATTY GISRAEQDEW GVLSQNRAEA AIASGFYARE ITPYTRKDGT LVERDDSPRA
GVSLEGVSAL QPVFRPEGTV TAGNACPLND GAAAVVVMSD SLAHELGLQP LARVVSTGVS
ALSPELMGMG PVESTRRALA QAGLTMDDID LVELNEAFAV QVVASARELG IDPAKLNVHG
GAIALGHPFG MTGARMTTTL LNGLKERDGT LGLATLCVGG GQGMAVVFER LS
//
