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Database: UniProt
Entry: A0A0M2H7P2_9MICO
LinkDB: A0A0M2H7P2_9MICO
Original site: A0A0M2H7P2_9MICO 
ID   A0A0M2H7P2_9MICO        Unreviewed;       402 AA.
AC   A0A0M2H7P2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Putative acyltransferase {ECO:0000313|EMBL:KJL40130.1};
DE            EC=2.3.1.- {ECO:0000313|EMBL:KJL40130.1};
GN   Name=fadA_2 {ECO:0000313|EMBL:KJL40130.1};
GN   ORFNames=RS81_01720 {ECO:0000313|EMBL:KJL40130.1};
OS   Microbacterium ketosireducens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL40130.1, ECO:0000313|Proteomes:UP000033956};
RN   [1] {ECO:0000313|EMBL:KJL40130.1, ECO:0000313|Proteomes:UP000033956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL40130.1,
RC   ECO:0000313|Proteomes:UP000033956};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) 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}.
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:KJL40130.1}.
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DR   EMBL; JYIZ01000047; KJL40130.1; -; Genomic_DNA.
DR   RefSeq; WP_045275657.1; NZ_JYIZ01000047.1.
DR   AlphaFoldDB; A0A0M2H7P2; -.
DR   STRING; 92835.RS81_01720; -.
DR   PATRIC; fig|92835.4.peg.1739; -.
DR   OrthoDB; 3204099at2; -.
DR   Proteomes; UP000033956; Unassembled WGS sequence.
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; -; 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; PTHR43365; BLR7806 PROTEIN; 1.
DR   PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 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:KJL40130.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033956};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KJL40130.1}.
FT   DOMAIN          5..228
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          280..401
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        91
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        358
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        388
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   402 AA;  41899 MW;  D0C3155417CA01F7 CRC64;
     MPEAYIYDAV RTPRGRNKGG SLHSVKPVDL VVGLIDALRE RNPSLRADLI DDIVLGVVSP
     VGEQGGDIAR TAALVAGLPE TVAGVQVNRF CASGLEAVNL AAQKVASGYE DLVLAGGVES
     MSRVPIGSDG GAYAQDPTTG YDHYFVPQGI GADLIATIEG FSREDVDAFA ARSQARADTA
     WREGRFAASV VPVTDINGVT LLAEDEHRRP GSTVESLGQL PASFAALGEQ AGFDAVALQK
     YHWVEKIDHV HGPGNSSGIV DGAALVVIGT REIGERLGLT PRARIVSTAV TGSDPTIMLT
     GPTPATQKAL EKAGLDASDI DLFELNEAFA AVVMKWQKDL GIPDDKVNVN GGAIALGHPL
     GATGAMILGT LLDELERQDL RRGLATLCVG AGMGIATVIE RV
//
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