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Database: UniProt
Entry: I3TIE7_TISMK
LinkDB: I3TIE7_TISMK
Original site: I3TIE7_TISMK 
ID   I3TIE7_TISMK            Unreviewed;       301 AA.
AC   I3TIE7;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Peroxisomal multifunctional enzyme type 2 {ECO:0000313|EMBL:AFK52535.1};
GN   OrderedLocusNames=TMO_0696 {ECO:0000313|EMBL:AFK52535.1};
OS   Tistrella mobilis (strain KA081020-065).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK52535.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK52535.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK52535.1,
RC   ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(2012).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|RuleBase:RU000363}.
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DR   EMBL; CP003236; AFK52535.1; -; Genomic_DNA.
DR   RefSeq; WP_014744215.1; NC_017956.1.
DR   AlphaFoldDB; I3TIE7; -.
DR   STRING; 1110502.TMO_0696; -.
DR   KEGG; tmo:TMO_0696; -.
DR   PATRIC; fig|1110502.3.peg.720; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_14_0_5; -.
DR   Proteomes; UP000005258; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR45024:SF3; BLL2957 PROTEIN; 1.
DR   PANTHER; PTHR45024; DEHYDROGENASES, SHORT CHAIN; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005258}.
SQ   SEQUENCE   301 AA;  32099 MW;  B5FB74DB47901F87 CRC64;
     MLEGKSVVVT GAGRGIGRDI ALLLAAKGAK VMVNDLGGSD KGDGADDAPA REVVREIEAA
     GGEAVADFGD VSQLDDAEAM IETAVRQFGR IDGVVNNAGI LRDMIFHKMT PEAWQAVISV
     HLNGSFNTSY AAARHFREQG SGRFVHFTST SGLIGNYGQA NYAAAKLGIV GLSRSIALDM
     ARFGVTSNCI APFAWSRLIG TIPVTNEAEM ARVQRIKEMT PNKIAPLVAA LLSDQSADVT
     GQIFTVRNNE IFLMSQPRPV RSAHRSEGWT AETVLSHALP AMRAGFTPLE RSGDVFSWDP
     V
//
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