ID   Y3007_MYCPA             Reviewed;         281 AA.
AC   Q73VK6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Uncharacterized oxidoreductase MAP_3007;
DE            EC=1.-.-.-;
GN   OrderedLocusNames=MAP_3007;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; AE016958; AAS05555.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q73VK6; -.
DR   SMR; Q73VK6; -.
DR   STRING; 262316.MAP_3007; -.
DR   EnsemblBacteria; AAS05555; AAS05555; MAP_3007.
DR   KEGG; mpa:MAP_3007; -.
DR   eggNOG; COG0656; Bacteria.
DR   HOGENOM; CLU_023205_0_1_11; -.
DR   OMA; KLWPTDQ; -.
DR   Proteomes; UP000000580; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   PANTHER; PTHR43827; PTHR43827; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..281
FT                   /note="Uncharacterized oxidoreductase MAP_3007"
FT                   /id="PRO_0000380738"
FT   ACT_SITE        56
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         194..246
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   281 AA;  30013 MW;  AEB37E987EA7747F CRC64;
     MTGESGSAAP SIALNDENTM PVLGLGVAEL SDDETERAVS AALEVGCRLI DTAAAYGNEA
     AVGRAIAASG IPRAELFVTT KLATSDQGFK GAMDACEASL ERLGLDYVDL YLIHWPAPAL
     GTYVNSFGGM IQSRGNGHAR SIGVSNFTEE YLTTVIDLTF VTPAVNQIEL HPLLNQEALR
     KTNAEHNVVT QSYTPLALGK LNDHPTVNSV AAEYGKTASQ VLLRWNLQLS NAVIFRSANA
     EHIASDFDVF DFELAAEHMD AINALNDGTR LRPDPDTYEG S