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Database: UniProt
Entry: F3ZC91_9ACTN
LinkDB: F3ZC91_9ACTN
Original site: F3ZC91_9ACTN 
ID   F3ZC91_9ACTN            Unreviewed;       316 AA.
AC   F3ZC91;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Putative dehydrogenase {ECO:0000313|EMBL:EGJ78908.1};
GN   ORFNames=STTU_6119 {ECO:0000313|EMBL:EGJ78908.1};
OS   Streptomyces sp. Tu6071.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ78908.1};
RN   [1] {ECO:0000313|EMBL:EGJ78908.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tu6071 {ECO:0000313|EMBL:EGJ78908.1};
RA   Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., Bechthold A.,
RA   Gunther S.;
RT   "Genome sequence of Streptomyces sp. Tu6071.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the HIBADH-related family.
CC       {ECO:0000256|ARBA:ARBA00009080}.
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DR   EMBL; CM001165; EGJ78908.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3ZC91; -.
DR   HOGENOM; CLU_035117_0_4_11; -.
DR   Proteomes; UP000003955; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0016054; P:organic acid catabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR029154; HIBADH-like_NADP-bd.
DR   InterPro; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43580; OXIDOREDUCTASE GLYR1-RELATED; 1.
DR   PANTHER; PTHR43580:SF2; OXIDOREDUCTASE GLYR1-RELATED; 1.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000103; HIBADH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          31..186
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          190..306
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        196
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ   SEQUENCE   316 AA;  32312 MW;  4B3BFA794601C822 CRC64;
     MEGARGDSDP ARPAGRTARQ GGTLMSDAPL VAVLGTGIMG AGMARSLLRE GLSVRVWNRS
     TDKARPLVAD GAELAADPAA AVRGADVVLT VLNDGTAVAS VMEQAAEGLR AGQPWLQAST
     VGLAATATLA EKAAAHGVVY LDSPVSGTKE PAEQGKLIVL VSGDEAARPA VTPVLDAIGQ
     RTVWAGSEPG DATRLKLVVN SWLVNLVSAV AESLNVADAL GVDPRLFLDT VTGGALDSPY
     LQMKADALLK GALDPSFALS TALKDTRLIL EATRGSGARL DLLDATAARF ARARDEGHGG
     EDMIATYFAG QPEGNA
//
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