ID H6C3P8_EXODN Unreviewed; 391 AA.
AC H6C3P8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Myo-inositol 2-dehydrogenase {ECO:0000313|EMBL:EHY58263.1};
GN ORFNames=HMPREF1120_06275 {ECO:0000313|EMBL:EHY58263.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY58263.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY58263.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY58263.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family.
CC {ECO:0000256|ARBA:ARBA00010928}.
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DR EMBL; JH226134; EHY58263.1; -; Genomic_DNA.
DR RefSeq; XP_009158724.1; XM_009160476.1.
DR AlphaFoldDB; H6C3P8; -.
DR STRING; 858893.H6C3P8; -.
DR GeneID; 20310914; -.
DR VEuPathDB; FungiDB:HMPREF1120_06275; -.
DR eggNOG; KOG2741; Eukaryota.
DR HOGENOM; CLU_023194_0_0_1; -.
DR InParanoid; H6C3P8; -.
DR OMA; AWTIFLE; -.
DR OrthoDB; 1992171at2759; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42840:SF3; BINDING ROSSMANN FOLD OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G10240)-RELATED; 1.
DR PANTHER; PTHR42840; NAD(P)-BINDING ROSSMANN-FOLD SUPERFAMILY PROTEIN-RELATED; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007304}.
FT DOMAIN 27..138
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 167..366
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
FT REGION 371..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 42743 MW; F750644EF996E0AF CRC64;
MASSLRSPSS LFSSSLQSAD EMPGRKLKVA IAGLGRMGAR HALHFYNLTP RAEVIAVTSP
ELKELEWANR TLEGVRTYAD YDEMLREEKD LEAVVISSAT IVHAEQAIKA INLGLHVLCE
KPLSTSPEVS QSVLSAYQNS IKRFPNQKVI CGFSRRFDAS YRDAYQKVRS GVVGKPAVIR
SQTCDKLDPS GFFVEYAQFS GGIFVDCSIH DIDLALWFFG EDSVVKSVSA VGITAVSPEL
RKYNDRDNAV GIIEFYGGKI CQLYCSRMMA AGQEDCTEIT GTKGKVSVNT QPTGTLVNIY
EPSGIRREIP QDYYGRFREA FITEANEFTA CCLDNTEVPL RLEGAVAAVK IGGALQESLI
TGKKIEFDER GKRIGAPAPR GGGQAPLSAR L
//