ID Q09EA5_STIAD Unreviewed; 347 AA.
AC Q09EA5;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Inositol 2-dehydrogenase {ECO:0000313|EMBL:EAU70091.1};
DE EC=1.1.1.18 {ECO:0000313|EMBL:EAU70091.1};
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:ADO74685.1};
GN OrderedLocusNames=STAUR_6929 {ECO:0000313|EMBL:ADO74685.1};
GN ORFNames=STIAU_8337 {ECO:0000313|EMBL:EAU70091.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU70091.1, ECO:0000313|Proteomes:UP000032702};
RN [1] {ECO:0000313|EMBL:EAU70091.1, ECO:0000313|Proteomes:UP000032702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU70091.1,
RC ECO:0000313|Proteomes:UP000032702};
RA Nierman W.C.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO74685.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO74685.1,
RC ECO:0000313|Proteomes:UP000001351};
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family.
CC {ECO:0000256|ARBA:ARBA00010928}.
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DR EMBL; CP002271; ADO74685.1; -; Genomic_DNA.
DR EMBL; AAMD01000001; EAU70091.1; -; Genomic_DNA.
DR STRING; 378806.STAUR_6929; -.
DR KEGG; sur:STAUR_6929; -.
DR PATRIC; fig|378806.16.peg.9475; -.
DR eggNOG; COG0673; Bacteria.
DR HOGENOM; CLU_023194_0_3_7; -.
DR OrthoDB; 9782091at2; -.
DR Proteomes; UP000001351; Chromosome.
DR Proteomes; UP000032702; Unassembled WGS sequence.
DR GO; GO:0050112; F:inositol 2-dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR030827; Myo_inos_IolG.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR04380; myo_inos_iolG; 1.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EAU70091.1}.
FT DOMAIN 19..136
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 148..344
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
SQ SEQUENCE 347 AA; 37998 MW; 10550EDF7ED5370D CRC64;
MAVPHPLPGN ARCYPHRMKL ALLGAGRIGQ IHAANIHHHP RARLHAVADV NAEAARSLGE
RYGAKASTDI DAVLADPALE GVFICTSTDT HVELILKAAR RKLPIFCEKP IDLDLAKVDT
CLAEVTRAGV PLMIGFNRRF DPHFRSLREA VRQGEAGDVE IVKITSRDPA PPPPAYVRVS
GGIFRDMMIH DLDMARFLLG EEPVEIFATG SCLVDPGIGE AGDIDTAMVI LKTQRGALCH
IDNSRRAVYG YDQRIEVFGS KGMLQAANPL PTTVTRYTRE AVLSDKPYHF FLDRYPEAYR
AELEHFLDVV TGRAEPLVTG RDGRAALVLA DAALQSLKLG KPIPIPR
//