ID A0A136MUI2_9BACT Unreviewed; 303 AA.
AC A0A136MUI2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Inositol 2-dehydrogenase {ECO:0000313|EMBL:KXK37526.1};
DE EC=1.1.1.18 {ECO:0000313|EMBL:KXK37526.1};
GN Name=iolG_9 {ECO:0000313|EMBL:KXK37526.1};
GN ORFNames=UZ16_OP3001001077 {ECO:0000313|EMBL:KXK37526.1};
OS Candidatus Hinthialibacteria bacterium OLB16.
OC Bacteria; Candidatus Hinthialibacterota.
OX NCBI_TaxID=1617433 {ECO:0000313|EMBL:KXK37526.1, ECO:0000313|Proteomes:UP000070296};
RN [1] {ECO:0000313|EMBL:KXK37526.1, ECO:0000313|Proteomes:UP000070296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB16 {ECO:0000313|EMBL:KXK37526.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXK37526.1}.
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DR EMBL; LMZT01000052; KXK37526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136MUI2; -.
DR STRING; 1617433.UZ16_OP3001001077; -.
DR PATRIC; fig|1617433.3.peg.1161; -.
DR Proteomes; UP000070296; Unassembled WGS sequence.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0050112; F:inositol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR043906; Gfo/Idh/MocA_OxRdtase_bact_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43818; BCDNA.GH03377; 1.
DR PANTHER; PTHR43818:SF5; OXIDOREDUCTASE FAMILY PROTEIN; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF19051; GFO_IDH_MocA_C2; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:KXK37526.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..303
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007476101"
FT DOMAIN 42..165
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 195..261
FT /note="Gfo/Idh/MocA-like oxidoreductase bacterial type C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF19051"
SQ SEQUENCE 303 AA; 33338 MW; 1D5458E13E5710F9 CRC64;
MKSISRRNFI SKSAVAAVGA GLAGQAVTAL AEDAKVSAND KISVALIGCG GQGRADLNAF
LRSPEIECLA LCDVDPTHLE KAQKGVEDKT GRKPDGHKDF REIIDRKDID VVIVATPDHW
HPIPTMLACQ TGKDVYVEKP LSVSIGEGRA MVKAARKHNR VVQMGTQQRS AGHFKDAVAF
VKSGELGKIR LVRTWAYLDW KGELPKVEDS DPPEGVDYDM WLGPAPKRPF NKRRFHFDFR
WYWDYSGGLM TDWGAHMIDI ANMGMDVISP KSALSIGGKN GYPDDAMETP DTQQAILEYD
ATP
//