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Database: UniProt
Entry: A0A1U7GIQ0_9BACT
LinkDB: A0A1U7GIQ0_9BACT
Original site: A0A1U7GIQ0_9BACT 
ID   A0A1U7GIQ0_9BACT        Unreviewed;       456 AA.
AC   A0A1U7GIQ0;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:OJW18933.1};
GN   ORFNames=BGO49_17975 {ECO:0000313|EMBL:OJW18933.1};
OS   Planctomycetales bacterium 71-10.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales.
OX   NCBI_TaxID=1895807 {ECO:0000313|EMBL:OJW18933.1, ECO:0000313|Proteomes:UP000185848};
RN   [1] {ECO:0000313|EMBL:OJW18933.1, ECO:0000313|Proteomes:UP000185848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=71-10 {ECO:0000313|EMBL:OJW18933.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJW18933.1}.
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DR   EMBL; MKTT01000085; OJW18933.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U7GIQ0; -.
DR   STRING; 1895807.BGO49_17975; -.
DR   Proteomes; UP000185848; 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; 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   PANTHER; PTHR43818; BCDNA.GH03377; 1.
DR   PANTHER; PTHR43818:SF10; NADH-DEPENDENT DEHYDROGENASE-RELATED; 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;
FT   DOMAIN          50..164
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
FT   DOMAIN          224..280
FT                   /note="Gfo/Idh/MocA-like oxidoreductase bacterial type C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19051"
SQ   SEQUENCE   456 AA;  50059 MW;  58681A300B95ACC6 CRC64;
     MSDDSTPRRE ATGSALSRRR FHRATAAAAL GAFAAPAVVR GRNLNERLAI ACIGVGGRGA
     SNLADVASED VVALCDVYDG AVARAAEAHP KARKFKDFRK LFDDLKGYDA VVVSTTEHTH
     AFATLPALQL GKHVYCEKPL THDVWEARRI REAAAKAGVA TQMGTQIHAG DNYRRVVELV
     QAGAVGAVKE VHVWVGRAWG RQSPEEAKAN GDIVSVTERP DGSTPVPSGL DWDLWLGPVA
     ERPFHEVYFP GPKWYRWWDF GNGTMSDLGS HWIDLPFWAL KLKAPSTIEA FGPPAPPEIA
     PASMKAVYEY EAKGDQPALT LTWYQGSMKP EPWASGAIPK WDSGVLFVGE KGMLLSDYGR
     HVLLPEDRFR DYRRPEPTIP KSLGHHAEWI HACKTGAPTT CNFEYAGWLT EANHLGNVAY
     RVGRKLEWDA AALGATNASE AEPFLRRDYR PGWSLG
//
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