ID A0A0T1WBE1_9MYCO Unreviewed; 335 AA.
AC A0A0T1WBE1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KQY06324.1};
GN ORFNames=ASD37_18720 {ECO:0000313|EMBL:KQY06324.1};
OS Mycobacterium sp. Root135.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1736457 {ECO:0000313|EMBL:KQY06324.1, ECO:0000313|Proteomes:UP000051127};
RN [1] {ECO:0000313|EMBL:KQY06324.1, ECO:0000313|Proteomes:UP000051127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root135 {ECO:0000313|EMBL:KQY06324.1,
RC ECO:0000313|Proteomes:UP000051127};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY06324.1, ECO:0000313|Proteomes:UP000051127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root135 {ECO:0000313|EMBL:KQY06324.1,
RC ECO:0000313|Proteomes:UP000051127};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family.
CC {ECO:0000256|ARBA:ARBA00010928}.
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:KQY06324.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMEZ01000006; KQY06324.1; -; Genomic_DNA.
DR RefSeq; WP_056554736.1; NZ_LMEZ01000006.1.
DR AlphaFoldDB; A0A0T1WBE1; -.
DR STRING; 1736457.ASD37_18720; -.
DR OrthoDB; 256869at2; -.
DR Proteomes; UP000051127; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051127}.
FT DOMAIN 4..119
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 131..329
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
SQ SEQUENCE 335 AA; 34993 MW; 5021456BA4EBC8A3 CRC64;
MTTLGVIGLG RIGAFHTETL SGLAGIDELV ITDERGDVAE AVAAKHGARY VATVDELLSS
GVDGVVVAAA TPAHAELTLA AVARGIPTFC EKPIASTAVE SARVAEAILA SGVPVQVGYQ
RRYDAAFAAA KRAVDDGSLG KLHTVRSTTM DPAPPPLDYI KGSGGIFRDC AVHDFDVINW
ITGQRAVEVY ATGTVQGDPL FAEYGDVDTA AVIVKFDGGA LGVVSNARYN ARGYDCRLEV
HGFDDSVAAG WDQGVPLRNT DPDNDFPTGP SHGFFMDRFT EAFRTELAAF VEVTKGGPVL
GATVADAVEV AWLAEAATES LKRGTPVTIA EVRNA
//