ID A0A0Q5AUK5_9MICO Unreviewed; 348 AA.
AC A0A0Q5AUK5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=L-idonate 5-dehydrogenase {ECO:0000313|EMBL:KQQ08740.1};
GN ORFNames=ASF46_15945 {ECO:0000313|EMBL:KQQ08740.1};
OS Rathayibacter sp. Leaf296.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=1736327 {ECO:0000313|EMBL:KQQ08740.1, ECO:0000313|Proteomes:UP000050868};
RN [1] {ECO:0000313|EMBL:KQQ08740.1, ECO:0000313|Proteomes:UP000050868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ08740.1,
RC ECO:0000313|Proteomes:UP000050868};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ08740.1, ECO:0000313|Proteomes:UP000050868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ08740.1,
RC ECO:0000313|Proteomes:UP000050868};
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072}.
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:KQQ08740.1}.
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DR EMBL; LMNR01000002; KQQ08740.1; -; Genomic_DNA.
DR RefSeq; WP_056868438.1; NZ_LMNR01000002.1.
DR AlphaFoldDB; A0A0Q5AUK5; -.
DR STRING; 1736327.ASF46_15945; -.
DR Proteomes; UP000050868; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43161:SF9; SORBITOL DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000050868};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 24..133
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 176..295
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 348 AA; 35890 MW; F1674EEF5C59D178 CRC64;
MKTTSISGKL DLAVAEVPLP KPGPGEIRIR VSFVGICGSD LHYYFEGANG AFVVKEPLTP
GHELSGHVDL DPSGRLTPGT PVTIHPARFG ATDDSIPDAP HLWSGGSYLG SASTTPHTQG
AMAEYLLVDA SMVRILPQGL PVLRAVLAEP LAVGLHAVAR AGSVHGARVL ISGAGPIGLL
TAAAASAAGA SSVVVSDVLA EPLALALTIG AHETRHVGVD TIEADSFDVV FECSGAAAAI
SSAVIAVRRR GTVVQVGMVP AEARPVALAP LISKEVTLIG VFRFLDEIDE ALLLLAQRPE
IEAVVTHVLP VEDVQQAFEL AKASSVSSKV VVDLSDDRHQ VDARIVAA
//
