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Database: UniProt
Entry: A0A0Q9EUG1_9GAMM
LinkDB: A0A0Q9EUG1_9GAMM
Original site: A0A0Q9EUG1_9GAMM 
ID   A0A0Q9EUG1_9GAMM        Unreviewed;       328 AA.
AC   A0A0Q9EUG1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Short-chain dehydrogenase {ECO:0000313|EMBL:KRD69396.1};
GN   ORFNames=ASE45_09560 {ECO:0000313|EMBL:KRD69396.1};
OS   Lysobacter sp. Root96.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1736612 {ECO:0000313|EMBL:KRD69396.1, ECO:0000313|Proteomes:UP000050805};
RN   [1] {ECO:0000313|EMBL:KRD69396.1, ECO:0000313|Proteomes:UP000050805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root96 {ECO:0000313|EMBL:KRD69396.1,
RC   ECO:0000313|Proteomes:UP000050805};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRD69396.1, ECO:0000313|Proteomes:UP000050805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root96 {ECO:0000313|EMBL:KRD69396.1,
RC   ECO:0000313|Proteomes:UP000050805};
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 short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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:KRD69396.1}.
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DR   EMBL; LMJN01000002; KRD69396.1; -; Genomic_DNA.
DR   RefSeq; WP_056305488.1; NZ_LMJN01000002.1.
DR   AlphaFoldDB; A0A0Q9EUG1; -.
DR   STRING; 1736612.ASE45_09560; -.
DR   OrthoDB; 9809287at2; -.
DR   Proteomes; UP000050805; Unassembled WGS sequence.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR48107:SF16; NADPH-DEPENDENT ALDEHYDE REDUCTASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR48107; NADPH-DEPENDENT ALDEHYDE REDUCTASE-LIKE PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050805}.
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   328 AA;  35093 MW;  BDA41BDE13E3F5E3 CRC64;
     MASTSKKAAK TTAGRQRAIQ RGVDALDRKK KPSEAKDQPV QAGTRKQPQN PMPAQHLRKP
     GNEHDLALSP KFLAPDYLGS GKLEGMTAVV TGGDSGIGRA VAVLFAREGA DVAIVYLDEH
     EDAADTRRHV EQEGRQCLAL AGDVKDPAFC KQAIEQTVRK FGRLDILVNN AAFQLHSERL
     EDLSDEHLQE TLQTNIAGYF HMARAALPHL KRGAAIINSG SETGIFGSKA LLDYSATKGA
     IHAFTKSLAS NLLERGTRVN AVAPGPVWTP LNPADRAAEE VAKFGQDSDM GRPAQPEEIS
     PAYVFLASPV CSSYVNGVVL PVMGGPRG
//
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