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Database: UniProt
Entry: A0A318S775_9DEIO
LinkDB: A0A318S775_9DEIO
Original site: A0A318S775_9DEIO 
ID   A0A318S775_9DEIO        Unreviewed;       391 AA.
AC   A0A318S775;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Threonine dehydrogenase-like Zn-dependent dehydrogenase {ECO:0000313|EMBL:PYE53547.1};
GN   ORFNames=DES52_10876 {ECO:0000313|EMBL:PYE53547.1};
OS   Deinococcus yavapaiensis KR-236.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=694435 {ECO:0000313|EMBL:PYE53547.1, ECO:0000313|Proteomes:UP000248326};
RN   [1] {ECO:0000313|EMBL:PYE53547.1, ECO:0000313|Proteomes:UP000248326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18048 {ECO:0000313|EMBL:PYE53547.1,
RC   ECO:0000313|Proteomes:UP000248326};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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:PYE53547.1}.
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DR   EMBL; QJSX01000008; PYE53547.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A318S775; -.
DR   OrthoDB; 9769198at2; -.
DR   Proteomes; UP000248326; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08283; FDH_like_1; 1.
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; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248326};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          26..145
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          196..264
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   391 AA;  42213 MW;  397C2219F917B8C0 CRC64;
     MKALVWQGVN RVGIENVPDP QILQPTDAIV KITSTAICGS DLHLLDGYVP TMMHGDILGH
     EFMGEIVDVG KDVRNVRVGD RVIVPFPISC GSCWYCTHDE SSLCDNSNPN AKNAEALWGH
     SPAGIYGYSH ITGGYSGGQA QYARTVFADS NLFKVPSHLT DDQVLFLTDI LPTGYMGAEQ
     ANIEPGDVVA VWGCGPVGQF VIRSAFLLGA GRVIAIDRFA ERLAMAEAAG AEALNYEKVD
     VFTSLKEMTA GRGPDSVIDA VGLEAHGQGL GGVYDAVKQT TRVAETERPH ALRAAIQACR
     KGGTVSVPGV YGGLGDKIPM GAFMNKGLEM HSGQTHVHRY VKRLLNHIEE GRIHPEEIIT
     HRLSLDEAPQ GYQMFKKKHD GCVKVVLNPW A
//
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