ID   A0A495W395_9PSEU        Unreviewed;       380 AA.
AC   A0A495W395;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Threonine dehydrogenase-like Zn-dependent dehydrogenase {ECO:0000313|EMBL:RKT55814.1};
GN   ORFNames=C8E97_4501 {ECO:0000313|EMBL:RKT55814.1};
OS   Saccharothrix australiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=2072 {ECO:0000313|EMBL:RKT55814.1, ECO:0000313|Proteomes:UP000282084};
RN   [1] {ECO:0000313|EMBL:RKT55814.1, ECO:0000313|Proteomes:UP000282084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43800 {ECO:0000313|EMBL:RKT55814.1,
RC   ECO:0000313|Proteomes:UP000282084};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-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:RKT55814.1}.
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DR   EMBL; RBXO01000001; RKT55814.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495W395; -.
DR   OrthoDB; 3987021at2; -.
DR   Proteomes; UP000282084; 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; cd08231; MDR_TM0436_like; 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; PTHR43401; L-THREONINE 3-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.
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:UP000282084};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          41..154
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          204..337
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   380 AA;  39316 MW;  3ACBC126BC8096E2 CRC64;
     MRPTVPRPTA THPAVTRAAV LRDFNAPLEL TEVPLPRELP PGSAIVRITS TTLCGTDAHL
     WRGVLPFVRT PIILGHEMAG EVVALGALSG RDAFGKPVEI GSRVVWSESV CGHCQGCTVL
     REPVLCDHRG YGFGQRADRW PFAIGGLSEY AYLPPGADRI VLDPEMPDTW AAAAGCAVKT
     VVRAFANAGG VEPGSTVAVQ GSGPLGLVAT AMARAAGAGR VITLGGPPNR LALAAKYGAD
     ATIDVTDVTD PDERVAQVEE LTGARGADLV LDFAGAPTAN REGVLMCGKR GTHVVVGLAG
     PQAAPVPMDV VMGREITVVG SLNGDVGDLA RALRFLSAFA GRFEWDALFS PPVGLAGAEQ
     AIRDMASMAA VKAVVDPGLD
//