ID   A0A151BP96_9ARCH        Unreviewed;       355 AA.
AC   A0A151BP96;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=L-threonine 3-dehydrogenase {ECO:0000313|EMBL:KYH41725.1};
GN   ORFNames=AYL32_003250 {ECO:0000313|EMBL:KYH41725.1};
OS   Candidatus Bathyarchaeota archaeon B26-2.
OC   Archaea; Candidatus Bathyarchaeota.
OX   NCBI_TaxID=1779371 {ECO:0000313|EMBL:KYH41725.1, ECO:0000313|Proteomes:UP000075437};
RN   [1] {ECO:0000313|EMBL:KYH41725.1, ECO:0000313|Proteomes:UP000075437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B26-2 {ECO:0000313|EMBL:KYH41725.1};
RA   He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., Wang F.;
RT   "Evidence for homoacetogenesis among multiple lineages of the archaeal
RT   phylum Bathyarchaeota widespread in marine sediments.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072, 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:KYH41725.1}.
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DR   EMBL; LUCE01000007; KYH41725.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151BP96; -.
DR   STRING; 1779371.AYL32_003250; -.
DR   PATRIC; fig|1779371.3.peg.596; -.
DR   Proteomes; UP000075437; Unassembled WGS sequence.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   GO; GO:0051262; P:protein tetramerization; IEA:UniProt.
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   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          12..351
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   355 AA;  38595 MW;  E5000ACCBB1C910F CRC64;
     MYAVVKGWRG PGAEIRSVET PKIGRDEVLV EVKALSICGT DVHIWNWDSW ARNRVKKIPL
     IFGHEFAGKV VEVGSDVTTV EVGDMVSAET HIVDGTCYQC RTDRMHVCRD MKILGVDTDG
     VFAEYVAVPK RNIWKNDPKL DPFLMALQEP LGNAVQTVLP KDHVEDVAGK NVAVLGCGPT
     GLMAIAILRE IGAAKVFATA GGLNKVRLEL AKKMGADLVL SAAEEGEKIV KTILDETDGN
     GVDVVLEMSG SPTALKQAFE ILTPGGRISL LGIFKGPVTL DVTNGIVFKA ATVYGITGRR
     MFQTWYQVRG LLSRPGFREK LASIITHKVP VRDIARGIDL LNNKEAAKVA LDPKW
//