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Database: UniProt
Entry: A1T2D5_MYCVP
LinkDB: A1T2D5_MYCVP
Original site: A1T2D5_MYCVP 
ID   A1T2D5_MYCVP            Unreviewed;       341 AA.
AC   A1T2D5;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=L-threonine 3-dehydrogenase {ECO:0000313|EMBL:ABM11335.1};
DE            EC=1.1.1.103 {ECO:0000313|EMBL:ABM11335.1};
GN   OrderedLocusNames=Mvan_0490 {ECO:0000313|EMBL:ABM11335.1};
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM11335.1, ECO:0000313|Proteomes:UP000009159};
RN   [1] {ECO:0000313|EMBL:ABM11335.1, ECO:0000313|Proteomes:UP000009159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) 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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; CP000511; ABM11335.1; -; Genomic_DNA.
DR   RefSeq; WP_011767832.1; NZ_JACKSD010000393.1.
DR   AlphaFoldDB; A1T2D5; -.
DR   STRING; 350058.Mvan_0490; -.
DR   KEGG; mva:Mvan_0490; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_0_11; -.
DR   Proteomes; UP000009159; Chromosome.
DR   GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   CDD; cd08233; butanediol_DH_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   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43161:SF23; (R,R)-BUTANEDIOL DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR43161; SORBITOL 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   ECO:0000313|EMBL:ABM11335.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009159};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..339
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   341 AA;  35890 MW;  21324BE8DC4F9966 CRC64;
     MEAIVLNGTN DVGLTSVPDP APQDGEVIIE VAATGLCGTD LHEYVAGPTF SQPPVVLGHE
     VSGRIVEVGA GVDQSRIGQG AAVIPMDFCG SCHYCHRSLY HLCQRPGWIG FTRNGGLANY
     VAVPSRLAVR VPDVVDLEEA ALTEPTAVAF HAVRRAELLL GETVMVLGAG ALGLTVIQCA
     RAAGAARIFV TEPSGVRASL ARDLGATLVL DPHDPGTTAC ILEETRGVGV DVVFHVAGSA
     EAFTQGLDCL RKQGRFMEMS SWAGAASLDV NRHLLKEIQL RMVFGYDMFD DFPAVLALIA
     DGKLALAPQI TARVPLDRAV KEGLGGLLEG REGLVKVLVK P
//
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