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Database: UniProt
Entry: C0W1X0_9ACTO
LinkDB: C0W1X0_9ACTO
Original site: C0W1X0_9ACTO 
ID   C0W1X0_9ACTO            Unreviewed;       342 AA.
AC   C0W1X0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=L-threonine 3-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00627};
DE            Short=TDH {ECO:0000256|HAMAP-Rule:MF_00627};
DE            EC=1.1.1.103 {ECO:0000256|HAMAP-Rule:MF_00627};
GN   Name=tdh {ECO:0000256|HAMAP-Rule:MF_00627,
GN   ECO:0000313|EMBL:EEH63486.1};
GN   ORFNames=HMPREF0044_1410 {ECO:0000313|EMBL:EEH63486.1};
OS   Gleimia coleocanis DSM 15436.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Gleimia.
OX   NCBI_TaxID=525245 {ECO:0000313|EMBL:EEH63486.1, ECO:0000313|Proteomes:UP000010301};
RN   [1] {ECO:0000313|EMBL:EEH63486.1, ECO:0000313|Proteomes:UP000010301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15436 {ECO:0000313|EMBL:EEH63486.1,
RC   ECO:0000313|Proteomes:UP000010301};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-
CC       amino-3-ketobutyrate. {ECO:0000256|HAMAP-Rule:MF_00627}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) +
CC         NADH; Xref=Rhea:RHEA:13161, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57926, ChEBI:CHEBI:57945, ChEBI:CHEBI:78948;
CC         EC=1.1.1.103; Evidence={ECO:0000256|HAMAP-Rule:MF_00627};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00627};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00627};
CC   -!- PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo-
CC       reductase pathway; glycine from L-threonine: step 1/2.
CC       {ECO:0000256|HAMAP-Rule:MF_00627}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00627}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00627}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00627}.
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:EEH63486.1}.
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DR   EMBL; ACFG01000034; EEH63486.1; -; Genomic_DNA.
DR   RefSeq; WP_006546268.1; NZ_DS999540.1.
DR   AlphaFoldDB; C0W1X0; -.
DR   STRING; 525245.HMPREF0044_1410; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_0_11; -.
DR   OrthoDB; 3567264at2; -.
DR   UniPathway; UPA00046; UER00505.
DR   Proteomes; UP000010301; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniPathway.
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   HAMAP; MF_00627; Thr_dehydrog; 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; IPR004627; L-Threonine_3-DHase.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00627};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00627};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00627};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00627}; Reference proteome {ECO:0000313|Proteomes:UP000010301};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00627}.
FT   DOMAIN          10..338
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   ACT_SITE        40
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT   ACT_SITE        43
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT   BINDING         175
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT   BINDING         195
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT   BINDING         200
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT   BINDING         262..264
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT   BINDING         286..287
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
FT   SITE            148
FT                   /note="Important for catalytic activity for the proton
FT                   relay mechanism but does not participate directly in the
FT                   coordination of zinc atom"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00627"
SQ   SEQUENCE   342 AA;  36542 MW;  0AF970EADA7B28E3 CRC64;
     MKALVKTRPG VGLELVDVPD PVLGPNEVLV KVTRTGICGT DVHIQKWDGW AQNTVQTPRI
     IGHEFAGTIE AMGELVTGLE IGQLVSGEGH YVCGRCRACL AGRREVCANT QGIGYHVDGA
     MSQYFVLPAA NVWVHPQDMS HDVASIFDPF GNAVHTALQF PCLAEDVLVT GAGPIGIMAA
     LVAQFQGARN VVLTDLSDER LELAQSLGIS QTVNVGNRAL KDVYGPLGLK EGFDVGLEMS
     GSPHALRSMI DHMVHGGRIA LLGTPVADVS IDLAKVIFNM LTLQGVTGRR IFETWYAASA
     LVASGLDLSG VITHRFHYTE FEEAFAVAGD GKSGKVVMNW ED
//
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