ID A0A061SSY3_9RHOB Unreviewed; 346 AA.
AC A0A061SSY3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=L-threonine 3-dehydrogenase {ECO:0000313|EMBL:KAJ04007.1};
DE EC=1.1.1.103 {ECO:0000313|EMBL:KAJ04007.1};
GN Name=tdh {ECO:0000313|EMBL:KAJ04007.1};
GN ORFNames=PM02_06770 {ECO:0000313|EMBL:KAJ04007.1};
OS Sulfitobacter mediterraneus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=83219 {ECO:0000313|EMBL:KAJ04007.1, ECO:0000313|Proteomes:UP000027337};
RN [1] {ECO:0000313|EMBL:KAJ04007.1, ECO:0000313|Proteomes:UP000027337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1FIGIMAR09 {ECO:0000313|EMBL:KAJ04007.1,
RC ECO:0000313|Proteomes:UP000027337};
RX PubMed=24855294;
RA Mas-Llado M., Pina-Villalonga J.M., Brunet-Galmes I., Nogales B., Bosch R.;
RT "Draft Genome Sequences of Two Isolates of the Roseobacter Group,
RT Sulfitobacter sp. Strains 3SOLIMAR09 and 1FIGIMAR09, from Harbors of
RT Mallorca Island (Mediterranean Sea).";
RL Genome Announc. 2:e00350-14(2014).
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|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:KAJ04007.1}.
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DR EMBL; JEMU01000004; KAJ04007.1; -; Genomic_DNA.
DR RefSeq; WP_037906513.1; NZ_JEMU01000004.1.
DR AlphaFoldDB; A0A061SSY3; -.
DR STRING; 83219.PM02_06770; -.
DR eggNOG; COG1063; Bacteria.
DR Proteomes; UP000027337; Unassembled WGS sequence.
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 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 ECO:0000313|EMBL:KAJ04007.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027337};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 17..343
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 346 AA; 37659 MW; 5087A0B43735B3D4 CRC64;
MTTNEMKALS KLHAREGLWM THAPVPEIGP DDVLIRINKT GICGTDIHIW NWDEWAEKTV
PVPMITGHEF AGEIVELGRN VEGLEIGQRC SGEGHLIGKN SRQSRAGKFH LDPATRGIGV
NEQGAFAQYL RLPAFNVVPL PDEISDDIGA ILDPLGNAVH TALSFDLVGE DVLITGAGPI
GIMAAAVARH VGARHVVITD INEDRLALAQ KVTDVVPVNV AKDDLRDVIP RLKMKQGFDV
GLEMSGNQVA LDQMIEAMTM GGRIAMLGIP PGKSPVDWSR IVFKAITIKG VYGREIFETW
YKMIAMLENG LDISAIITHR FGVDDFEKGF AAMKSGQSGK VVLDWT
//
