ID A0A0T6ANF5_9BACT Unreviewed; 373 AA.
AC A0A0T6ANF5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=L-threonine 3-dehydrogenase, threonine 3-dehydrogenase {ECO:0000313|EMBL:KRT76641.1};
DE EC=1.1.1.103 {ECO:0000313|EMBL:KRT76641.1};
GN ORFNames=XU14_C0036G0014 {ECO:0000313|EMBL:KRT76641.1};
OS Armatimonadetes bacterium CSP1-3.
OC Bacteria; Armatimonadota.
OX NCBI_TaxID=1640515 {ECO:0000313|EMBL:KRT76641.1, ECO:0000313|Proteomes:UP000051026};
RN [1] {ECO:0000313|EMBL:KRT76641.1, ECO:0000313|Proteomes:UP000051026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-3 {ECO:0000313|EMBL:KRT76641.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) 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|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:KRT76641.1}.
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DR EMBL; LDXQ01000036; KRT76641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6ANF5; -.
DR PATRIC; fig|1640515.3.peg.1489; -.
DR Proteomes; UP000051026; 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:KRT76641.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 33..363
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 373 AA; 39799 MW; BDFF392E22521B00 CRC64;
MVARPPAPHP APLRDRTPAV PTEMHALVKP APGPGLFLAT VPVPALRAGE ILVQVQAGGI
CGTDLHIYNW NEWAASRIHP PRIIGHEFCG TVVDVAPDVT EVRVGDFVAG EGHVACGECP
PCRRGDRHIC DRLEIIGIDR DGAFADYVAM PARNAWRLDR ASVPVEVAAV MDPLGNAVHT
ALATDPAGKR VAVIGCGPIG LMAVPVLRLS GAAFVAASDV RPERRALAER VGADLVLDGS
VDDVPARLRE ATGGQGVDVV LEMSGHPAGI RDGLRALRSG GWMSLLGLPS RPVEIDLTND
IIFKMVHLQG VFGRRMWQTW EQATSLLRRG LDIRPIITHR LPLERFAEAF ALLRAGSAGK
VILLLAARGE AKS
//