ECOLI:TDH

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	tdh
Protein Name(s)	L-threonine 3-dehydrogenase
External Links
UniProt	P07913
EMBL	X06690 U00039 U00096 AP009048
PIR	A33276
RefSeq	NP_418073.1 YP_491817.1
ProteinModelPortal	P07913
SMR	P07913
DIP	DIP-6855N
IntAct	P07913
STRING	511145.b3616
PaxDb	P07913
PRIDE	P07913
EnsemblBacteria	AAC76640 BAE77676
GeneID	12934313 948139
KEGG	ecj:Y75_p3558 eco:b3616
PATRIC	32122719
EchoBASE	EB0986
EcoGene	EG10993
eggNOG	COG1063
HOGENOM	HOG000294686
InParanoid	P07913
KO	K00060
OMA	ITGHEMA
OrthoDB	EOG60PH85
PhylomeDB	P07913
BioCyc	EcoCyc:THREODEHYD-MONOMER ECOL316407:JW3591-MONOMER MetaCyc:THREODEHYD-MONOMER
SABIO-RK	P07913
UniPathway	UPA00046
PRO	PR:P07913
Proteomes	UP000000318 UP000000625
Genevestigator	P07913
GO	GO:0005737 GO:0005829 GO:0046870 GO:0008198 GO:0008743 GO:0030145 GO:0016491 GO:0008270 GO:0006564 GO:0019518 GO:0006567
Gene3D	3.40.50.720 3.90.180.10
HAMAP	MF_00627
InterPro	IPR013149 IPR013154 IPR002085 IPR002328 IPR011032 IPR004627 IPR016040
PANTHER	PTHR11695
Pfam	PF08240 PF00107
SUPFAM	SSF50129
TIGRFAMs	TIGR00692
PROSITE	PS00059

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
part_of	GO:0005829	cytosol	PMID:16858726^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0046870	cadmium ion binding	PMID:3056527^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	PMID:6780553^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	PMID:3518793^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	PMID:6780553^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008743	L-threonine 3-dehydrogenase activity	PMID:6780553^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:2007567^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006564	L-serine biosynthetic process	PMID:3108237^[6]	ECO:0000316	genetic interaction evidence used in manual assertion	EcoliWiki:serB	P	Seeded From UniProt	complete
involved_in	GO:0006564	L-serine biosynthetic process	PMID:3108237^[6]	ECO:0000316	genetic interaction evidence used in manual assertion	EcoliWiki:serA	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:6780553^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0008743	L-threonine 3-dehydrogenase activity	PMID:22411989^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008198	ferrous iron binding	PMID:22411989^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006567	threonine catabolic process	PMID:8519804^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0006567	threonine catabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004627	P	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002328 InterPro:IPR004627	F	Seeded From UniProt	complete
enables	GO:0008743	L-threonine 3-dehydrogenase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004627	F	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002328 InterPro:IPR020843	F	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002328 InterPro:IPR004627 InterPro:IPR013149 InterPro:IPR013154	P	Seeded From UniProt	complete
enables	GO:0008743	L-threonine 3-dehydrogenase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.1.1.103	F	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000333474	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000333474	C	Seeded From UniProt	complete
enables	GO:0008743	L-threonine 3-dehydrogenase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000333474	F	Seeded From UniProt	complete
involved_in	GO:0006567	threonine catabolic process	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000333474	P	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	P	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
involved_in	GO:0019518	L-threonine catabolic process to glycine	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00046	P	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
↑ Craig, PA & Dekker, EE (1988) Cd2+ activation of L-threonine dehydrogenase from Escherichia coli K-12. Biochim. Biophys. Acta 957 222-9 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Boylan, SA & Dekker, EE (1981) L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12. J. Biol. Chem. 256 1809-15 PubMed GONUTS page
↑ Craig, PA & Dekker, EE (1986) L-threonine dehydrogenase from Escherichia coli K-12: thiol-dependent activation by Mn2+. Biochemistry 25 1870-6 PubMed GONUTS page
↑ Epperly, BR & Dekker, EE (1991) L-threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies. J. Biol. Chem. 266 6086-92 PubMed GONUTS page
↑ ^6.0 ^6.1 Ravnikar, PD & Somerville, RL (1987) Genetic characterization of a highly efficient alternate pathway of serine biosynthesis in Escherichia coli. J. Bacteriol. 169 2611-7 PubMed GONUTS page
↑ ^7.0 ^7.1 Anjem, A & Imlay, JA (2012) Mononuclear iron enzymes are primary targets of hydrogen peroxide stress. J. Biol. Chem. 287 15544-56 PubMed GONUTS page
↑ Chen, YW et al. (1995) Functional analysis of E. coli threonine dehydrogenase by means of mutant isolation and characterization. Biochim. Biophys. Acta 1253 208-14 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:16858726-1] Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page

[PMID:3056527-2] Craig, PA & Dekker, EE (1988) Cd2+ activation of L-threonine dehydrogenase from Escherichia coli K-12. Biochim. Biophys. Acta 957 222-9 PubMed GONUTS page

[PMID:6780553-3] 3.0 ^3.1 ^3.2 ^3.3 Boylan, SA & Dekker, EE (1981) L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12. J. Biol. Chem. 256 1809-15 PubMed GONUTS page

[PMID:3518793-4] Craig, PA & Dekker, EE (1986) L-threonine dehydrogenase from Escherichia coli K-12: thiol-dependent activation by Mn2+. Biochemistry 25 1870-6 PubMed GONUTS page

[PMID:2007567-5] Epperly, BR & Dekker, EE (1991) L-threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies. J. Biol. Chem. 266 6086-92 PubMed GONUTS page

[PMID:3108237-6] 6.0 ^6.1 Ravnikar, PD & Somerville, RL (1987) Genetic characterization of a highly efficient alternate pathway of serine biosynthesis in Escherichia coli. J. Bacteriol. 169 2611-7 PubMed GONUTS page

[PMID:22411989-7] 7.0 ^7.1 Anjem, A & Imlay, JA (2012) Mononuclear iron enzymes are primary targets of hydrogen peroxide stress. J. Biol. Chem. 287 15544-56 PubMed GONUTS page

[PMID:8519804-8] Chen, YW et al. (1995) Functional analysis of E. coli threonine dehydrogenase by means of mutant isolation and characterization. Biochim. Biophys. Acta 1253 208-14 PubMed GONUTS page

[PMID:18304323-9] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

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ECOLI:TDH

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