ECOLI:SDHD

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	dsdA
Protein Name(s)	D-serine dehydratase D-serine deaminase DSD
External Links
UniProt	P00926
EMBL	J01603 U00096 AP009048 X86379
PIR	C65010
RefSeq	NP_416867.1 YP_490608.1
PDB	3SS7 3SS9
PDBsum	3SS7 3SS9
ProteinModelPortal	P00926
SMR	P00926
IntAct	P00926
STRING	511145.b2366
PaxDb	P00926
PRIDE	P00926
EnsemblBacteria	AAC75425 BAA16229
GeneID	12931561 946837
KEGG	ecj:Y75_p2333 eco:b2366
PATRIC	32120111
EchoBASE	EB0245
EcoGene	EG10249
eggNOG	COG3048
HOGENOM	HOG000218072
InParanoid	P00926
KO	K01753
OMA	QDFGIDN
OrthoDB	EOG6HXJ23
PhylomeDB	P00926
BioCyc	EcoCyc:DSERDEAM-MONOMER ECOL316407:JW2363-MONOMER MetaCyc:DSERDEAM-MONOMER
BRENDA	4.3.1.18
PRO	PR:P00926
Proteomes	UP000000318 UP000000625
Genevestigator	P00926
GO	GO:0005737 GO:0008721 GO:0016836 GO:0030170 GO:0006974 GO:0036088 GO:0070178 GO:0051410
HAMAP	MF_01030
InterPro	IPR011780 IPR000634 IPR001926
PANTHER	PTHR10314:SF9
Pfam	PF00291
SUPFAM	SSF53686
TIGRFAMs	TIGR02035
PROSITE	PS00165

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0008721	D-serine ammonia-lyase activity	PMID:5327100^[1]	ECO:0000314			F	D-serine ammonia-lyase (DsdA) catalyzes the deamination of D-serine to form pyruvate and ammonia.This is shown in Figure 7 and 8 because it shows the formation of pyruvate from the deamination of D-serine.	complete CACAO 4807
enables	GO:0008721	D-serine ammonia-lyase activity	PMID:5327100^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0036088	D-serine catabolic process	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10249 PANTHER:PTN000034699	P	Seeded From UniProt	complete
enables	GO:0008721	D-serine ammonia-lyase activity	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10249 PANTHER:PTN000034699 UniProtKB:Q9HYN9	F	Seeded From UniProt	complete
involved_in	GO:0006567	threonine catabolic process	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10990 PANTHER:PTN000034171 SGD:S000000569	P	Seeded From UniProt	complete
involved_in	GO:0006565	L-serine catabolic process	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10990 PANTHER:PTN000034171 SGD:S000000569 UniProtKB:P20132	P	Seeded From UniProt	complete
enables	GO:0004794	L-threonine ammonia-lyase activity	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10990 PANTHER:PTN000034171 SGD:S000000569	F	Seeded From UniProt	complete
enables	GO:0003941	L-serine ammonia-lyase activity	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10990 PANTHER:PTN000034171 SGD:S000000569 UniProtKB:P20132	F	Seeded From UniProt	complete
involved_in	GO:0070178	D-serine metabolic process	PMID:5327100^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0030170	pyridoxal phosphate binding	PMID:789365^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016836	hydro-lyase activity	PMID:4917239^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008721	D-serine ammonia-lyase activity	PMID:5327100^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:11967071^[5]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:4917239^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0051410	detoxification of nitrogen compound	PMID:14216615^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0036088	D-serine catabolic process	PMID:14216615^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0036088	D-serine catabolic process	PMID:5327100^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0030170	pyridoxal phosphate binding	PMID:5327101^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0030170	pyridoxal phosphate binding	PMID:5327100^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008721	D-serine ammonia-lyase activity	PMID:5327101^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0006520	cellular amino acid metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000634	P	Seeded From UniProt	complete
enables	GO:0008721	D-serine ammonia-lyase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011780	F	Seeded From UniProt	complete
enables	GO:0030170	pyridoxal phosphate binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000634 InterPro:IPR011780	F	Seeded From UniProt	complete
involved_in	GO:0046416	D-amino acid metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011780	P	Seeded From UniProt	complete
enables	GO:0008721	D-serine ammonia-lyase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:4.3.1.18	F	Seeded From UniProt	complete
involved_in	GO:0046416	D-amino acid metabolic process	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000100519	P	Seeded From UniProt	complete
enables	GO:0016836	hydro-lyase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000100519	F	Seeded From UniProt	complete
enables	GO:0016829	lyase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0456	F	Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 Dupourque, D et al. (1966) Purification and properties of D-serine dehydrase from Escherichia coli. J. Biol. Chem. 241 1233-8 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Kazarinoff, MN & Snell, EE (1976) D-Serine dehydratase from Escherichia coli. Essential arginine residue at the pyridoxal 5'-phosphate binding site. J. Biol. Chem. 251 6179-82 PubMed GONUTS page
↑ ^4.0 ^4.1 Dowhan, W Jr & Snell, EE (1970) D-serine dehydratase from Escherichia coli. II. Analytical studies and subunit structure. J. Biol. Chem. 245 4618-28 PubMed GONUTS page
↑ Khil, PP & Camerini-Otero, RD (2002) Over 1000 genes are involved in the DNA damage response of Escherichia coli. Mol. Microbiol. 44 89-105 PubMed GONUTS page
↑ ^6.0 ^6.1 MCFALL, E (1964) GENETIC STRUCTURE OF THE D-SERINE DEAMINASE SYSTEM OF ESCHERICHIA COLI. J. Mol. Biol. 9 746-53 PubMed GONUTS page
↑ ^7.0 ^7.1 Labow, R & Robinson, WG (1966) Crystalline D-serine dehydrase. J. Biol. Chem. 241 1239-43 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:5327100-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 Dupourque, D et al. (1966) Purification and properties of D-serine dehydrase from Escherichia coli. J. Biol. Chem. 241 1233-8 PubMed GONUTS page

[PMID:21873635-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:789365-3] Kazarinoff, MN & Snell, EE (1976) D-Serine dehydratase from Escherichia coli. Essential arginine residue at the pyridoxal 5'-phosphate binding site. J. Biol. Chem. 251 6179-82 PubMed GONUTS page

[PMID:4917239-4] 4.0 ^4.1 Dowhan, W Jr & Snell, EE (1970) D-serine dehydratase from Escherichia coli. II. Analytical studies and subunit structure. J. Biol. Chem. 245 4618-28 PubMed GONUTS page

[PMID:11967071-5] Khil, PP & Camerini-Otero, RD (2002) Over 1000 genes are involved in the DNA damage response of Escherichia coli. Mol. Microbiol. 44 89-105 PubMed GONUTS page

[PMID:14216615-6] 6.0 ^6.1 MCFALL, E (1964) GENETIC STRUCTURE OF THE D-SERINE DEAMINASE SYSTEM OF ESCHERICHIA COLI. J. Mol. Biol. 9 746-53 PubMed GONUTS page

[PMID:5327101-7] 7.0 ^7.1 Labow, R & Robinson, WG (1966) Crystalline D-serine dehydrase. J. Biol. Chem. 241 1239-43 PubMed GONUTS page

[PMID:18304323-8] 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:SDHD

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