P16095 (SDHL_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-serine dehydratase 1
Short name=SDH 1
EC=4.3.1.17

Alternative name(s):
L-serine deaminase 1
Short name=L-SD1

Gene names

Name:	sdaA
Ordered Locus Names:	b1814, JW1803

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	454 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Deaminates also threonine, particularly when it is present in high concentration.
Catalytic activity	L-serine = pyruvate + NH3.
Cofactor	Binds 1 4Fe-4S cluster Probable.
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
Induction	It is made aerobically and anaerobically, in minimal medium.
Post-translational modification	Activated by post-translational modification by a system involving at least three gene products. Activation is mimicked in vitro by iron and dithiothreitol. There is considerable evidence for a free-radical activation mechanism.
Sequence similarities	Belongs to the iron-sulfur dependent L-serine dehydratase family.

Ontologies

Keywords
Biological process	Gluconeogenesis
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	L-serine catabolic process Inferred from direct assay PubMed 15155761. Source: EcoCyc gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW L-serine ammonia-lyase activity Inferred from direct assay PubMed 15155761. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 454	454	L-serine dehydratase 1		PRO_0000171903

Sequences

	Sequence		Length	Mass (Da)
	P16095 [UniParc]. Last modified April 1, 1993. Version 3. Checksum: B2CD530423E95BE1	FASTA	454	48,907
	10 20 30 40 50 60 MISLFDMFKV GIGPSSSHTV GPMKAGKQFV DDLVEKGLLD SVTRVAVDVY GSLSLTGKGH 70 80 90 100 110 120 HTDIAIIMGL AGNEPATVDI DSIPGFIRDV EERERLLLAQ GRHEVDFPRD NGMRFHNGNL 130 140 150 160 170 180 PLHENGMQIH AYNGDEVVYS KTYYSIGGGF IVDEEHFGQD AANEVSVPYP FKSATELLAY 190 200 210 220 230 240 CNETGYSLSG LAMQNELALH SKKEIDEYFA HVWQTMQACI DRGMNTEGVL PGPLRVPRRA 250 260 270 280 290 300 SALRRMLVSS DKLSNDPMNV IDWVNMFALA VNEENAAGGR VVTAPTNGAC GIVPAVLAYY 310 320 330 340 350 360 DHFIESVSPD IYTRYFMAAG AIGALYKMNA SISGAEVGCQ GEVGVACSMA AAGLAELLGG 370 380 390 400 410 420 SPEQVCVAAE IGMEHNLGLT CDPVAGQVQV PCIERNAIAS VKAINAARMA LRRTSAPRVS 430 440 450 LDKVIETMYE TGKDMNAKYR ETSRGGLAIK VQCD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"L-serine degradation in Escherichia coli K-12: cloning and sequencing of the sdaA gene." Su H., Lang B.F., Newman E.B. J. Bacteriol. 171:5095-5102(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Use of gene fusions of the structural gene sdaA to purify L-serine deaminase 1 from Escherichia coli K-12." Su H., Moniakis J., Newman E.B. Eur. J. Biochem. 211:521-527(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, SEQUENCE REVISION, CHARACTERIZATION. Strain: K12.
[3]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M28695 Genomic DNA. Translation: AAA63580.1. U00096 Genomic DNA. Translation: AAC74884.1. AP009048 Genomic DNA. Translation: BAA15621.1.
PIR	DWECL. F64942.
RefSeq	NP_416328.1. NC_000913.2. YP_490075.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P16095.
SMR	P16095. Positions 16-157.
ModBase	Search...
Protein-protein interaction databases
IntAct	P16095. 3 interactions.
STRING	511145.b1814.
Proteomic databases
PaxDb	P16095.
PRIDE	P16095.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74884; AAC74884; b1814. BAA15621; BAA15621; BAA15621.
GeneID	12931955. 946331.
KEGG	ecj:Y75_p1789. eco:b1814.
PATRIC	32118947. VBIEscCol129921_1891.
Organism-specific databases
EchoBASE	EB0923.
EcoGene	EG10930. sdaA.
Phylogenomic databases
eggNOG	COG1760.
HOGENOM	HOG000036732.
KO	K01752.
OMA	GKEFIDD.
ProtClustDB	PRK15023.
Enzyme and pathway databases
BioCyc	EcoCyc:LSERINEDEAM1-MONOMER. ECOL316407:JW1803-MONOMER. MetaCyc:LSERINEDEAM1-MONOMER.
UniPathway	UPA00138.
Gene expression databases
Genevestigator	P16095.
Family and domain databases
InterPro	IPR004644. Fe-S_L-Ser_mono. IPR005130. Ser_deHydtase-like_asu. IPR005131. Ser_deHydtase_bsu. [Graphical view]
Pfam	PF03313. SDH_alpha. 1 hit. PF03315. SDH_beta. 1 hit. [Graphical view]
TIGRFAMs	TIGR00720. sda_mono. 1 hit.
ProtoNet	Search...

Entry information

Entry name

SDHL_ECOLI

Accession

Primary (citable) accession number: P16095

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1993
Last modified:	May 1, 2013
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program