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Protein

L-serine dehydratase 1

Gene

sdaA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Deaminates also threonine, particularly when it is present in high concentration.

Catalytic activityi

L-serine = pyruvate + NH3.

Cofactori

[4Fe-4S] clusterCuratedNote: Binds 1 [4Fe-4S] cluster.Curated

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

GO - Molecular functioni

GO - Biological processi

  • gluconeogenesis Source: UniProtKB-UniPathway
  • L-serine catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Gluconeogenesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:LSERINEDEAM1-MONOMER.
ECOL316407:JW1803-MONOMER.
MetaCyc:LSERINEDEAM1-MONOMER.
BRENDAi4.3.1.17. 2026.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
L-serine dehydratase 1 (EC:4.3.1.17)
Short name:
SDH 1
Alternative name(s):
L-serine deaminase 1
Short name:
L-SD1
Gene namesi
Name:sdaA
Ordered Locus Names:b1814, JW1803
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10930. sdaA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454L-serine dehydratase 1PRO_0000171903Add
BLAST

Post-translational modificationi

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.

Proteomic databases

EPDiP16095.
PaxDbiP16095.
PRIDEiP16095.

Expressioni

Inductioni

It is made aerobically and anaerobically, in minimal medium.

Interactioni

Protein-protein interaction databases

BioGridi4260949. 2 interactions.
IntActiP16095. 3 interactions.
STRINGi511145.b1814.

Structurei

3D structure databases

ProteinModelPortaliP16095.
SMRiP16095. Positions 2-451.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105EJQ. Bacteria.
COG1760. LUCA.
HOGENOMiHOG000036732.
InParanoidiP16095.
KOiK01752.
OMAiCQATTQQ.
OrthoDBiEOG64V2GZ.
PhylomeDBiP16095.

Family and domain databases

Gene3Di3.30.1330.90. 1 hit.
InterProiIPR029009. ASB_dom.
IPR004644. Fe-S_L-Ser_mono.
IPR005130. Ser_deHydtase-like_asu.
IPR005131. Ser_deHydtase_bsu.
[Graphical view]
PfamiPF03313. SDH_alpha. 1 hit.
PF03315. SDH_beta. 1 hit.
[Graphical view]
SUPFAMiSSF143548. SSF143548. 1 hit.
TIGRFAMsiTIGR00720. sda_mono. 1 hit.

Sequencei

Sequence statusi: Complete.

P16095-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISLFDMFKV GIGPSSSHTV GPMKAGKQFV DDLVEKGLLD SVTRVAVDVY
60 70 80 90 100
GSLSLTGKGH HTDIAIIMGL AGNEPATVDI DSIPGFIRDV EERERLLLAQ
110 120 130 140 150
GRHEVDFPRD NGMRFHNGNL PLHENGMQIH AYNGDEVVYS KTYYSIGGGF
160 170 180 190 200
IVDEEHFGQD AANEVSVPYP FKSATELLAY CNETGYSLSG LAMQNELALH
210 220 230 240 250
SKKEIDEYFA HVWQTMQACI DRGMNTEGVL PGPLRVPRRA SALRRMLVSS
260 270 280 290 300
DKLSNDPMNV IDWVNMFALA VNEENAAGGR VVTAPTNGAC GIVPAVLAYY
310 320 330 340 350
DHFIESVSPD IYTRYFMAAG AIGALYKMNA SISGAEVGCQ GEVGVACSMA
360 370 380 390 400
AAGLAELLGG SPEQVCVAAE IGMEHNLGLT CDPVAGQVQV PCIERNAIAS
410 420 430 440 450
VKAINAARMA LRRTSAPRVS LDKVIETMYE TGKDMNAKYR ETSRGGLAIK

VQCD
Length:454
Mass (Da):48,907
Last modified:April 1, 1993 - v3
Checksum:iB2CD530423E95BE1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28695 Genomic DNA. Translation: AAA63580.1.
U00096 Genomic DNA. Translation: AAC74884.1.
AP009048 Genomic DNA. Translation: BAA15621.1.
PIRiF64942. DWECL.
RefSeqiNP_416328.1. NC_000913.3.
WP_000624298.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74884; AAC74884; b1814.
BAA15621; BAA15621; BAA15621.
GeneIDi946331.
KEGGiecj:JW1803.
eco:b1814.
PATRICi32118947. VBIEscCol129921_1891.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28695 Genomic DNA. Translation: AAA63580.1.
U00096 Genomic DNA. Translation: AAC74884.1.
AP009048 Genomic DNA. Translation: BAA15621.1.
PIRiF64942. DWECL.
RefSeqiNP_416328.1. NC_000913.3.
WP_000624298.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP16095.
SMRiP16095. Positions 2-451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260949. 2 interactions.
IntActiP16095. 3 interactions.
STRINGi511145.b1814.

Proteomic databases

EPDiP16095.
PaxDbiP16095.
PRIDEiP16095.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74884; AAC74884; b1814.
BAA15621; BAA15621; BAA15621.
GeneIDi946331.
KEGGiecj:JW1803.
eco:b1814.
PATRICi32118947. VBIEscCol129921_1891.

Organism-specific databases

EchoBASEiEB0923.
EcoGeneiEG10930. sdaA.

Phylogenomic databases

eggNOGiENOG4105EJQ. Bacteria.
COG1760. LUCA.
HOGENOMiHOG000036732.
InParanoidiP16095.
KOiK01752.
OMAiCQATTQQ.
OrthoDBiEOG64V2GZ.
PhylomeDBiP16095.

Enzyme and pathway databases

UniPathwayiUPA00138.
BioCyciEcoCyc:LSERINEDEAM1-MONOMER.
ECOL316407:JW1803-MONOMER.
MetaCyc:LSERINEDEAM1-MONOMER.
BRENDAi4.3.1.17. 2026.

Miscellaneous databases

PROiP16095.

Family and domain databases

Gene3Di3.30.1330.90. 1 hit.
InterProiIPR029009. ASB_dom.
IPR004644. Fe-S_L-Ser_mono.
IPR005130. Ser_deHydtase-like_asu.
IPR005131. Ser_deHydtase_bsu.
[Graphical view]
PfamiPF03313. SDH_alpha. 1 hit.
PF03315. SDH_beta. 1 hit.
[Graphical view]
SUPFAMiSSF143548. SSF143548. 1 hit.
TIGRFAMsiTIGR00720. sda_mono. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. 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.

Entry informationi

Entry nameiSDHL_ECOLI
AccessioniPrimary (citable) accession number: P16095
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1993
Last modified: March 16, 2016
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.