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Protein

NAD-dependent L-serine dehydrogenase

Gene

PA0743

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

NAD-dependent L-serine dehydrogenase that catalyzes the oxidation of L-serine and methyl-L-serine and is possibly involved in serine catabolism. Has low activity toward beta-hydroxyisobutyrate.1 Publication

Catalytic activityi

L-serine + NAD+ = 2-aminoacetaldehyde + CO2 + NADH.1 Publication

Kineticsi

kcat is 10.4 sec(-1) with L-serine as substrate. kcat is 9.6 sec(-1) with methyl-DL-serine as substrate. kcat is 5.8 sec(-1) with DL-glycerate as substrate. kcat is 11.6 sec(-1) with methyl-2,2-dimethyl-3-hydroxypropionate as substrate. kcat is 1.6 sec(-1) with NAD as substrate.

  1. KM=2.5 mM for L-serine1 Publication
  2. KM=2.4 mM for methyl-DL-serine1 Publication
  3. KM=19.8 mM for DL-glycerate1 Publication
  4. KM=17.4 mM for methyl-2,2-dimethyl-3-hydroxypropionate1 Publication
  5. KM=3.4 mM for NAD1 Publication
  1. Vmax=18.7 µmol/min/mg enzyme with L-serine as substrate1 Publication
  2. Vmax=17.2 µmol/min/mg enzyme with methyl-DL-serine as substrate1 Publication
  3. Vmax=10.4 µmol/min/mg enzyme with DL-glycerate as substrate1 Publication
  4. Vmax=20.9 µmol/min/mg enzyme with methyl-2,2-dimethyl-3-hydroxypropionate as substrate1 Publication
  5. Vmax=2.8 µmol/min/mg enzyme with NAD as substrate1 Publication

Pathwayi: Amino-acid degradation

This protein is involved in Amino-acid degradation.
View all proteins of this organism that are known to be involved in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei66NAD; via carbonyl oxygen1 Publication1
Binding sitei96NAD; via amide nitrogen1 Publication1
Active sitei1711 Publication1
Binding sitei246NAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi2 – 31NAD1 PublicationAdd BLAST30
Nucleotide bindingi65 – 66NADBy similarity2

GO - Molecular functioni

GO - Biological processi

  • branched-chain amino acid catabolic process Source: UniProtKB-KW
  • L-serine catabolic process Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Branched-chain amino acid catabolism

Keywords - Ligandi

NAD, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
NAD-dependent L-serine dehydrogenase (EC:1.1.1.3871 Publication)
Alternative name(s):
L-serine 3-dehydrogenase (NAD(+))
Gene namesi
Ordered Locus Names:PA0743
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA0743.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi96T → A: Almost abolished activity. 1 Publication1
Mutagenesisi122S → A: Strongly reduced activity. 1 Publication1
Mutagenesisi171K → A: Strongly reduced activity. 1
Mutagenesisi175N → A: Strongly reduced activity. 1 Publication1
Mutagenesisi214W → A: Almost abolished activity. 1 Publication1
Mutagenesisi219Y → A: Strongly reduced activity. 1 Publication1
Mutagenesisi246K → A: Almost abolished activity. 1 Publication1
Mutagenesisi247D → A: Almost abolished activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004291321 – 298NAD-dependent L-serine dehydrogenaseAdd BLAST298

Proteomic databases

PaxDbiQ9I5I6.

Interactioni

Subunit structurei

Homotetramer, dimer of dimers.1 Publication

Protein-protein interaction databases

STRINGi208964.PA0743.

Structurei

Secondary structure

1298
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Helixi13 – 22Combined sources10
Beta strandi26 – 30Combined sources5
Helixi34 – 42Combined sources9
Helixi51 – 55Combined sources5
Beta strandi59 – 63Combined sources5
Helixi68 – 76Combined sources9
Beta strandi77 – 81Combined sources5
Beta strandi90 – 93Combined sources4
Helixi99 – 110Combined sources12
Turni111 – 113Combined sources3
Beta strandi115 – 118Combined sources4
Beta strandi121 – 123Combined sources3
Helixi125 – 130Combined sources6
Beta strandi133 – 139Combined sources7
Helixi141 – 154Combined sources14
Beta strandi155 – 163Combined sources9
Helixi166 – 194Combined sources29
Helixi199 – 207Combined sources9
Helixi214 – 218Combined sources5
Turni223 – 225Combined sources3
Helixi230 – 233Combined sources4
Beta strandi237 – 240Combined sources4
Helixi241 – 258Combined sources18
Helixi263 – 277Combined sources15
Helixi285 – 288Combined sources4
Helixi289 – 292Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OBBX-ray2.20A1-298[»]
3Q3CX-ray2.30A1-298[»]
ProteinModelPortaliQ9I5I6.
SMRiQ9I5I6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9I5I6.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CF3. Bacteria.
COG2084. LUCA.
HOGENOMiHOG000219610.
InParanoidiQ9I5I6.
KOiK19711.
OMAiNIVHCGE.
PhylomeDBiQ9I5I6.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR002204. 3-OH-isobutyrate_DH-rel_CS.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006115. 6PGDH_NADP-bd.
IPR011548. HIBADH.
IPR015815. HIBADH-related.
IPR016040. NAD(P)-bd_dom.
IPR029154. NADP-bd.
[Graphical view]
PfamiPF14833. NAD_binding_11. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000103. HIBADH. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01692. HIBADH. 1 hit.
PROSITEiPS00895. 3_HYDROXYISOBUT_DH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9I5I6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQIAFIGLG HMGAPMATNL LKAGYLLNVF DLVQSAVDGL VAAGASAARS
60 70 80 90 100
ARDAVQGADV VISMLPASQH VEGLYLDDDG LLAHIAPGTL VLECSTIAPT
110 120 130 140 150
SARKIHAAAR ERGLAMLDAP VSGGTAGAAA GTLTFMVGGD AEALEKARPL
160 170 180 190 200
FEAMGRNIFH AGPDGAGQVA KVCNNQLLAV LMIGTAEAMA LGVANGLEAK
210 220 230 240 250
VLAEIMRRSS GGNWALEVYN PWPGVMENAP ASRDYSGGFM AQLMAKDLGL
260 270 280 290
AQEAAQASAS STPMGSLALS LYRLLLKQGY AERDFSVVQK LFDPTQGQ
Length:298
Mass (Da):30,754
Last modified:March 1, 2001 - v1
Checksum:i27100627BEBB469C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG04132.1.
PIRiB83553.
RefSeqiNP_249434.1. NC_002516.2.
WP_003114168.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG04132; AAG04132; PA0743.
GeneIDi882135.
KEGGipae:PA0743.
PATRICi19835758. VBIPseAer58763_0772.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG04132.1.
PIRiB83553.
RefSeqiNP_249434.1. NC_002516.2.
WP_003114168.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OBBX-ray2.20A1-298[»]
3Q3CX-ray2.30A1-298[»]
ProteinModelPortaliQ9I5I6.
SMRiQ9I5I6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA0743.

Proteomic databases

PaxDbiQ9I5I6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG04132; AAG04132; PA0743.
GeneIDi882135.
KEGGipae:PA0743.
PATRICi19835758. VBIPseAer58763_0772.

Organism-specific databases

PseudoCAPiPA0743.

Phylogenomic databases

eggNOGiENOG4105CF3. Bacteria.
COG2084. LUCA.
HOGENOMiHOG000219610.
InParanoidiQ9I5I6.
KOiK19711.
OMAiNIVHCGE.
PhylomeDBiQ9I5I6.

Miscellaneous databases

EvolutionaryTraceiQ9I5I6.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR002204. 3-OH-isobutyrate_DH-rel_CS.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006115. 6PGDH_NADP-bd.
IPR011548. HIBADH.
IPR015815. HIBADH-related.
IPR016040. NAD(P)-bd_dom.
IPR029154. NADP-bd.
[Graphical view]
PfamiPF14833. NAD_binding_11. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000103. HIBADH. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01692. HIBADH. 1 hit.
PROSITEiPS00895. 3_HYDROXYISOBUT_DH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSERDH_PSEAE
AccessioniPrimary (citable) accession number: Q9I5I6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 14, 2014
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.