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Protein

Putative L-aspartate dehydrogenase

Gene

aspdh

Organism
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.By similarity

Catalytic activityi

L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei127 – 1271NAD; via amide nitrogenBy similarity
Binding sitei194 – 1941NADBy similarity

GO - Molecular functioni

  1. aspartate dehydrogenase activity Source: UniProtKB-EC
  2. NADP binding Source: InterPro

GO - Biological processi

  1. NAD biosynthetic process Source: UniProtKB-UniPathway
  2. NADP catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

UniPathwayiUPA00253; UER00456.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative L-aspartate dehydrogenase (EC:1.4.1.21)
Alternative name(s):
Aspartate dehydrogenase domain-containing protein
Gene namesi
Name:aspdh
OrganismiXenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Taxonomic identifieri8364 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana
ProteomesiUP000008143: Unplaced

Organism-specific databases

XenbaseiXB-GENE-6454901. aspdh.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284Putative L-aspartate dehydrogenasePRO_0000144904Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ5FW48.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the L-aspartate dehydrogenase family.Curated

Phylogenomic databases

HOVERGENiHBG062283.
InParanoidiQ5FW48.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR011182. L-Asp_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFiPIRSF005227. Asp_dh_NAD_syn. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5FW48-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEERRMRIG VVGYGHIGKY LVDKIVREGA NHSMELAFVW NRRREKLSGA
60 70 80 90 100
VDPRLQLQDL SDCQKWAADL IVEVAHPCIT REYGEKFLSV AHFLVGSPTA
110 120 130 140 150
LADTVTEAKL RERARLSGNT LYVPCGALWG AEDIFKMAER GTLKALRITM
160 170 180 190 200
TKHPNSFKLE GDLVQKNQEA MSNRTVLYEG PVRGLCPLAP NNVNTMAAAC
210 220 230 240 250
MAAHTLGFDG VVGVLVSDPS VPDWHFVDIE VTGGTIEKTG QVFSVKTSRR
260 270 280
NPAAPCSVTG SATFASFWSS LLACKGHGGR VYIC
Length:284
Mass (Da):31,054
Last modified:March 1, 2005 - v1
Checksum:i790C024CBE196BCC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC089631 mRNA. Translation: AAH89631.1.
RefSeqiNP_001015700.1. NM_001015700.1.
UniGeneiStr.33092.

Genome annotation databases

GeneIDi548417.
KEGGixtr:548417.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC089631 mRNA. Translation: AAH89631.1.
RefSeqiNP_001015700.1. NM_001015700.1.
UniGeneiStr.33092.

3D structure databases

ProteinModelPortaliQ5FW48.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi548417.
KEGGixtr:548417.

Organism-specific databases

CTDi554235.
XenbaseiXB-GENE-6454901. aspdh.

Phylogenomic databases

HOVERGENiHBG062283.
InParanoidiQ5FW48.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00456.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR011182. L-Asp_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFiPIRSF005227. Asp_dh_NAD_syn. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. NIH - Xenopus Gene Collection (XGC) project
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.

Entry informationi

Entry nameiASPD_XENTR
AccessioniPrimary (citable) accession number: Q5FW48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: March 1, 2005
Last modified: January 7, 2015
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.