Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A9A1F7

- ASPD_NITMS

UniProt

A9A1F7 - ASPD_NITMS

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Nitrosopumilus maritimus (strain SCM1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei125 – 1251NAD; via amide nitrogenUniRule annotation
Binding sitei192 – 1921NADUniRule annotation
Active sitei222 – 2221UniRule annotation

GO - Molecular functioni

  1. aspartate dehydrogenase activity Source: UniProtKB-EC
  2. NAD binding Source: UniProtKB-HAMAP
  3. NADP binding Source: UniProtKB-HAMAP
  4. oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor Source: UniProtKB-HAMAP

GO - Biological processi

  1. NAD biosynthetic process Source: UniProtKB-HAMAP
  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

BioCyciNMAR436308:GI3J-1273-MONOMER.
UniPathwayiUPA00253; UER00456.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable L-aspartate dehydrogenaseUniRule annotation (EC:1.4.1.21UniRule annotation)
Gene namesi
Name:nadXUniRule annotation
Ordered Locus Names:Nmar_1240
OrganismiNitrosopumilus maritimus (strain SCM1)
Taxonomic identifieri436308 [NCBI]
Taxonomic lineageiArchaeaThaumarchaeotaNitrosopumilalesNitrosopumilaceaeNitrosopumilus
ProteomesiUP000000792: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 272272Probable L-aspartate dehydrogenasePRO_1000140088Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi436308.Nmar_1240.

Structurei

3D structure databases

ProteinModelPortaliA9A1F7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the L-aspartate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1712.
HOGENOMiHOG000206326.
KOiK06989.
OMAiECAGHSA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01265. NadX.
InterProiIPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR022487. Asp_DH_arc.
IPR020626. Asp_DH_prok.
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.
TIGRFAMsiTIGR03855. NAD_NadX. 1 hit.

Sequencei

Sequence statusi: Complete.

A9A1F7 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKRIALLGCG SMGTQIALAI DSENFPATLT HVYDESKDAS FSLTQKLKNK
60 70 80 90 100
PEIVENSHLL SSQPIDIVVE AASQNAVKDV ALSVIQNKKD LMIMSVGALL
110 120 130 140 150
DESIYDILSD ACNDFKKTIY LPSGAIAGLD GLKSVKDELE SISITTTKHP
160 170 180 190 200
RSLKGAKFFE TSDINLDEIT SSTVVYKGTA KEAVTLFPAN INVAALLSLT
210 220 230 240 250
GIGSEKTSVT IVADPNTDKN THHIEASGKF GTMTFTIENV PDSNNPKTSR
260 270
LAILSAIETL KKYCSDDIQI GT
Length:272
Mass (Da):29,185
Last modified:January 15, 2008 - v1
Checksum:i66E9C99CAF4E57D9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000866 Genomic DNA. Translation: ABX13136.1.
RefSeqiYP_001582574.1. NC_010085.1.

Genome annotation databases

EnsemblBacteriaiABX13136; ABX13136; Nmar_1240.
GeneIDi5773947.
KEGGinmr:Nmar_1240.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000866 Genomic DNA. Translation: ABX13136.1 .
RefSeqi YP_001582574.1. NC_010085.1.

3D structure databases

ProteinModelPortali A9A1F7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 436308.Nmar_1240.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX13136 ; ABX13136 ; Nmar_1240 .
GeneIDi 5773947.
KEGGi nmr:Nmar_1240.

Phylogenomic databases

eggNOGi COG1712.
HOGENOMi HOG000206326.
KOi K06989.
OMAi ECAGHSA.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00456 .
BioCyci NMAR436308:GI3J-1273-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_01265. NadX.
InterProi IPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR022487. Asp_DH_arc.
IPR020626. Asp_DH_prok.
IPR011182. L-Asp_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view ]
PIRSFi PIRSF005227. Asp_dh_NAD_syn. 1 hit.
TIGRFAMsi TIGR03855. NAD_NadX. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SCM1.

Entry informationi

Entry nameiASPD_NITMS
AccessioniPrimary (citable) accession number: A9A1F7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 15, 2008
Last modified: October 1, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.UniRule annotation

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