Skip Header

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

C0QTA7

- PDXA_PERMH

UniProt

C0QTA7 - PDXA_PERMH

(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

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Persephonella marina (strain DSM 14350 / EX-H1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the NAD(P)-dependent oxidation of 4-(phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphohydroxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).UniRule annotation

Catalytic activityi

4-phosphonooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH.

Cofactori

Binds 1 divalent metal cation per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei129 – 1291SubstrateUniRule annotation
Binding sitei130 – 1301SubstrateUniRule annotation
Metal bindingi159 – 1591Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi204 – 2041Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi257 – 2571Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei265 – 2651SubstrateUniRule annotation
Binding sitei274 – 2741SubstrateUniRule annotation
Binding sitei283 – 2831SubstrateUniRule annotation

GO - Molecular functioni

  1. 4-hydroxythreonine-4-phosphate dehydrogenase activity Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-HAMAP
  3. NAD binding Source: InterPro

GO - Biological processi

  1. pyridoxal phosphate biosynthetic process Source: UniProtKB-HAMAP
  2. pyridoxine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridoxine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, NADP

Enzyme and pathway databases

BioCyciPMAR123214:GIZP-124-MONOMER.
UniPathwayiUPA00244; UER00312.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotation (EC:1.1.1.262UniRule annotation)
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenaseUniRule annotation
Gene namesi
Name:pdxAUniRule annotation
Ordered Locus Names:PERMA_0123
OrganismiPersephonella marina (strain DSM 14350 / EX-H1)
Taxonomic identifieri123214 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesHydrogenothermaceaePersephonella
ProteomesiUP000001366: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3193194-hydroxythreonine-4-phosphate dehydrogenasePRO_1000146491Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi123214.PERMA_0123.

Structurei

3D structure databases

ProteinModelPortaliC0QTA7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221591.
KOiK00097.
OMAiAPINKHN.
OrthoDBiEOG6GN6ZC.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
HAMAPiMF_00536. PdxA.
InterProiIPR024084. IsoPropMal-DH-like_dom.
IPR005255. PdxA.
[Graphical view]
PfamiPF04166. PdxA. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00557. pdxA. 1 hit.

Sequencei

Sequence statusi: Complete.

C0QTA7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKIGITLGD PSGISPEILI KSIDKLKKAI YVIYGSYKII EKVSSILDKK
60 70 80 90 100
TEINIIDSPE EAEKEGVYLI NVYDRDFCVG KPDKETGKAS VLFLERAVKD
110 120 130 140 150
ILSKKLDAIV TLPISKEYVM KAGFRYAGHT DYLADITKTE DYLMMLLCEK
160 170 180 190 200
MKVALVTTHI PLKDVPENIK PEILESKIRL LNRELQSKFG IKKPKIAVLG
210 220 230 240 250
LNPHAGDGGN IGREEIDIIN PVVQKLKSEG IDLEGSLSAD TAFNRYREFD
260 270 280 290 300
AYLAMYHDQG LIPLKLLCFK KAVNITLGIP FIRTSPDHGT GFDIAGKGIA
310
DPSSFIEAVK LALKLSKQY
Length:319
Mass (Da):35,461
Last modified:May 5, 2009 - v1
Checksum:i547F5F5A236D08C2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001230 Genomic DNA. Translation: ACO03563.1.
RefSeqiYP_002729922.1. NC_012440.1.

Genome annotation databases

EnsemblBacteriaiACO03563; ACO03563; PERMA_0123.
GeneIDi7675488.
KEGGipmx:PERMA_0123.
PATRICi22913725. VBIPerMar119911_0182.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001230 Genomic DNA. Translation: ACO03563.1 .
RefSeqi YP_002729922.1. NC_012440.1.

3D structure databases

ProteinModelPortali C0QTA7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 123214.PERMA_0123.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACO03563 ; ACO03563 ; PERMA_0123 .
GeneIDi 7675488.
KEGGi pmx:PERMA_0123.
PATRICi 22913725. VBIPerMar119911_0182.

Phylogenomic databases

eggNOGi COG1995.
HOGENOMi HOG000221591.
KOi K00097.
OMAi APINKHN.
OrthoDBi EOG6GN6ZC.

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci PMAR123214:GIZP-124-MONOMER.

Family and domain databases

Gene3Di 3.40.718.10. 1 hit.
HAMAPi MF_00536. PdxA.
InterProi IPR024084. IsoPropMal-DH-like_dom.
IPR005255. PdxA.
[Graphical view ]
Pfami PF04166. PdxA. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00557. pdxA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 14350 / EX-H1.

Entry informationi

Entry nameiPDXA_PERMH
AccessioniPrimary (citable) accession number: C0QTA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 5, 2009
Last modified: October 29, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is located at the dimer interface.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