Skip Header

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

A8G9P1

- PDXA_SERP5

UniProt

A8G9P1 - PDXA_SERP5

(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
Serratia proteamaculans (strain 568)
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. Can use ions such as zinc, magnesium or cobalt.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei136 – 1361SubstrateUniRule annotation
Binding sitei137 – 1371SubstrateUniRule annotation
Metal bindingi166 – 1661Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi211 – 2111Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi266 – 2661Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei274 – 2741SubstrateUniRule annotation
Binding sitei283 – 2831SubstrateUniRule annotation
Binding sitei292 – 2921SubstrateUniRule annotation

GO - Molecular functioni

  1. 4-hydroxythreonine-4-phosphate dehydrogenase activity Source: UniProtKB-HAMAP
  2. cobalt ion binding Source: UniProtKB-HAMAP
  3. magnesium ion binding Source: UniProtKB-HAMAP
  4. NAD binding Source: InterPro
  5. zinc ion binding Source: UniProtKB-HAMAP

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

Cobalt, Magnesium, Metal-binding, NAD, NADP, Zinc

Enzyme and pathway databases

BioCyciSPRO399741:GI55-753-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:Spro_0725
OrganismiSerratia proteamaculans (strain 568)
Taxonomic identifieri399741 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia
ProteomesiUP000007074: 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 – 3303304-hydroxythreonine-4-phosphate dehydrogenasePRO_1000061033Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi399741.Spro_0725.

Structurei

3D structure databases

ProteinModelPortaliA8G9P1.
SMRiA8G9P1. Positions 1-327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
KOiK00097.
OMAiDTLFQDK.
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.

A8G9P1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHNNNRIVIT PGEPAGVGPD LVAALAQQDW PVELVVCADP ALLLERARQL
60 70 80 90 100
DLPLQLRTYQ PQQPAQPQRA GTLTVLPVAT AHPVVAGELN VGNSAYVVET
110 120 130 140 150
LARACDGCLN GEFAALITGP VNKGVINDAG VPFIGHTEFF ADRSGCDRVV
160 170 180 190 200
MMLATEELRV ALATTHLPLL AVPGAITRQS LHEVIRILDH DLKTKFGLAQ
210 220 230 240 250
PQIYVCGLNP HAGEGGHMGR EEIDTIIPAL DELRAEGITL IGPLPADTLF
260 270 280 290 300
QPKYLQHADA VLAMYHDQGL PVLKYQGFGR AVNITLGLPF IRTSVDHGTA
310 320 330
LELAGTGTAD AGSFKTALNL AIKMIINCNE
Length:330
Mass (Da):35,205
Last modified:November 13, 2007 - v1
Checksum:i031CDA1113DF029D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000826 Genomic DNA. Translation: ABV39831.1.
RefSeqiWP_012005176.1. NC_009832.1.
YP_001476959.1. NC_009832.1.

Genome annotation databases

EnsemblBacteriaiABV39831; ABV39831; Spro_0725.
GeneIDi5605069.
KEGGispe:Spro_0725.
PATRICi32414090. VBISerPro44537_0752.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000826 Genomic DNA. Translation: ABV39831.1 .
RefSeqi WP_012005176.1. NC_009832.1.
YP_001476959.1. NC_009832.1.

3D structure databases

ProteinModelPortali A8G9P1.
SMRi A8G9P1. Positions 1-327.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 399741.Spro_0725.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABV39831 ; ABV39831 ; Spro_0725 .
GeneIDi 5605069.
KEGGi spe:Spro_0725.
PATRICi 32414090. VBISerPro44537_0752.

Phylogenomic databases

eggNOGi COG1995.
HOGENOMi HOG000221592.
KOi K00097.
OMAi DTLFQDK.
OrthoDBi EOG6GN6ZC.

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci SPRO399741:GI55-753-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: 568.

Entry informationi

Entry nameiPDXA_SERP5
AccessioniPrimary (citable) accession number: A8G9P1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: October 29, 2014
This is version 51 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