Skip Header

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

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)
Status
Reviewed-Annotation score: 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

Zn2+UniRule annotation, Mg2+UniRule annotation, Co2+UniRule annotationNote: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co2+.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei135 – 1351SubstrateUniRule annotation
Binding sitei136 – 1361SubstrateUniRule annotation
Metal bindingi165 – 1651Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi210 – 2101Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi265 – 2651Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei273 – 2731SubstrateUniRule annotation
Binding sitei282 – 2821SubstrateUniRule annotation
Binding sitei291 – 2911SubstrateUniRule 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

BioCyciSDEG203122:GI2M-743-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:Sde_0738
OrganismiSaccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)
Taxonomic identifieri203122 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeSaccharophagus
ProteomesiUP000001947: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3353354-hydroxythreonine-4-phosphate dehydrogenasePRO_1000051513Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi203122.Sde_0738.

Structurei

3D structure databases

ProteinModelPortaliQ21MS9.
SMRiQ21MS9. Positions 7-320.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
KOiK00097.
OMAiRAGQGCL.
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.

Q21MS9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSHPAIIALT PGEPAGIGPD LTVMAAQQAR DYPLVALCDP QLLKDRAKLL
60 70 80 90 100
GLPLTVSTYI QGSAVTTSAQ HISVMPIPLG APCEAGTLDS TNAAYVIETL
110 120 130 140 150
KQATEGCLSG EFAAVVTGPV QKSVINEAGI NFSGHTEYFA DNSNTPRVVM
160 170 180 190 200
MLATEGLRVA LATTHLPLKD VSAAITTASL TETLNILLAD LQLKFGLSQP
210 220 230 240 250
RVLVCGLNPH AGEGGHLGME EIDTIIPVLE QFRARGHNLV GPLPADTLFN
260 270 280 290 300
PKYLSDADAV LAMYHDQGLP VLKYKGFGNA VNITLGLPFI RTSVDHGTAL
310 320 330
DLAGTGKANI GSLQVALGYA QNLAMQQASI NEIAG
Length:335
Mass (Da):35,022
Last modified:April 18, 2006 - v1
Checksum:i2C97F33B5DF966A5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000282 Genomic DNA. Translation: ABD80000.1.
RefSeqiWP_011467221.1. NC_007912.1.
YP_526212.1. NC_007912.1.

Genome annotation databases

EnsemblBacteriaiABD80000; ABD80000; Sde_0738.
GeneIDi3966259.
KEGGisde:Sde_0738.
PATRICi23400225. VBISacDeg56404_0816.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000282 Genomic DNA. Translation: ABD80000.1.
RefSeqiWP_011467221.1. NC_007912.1.
YP_526212.1. NC_007912.1.

3D structure databases

ProteinModelPortaliQ21MS9.
SMRiQ21MS9. Positions 7-320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi203122.Sde_0738.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD80000; ABD80000; Sde_0738.
GeneIDi3966259.
KEGGisde:Sde_0738.
PATRICi23400225. VBISacDeg56404_0816.

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
KOiK00097.
OMAiRAGQGCL.
OrthoDBiEOG6GN6ZC.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.
BioCyciSDEG203122:GI2M-743-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 2-40 / ATCC 43961 / DSM 17024.

Entry informationi

Entry nameiPDXA_SACD2
AccessioniPrimary (citable) accession number: Q21MS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 18, 2006
Last modified: February 4, 2015
This is version 63 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

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.