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Q07YJ9

- PDXA_SHEFN

UniProt

Q07YJ9 - PDXA_SHEFN

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Shewanella frigidimarina (strain NCIMB 400)
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

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 Co(2+).UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei134 – 1341SubstrateUniRule annotation
Binding sitei135 – 1351SubstrateUniRule annotation
Metal bindingi164 – 1641Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi209 – 2091Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi264 – 2641Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei272 – 2721SubstrateUniRule annotation
Binding sitei281 – 2811SubstrateUniRule annotation
Binding sitei290 – 2901SubstrateUniRule 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

BioCyciSFRI318167:GIXS-3192-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:Sfri_3078
OrganismiShewanella frigidimarina (strain NCIMB 400)
Taxonomic identifieri318167 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000000684: 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 – 3273274-hydroxythreonine-4-phosphate dehydrogenasePRO_1000128261Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi318167.Sfri_3078.

Structurei

3D structure databases

ProteinModelPortaliQ07YJ9.
SMRiQ07YJ9. Positions 2-322.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
KOiK00097.
OMAiEQNSAYV.
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.

Q07YJ9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTKRIAITPG EPASIGPDLV IKLAQQAWPV ELVVCADPNL LMTRAKMLGL
60 70 80 90 100
PLQLRPYQPS QPPKPQTAGT LTIAPFTLAE EVECGVLNEA NSAYVVETLR
110 120 130 140 150
YAGEKNMSNE FDAVVTGPVH KGIINQAGIP FSGHTEFFAL QANCADVVMM
160 170 180 190 200
LAAPGLQVAL MTTHIPLAYV AKAITRDRLH HIITILHREL VSKFGLGSPK
210 220 230 240 250
IYVCGLNPHA GEDGHLGREE IDTIIPALNE LREQGMDIVG PLPADTLFQP
260 270 280 290 300
KYLEQADVVL AMYHDQGLPV LKSLGFGKSV NITLGLPYIR TSVDHGTALE
310 320
LAGSGKADCG SFTCALNKAI ELASKSK
Length:327
Mass (Da):35,087
Last modified:October 31, 2006 - v1
Checksum:i262E2D02DC9A35B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000447 Genomic DNA. Translation: ABI72915.1.
RefSeqiWP_011638521.1. NC_008345.1.
YP_751754.1. NC_008345.1.

Genome annotation databases

EnsemblBacteriaiABI72915; ABI72915; Sfri_3078.
GeneIDi4279981.
KEGGisfr:Sfri_3078.
PATRICi23500301. VBISheFri14343_3191.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000447 Genomic DNA. Translation: ABI72915.1 .
RefSeqi WP_011638521.1. NC_008345.1.
YP_751754.1. NC_008345.1.

3D structure databases

ProteinModelPortali Q07YJ9.
SMRi Q07YJ9. Positions 2-322.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 318167.Sfri_3078.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABI72915 ; ABI72915 ; Sfri_3078 .
GeneIDi 4279981.
KEGGi sfr:Sfri_3078.
PATRICi 23500301. VBISheFri14343_3191.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci SFRI318167:GIXS-3192-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: NCIMB 400.

Entry informationi

Entry nameiPDXA_SHEFN
AccessioniPrimary (citable) accession number: Q07YJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 31, 2006
Last modified: November 26, 2014
This is version 59 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