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Q12K60

- PDXA_SHEDO

UniProt

Q12K60 - PDXA_SHEDO

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
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

BioCyciSDEN318161:GHKQ-2996-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:Sden_2887
OrganismiShewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
Taxonomic identifieri318161 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000001982: 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 – 3283284-hydroxythreonine-4-phosphate dehydrogenasePRO_1000128260Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi318161.Sden_2887.

Structurei

3D structure databases

ProteinModelPortaliQ12K60.
SMRiQ12K60. 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.

Q12K60-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTKRIAITAG EPASIGPDLV ITLAQQAWPA ELVVCANPEL LLARAAKLGL
60 70 80 90 100
PLRLIPYHSE NKPQPQAAGT LTIAPFELAA EVECGVLNEL NSAYVVDTLR
110 120 130 140 150
FAGEKNMSRE FDAVVTGPVH KGIINQAGIA FSGHTEYFAV QANCQDVVMM
160 170 180 190 200
LAAPGLQVAL MTTHIPLAYV AKAITRERLH HIIHILHKEL KSKFGLGSPK
210 220 230 240 250
IYVCGLNPHA GEDGHIGREE LDVMIPALNE LRAQGIQLVG PLPADTLFQP
260 270 280 290 300
KYLQDADVIL AMYHDQGLPV LKSLGFGKSV NITLGLPYIR TSVDHGTALE
310 320
LAGTGLADSG SFTCALNKAI ELASKVSN
Length:328
Mass (Da):35,054
Last modified:August 22, 2006 - v1
Checksum:i6C050F2226CB0A02
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000302 Genomic DNA. Translation: ABE56166.1.
RefSeqiYP_563889.1. NC_007954.1.

Genome annotation databases

EnsemblBacteriaiABE56166; ABE56166; Sden_2887.
GeneIDi4019412.
KEGGisdn:Sden_2887.
PATRICi23491808. VBISheDen79529_3032.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000302 Genomic DNA. Translation: ABE56166.1 .
RefSeqi YP_563889.1. NC_007954.1.

3D structure databases

ProteinModelPortali Q12K60.
SMRi Q12K60. Positions 2-322.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 318161.Sden_2887.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABE56166 ; ABE56166 ; Sden_2887 .
GeneIDi 4019412.
KEGGi sdn:Sden_2887.
PATRICi 23491808. VBISheDen79529_3032.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci SDEN318161:GHKQ-2996-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: OS217 / ATCC BAA-1090 / DSM 15013.

Entry informationi

Entry nameiPDXA_SHEDO
AccessioniPrimary (citable) accession number: Q12K60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: August 22, 2006
Last modified: November 26, 2014
This is version 66 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