SubmitCancel

Skip Header

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

P58711

- PDXA_NOSS1

UniProt

P58711 - PDXA_NOSS1

(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, alr4755
Organism
Nostoc sp. (strain PCC 7120 / UTEX 2576)
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) By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 divalent metal cation per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei149 – 1491Substrate By similarity
Metal bindingi184 – 1841Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi229 – 2291Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi295 – 2951Divalent metal cation; shared with dimeric partner By similarity
Binding sitei303 – 3031Substrate By similarity
Binding sitei312 – 3121Substrate By similarity
Binding sitei321 – 3211Substrate By similarity

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

UniPathwayiUPA00244; UER00312.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxythreonine-4-phosphate dehydrogenase (EC:1.1.1.262)
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase
Gene namesi
Name:pdxA
Ordered Locus Names:alr4755
OrganismiNostoc sp. (strain PCC 7120 / UTEX 2576)
Taxonomic identifieri103690 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
ProteomesiUP000002483: Chromosome

Subcellular locationi

Cytoplasm By similarity 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 – 3623624-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotationPRO_0000188795Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi103690.alr4755.

Structurei

3D structure databases

ProteinModelPortaliP58711.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221591.
KOiK00097.
OMAiDTCWISA.
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.

P58711-1 [UniParc]FASTAAdd to Basket

« Hide

MYQLNQNQTV NTPQKYRPRL ALTVGDPGGI GAEVILKALA DLEIGHNYDL    50
TVVSNKNLLQ ETYKQLSSME NLLPLADPNL LKIIDVTVDR ETARQINLGT 100
GNAASGAASF AYMDYAIAQT LAGNFDGIVT GPIAKSAWKA AGYNYPGQTE 150
LLAQKSGVER FGMLFVARSP YTGWTLRALL ATTHIPLRQV ADTLTPQLLT 200
QKLDLLVECL EKDFGITSGR IAIAGLNPHS GEQGQLGTEE LDWLIPWLES 250
ERQKRPHFQL DGPIPPDTMW VKPGQAWYGN AIVQHPADAY LALYHDQGLI 300
PVKLMAFDRA VNTSIGLPFV RTSPDHGTAF DIAGQGIADA TSMKEAISLA 350
AELVCQRLHL EK 362
Length:362
Mass (Da):39,499
Last modified:January 31, 2002 - v1
Checksum:i111DC59550FCCD3E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000019 Genomic DNA. Translation: BAB76454.1.
PIRiAC2400.
RefSeqiNP_488795.1. NC_003272.1.
WP_010998886.1. NC_003272.1.

Genome annotation databases

EnsemblBacteriaiBAB76454; BAB76454; BAB76454.
GeneIDi1108356.
KEGGiana:alr4755.
PATRICi22780153. VBINosSp37423_5519.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000019 Genomic DNA. Translation: BAB76454.1 .
PIRi AC2400.
RefSeqi NP_488795.1. NC_003272.1.
WP_010998886.1. NC_003272.1.

3D structure databases

ProteinModelPortali P58711.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 103690.alr4755.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB76454 ; BAB76454 ; BAB76454 .
GeneIDi 1108356.
KEGGi ana:alr4755.
PATRICi 22780153. VBINosSp37423_5519.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .

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: PCC 7120 / UTEX 2576.

Entry informationi

Entry nameiPDXA_NOSS1
AccessioniPrimary (citable) accession number: P58711
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: January 31, 2002
Last modified: September 3, 2014
This is version 77 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 By similarity.

Keywords - Technical termi

Complete 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