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A6GVP1

- HEM1_FLAPJ

UniProt

A6GVP1 - HEM1_FLAPJ

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Protein
Glutamyl-tRNA reductase
Gene
hemA, FP0044
Organism
Flavobacterium psychrophilum (strain JIP02/86 / ATCC 49511)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity.UniRule annotation

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei58 – 581Nucleophile By similarity
Sitei103 – 1031Important for activity By similarity
Binding sitei113 – 1131Substrate By similarity
Binding sitei124 – 1241Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi193 – 1986NADP By similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:FP0044
OrganismiFlavobacterium psychrophilum (strain JIP02/86 / ATCC 49511)
Taxonomic identifieri402612 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeFlavobacterium
ProteomesiUP000006394: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 413413Glutamyl-tRNA reductaseUniRule annotation
PRO_0000335034Add
BLAST

Proteomic databases

PRIDEiA6GVP1.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi402612.FP0044.

Structurei

3D structure databases

ProteinModelPortaliA6GVP1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 604Substrate binding By similarity
Regioni118 – 1203Substrate binding By similarity

Domaini

Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization By similarity.UniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000251726.
KOiK02492.
OMAiLAHKLTN.
OrthoDBiEOG6QG8G0.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A6GVP1-1 [UniParc]FASTAAdd to Basket

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MENNTIPKHN TFYAIGLNYK KADAEIRGKF SIDAQSKSNL LQQAKTEGIE    50
SLIVTSTCNR TEIYGFAQHP FQLIKLLCEN SKGTVEDFQK VAYVYKNQEA 100
ISHLFKVGTG LDSQILGDFE IISQIKIAFT ESKALDLANS FMERLVNSVI 150
QASKRIKTDT DISSGATSVS FASVQYIMKN VANIGEKNIL LFGTGKIGRN 200
TCENLVKHSK NEHITLINRT KDKAEKLAGK LNLIVKDYAD LHIELQKADV 250
LVVATGAQNP TIDKAILNLK KPLLILDLSI PKNVNSDVNE LENVTLVHLD 300
DLSQITDETL EKRKLHIPAA EAIIEEIKNE FSSWMNGRKY APTIHALKAK 350
LNTIKEKELI FQRKKLSNFD EEQAELISNR IIQKITNHFA NHLKDEETMV 400
DESIDYINKI FQL 413
Length:413
Mass (Da):46,514
Last modified:July 24, 2007 - v1
Checksum:iC8FE2BB7453ECFE0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM398681 Genomic DNA. Translation: CAL42163.1.
RefSeqiYP_001294984.1. NC_009613.3.

Genome annotation databases

EnsemblBacteriaiCAL42163; CAL42163; FP0044.
GeneIDi5298867.
KEGGifps:FP0044.
PATRICi21904908. VBIFlaPsy4505_0048.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM398681 Genomic DNA. Translation: CAL42163.1 .
RefSeqi YP_001294984.1. NC_009613.3.

3D structure databases

ProteinModelPortali A6GVP1.
ModBasei Search...

Protein-protein interaction databases

STRINGi 402612.FP0044.

Proteomic databases

PRIDEi A6GVP1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAL42163 ; CAL42163 ; FP0044 .
GeneIDi 5298867.
KEGGi fps:FP0044.
PATRICi 21904908. VBIFlaPsy4505_0048.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000251726.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6QG8G0.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view ]
Pfami PF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMi SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JIP02/86 / ATCC 49511.

Entry informationi

Entry nameiHEM1_FLAPJ
AccessioniPrimary (citable) accession number: A6GVP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 24, 2007
Last modified: September 3, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA By similarity.

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

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