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A5WC75

- HEM1_PSYWF

UniProt

A5WC75 - HEM1_PSYWF

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Protein
Glutamyl-tRNA reductase
Gene
hemA, PsycPRwf_0311
Organism
Psychrobacter sp. (strain PRwf-1)
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 sitei48 – 481Nucleophile By similarity
Sitei122 – 1221Important for activity By similarity
Binding sitei132 – 1321Substrate By similarity
Binding sitei143 – 1431Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi212 – 2176NADP By similarity

GO - Molecular functioni

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

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

BioCyciPPRW349106:GHZF-316-MONOMER.
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:PsycPRwf_0311
OrganismiPsychrobacter sp. (strain PRwf-1)
Taxonomic identifieri349106 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
ProteomesiUP000001993: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Glutamyl-tRNA reductaseUniRule annotation
PRO_1000071248Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi349106.PsycPRwf_0311.

Structurei

3D structure databases

ProteinModelPortaliA5WC75.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate binding By similarity
Regioni137 – 1393Substrate 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.
HOGENOMiHOG000109650.
KOiK02492.
OMAiLNKQFET.
OrthoDBiEOG6MWNBM.

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.
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. 2 hits.
TIGRFAMsiTIGR01035. hemA. 1 hit.

Sequencei

Sequence statusi: Complete.

A5WC75-1 [UniParc]FASTAAdd to Basket

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MNLVVIGVNH KTAPVALRER LAFVGGDIQV AQAQLQQITA GSLIISTCNR    50
TEIYALAPST QLLANSDAAL SKQSDLSLAD EPVSTVDLTE QLITWLADFK 100
QVPLEETRPY LYDYVDGQAL THMLRVAAGL DSMILGEPQI FGQIKRSVNQ 150
AKEQGFLTNQ LNWVVEQIFA AAKRVRNETD VGTQAISLGY AASKLVTQIF 200
DRPEETTFLL IAAGEMNRLV AQNIAGLGVK RILICNRTPE RANLLAQELA 250
HLGIQIEVHP LTELDSLLYQ ADIVSSCSGS MDMLIDKAMT RRALKKRRYK 300
PMLMVDLAVP RDIDSSVGKL DDVYLYSIDD LQHVIAGNLE KRRQAAVEAE 350
LLVSHLVVEI ERRFQVRKVG QDIHDYRALA AQKAEAVLNE ALHELRTSEA 400
TAEEVMTELT RRLTQTLVHA PSSLMRRAAR DGNNEAIDLI ILGLKDAYRK 450
K 451
Length:451
Mass (Da):50,055
Last modified:July 10, 2007 - v1
Checksum:i5CC9E2785FFB4E97
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000713 Genomic DNA. Translation: ABQ93266.1.
RefSeqiWP_011959600.1. NC_009524.1.
YP_001279216.1. NC_009524.1.

Genome annotation databases

EnsemblBacteriaiABQ93266; ABQ93266; PsycPRwf_0311.
GeneIDi5204520.
KEGGiprw:PsycPRwf_0311.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000713 Genomic DNA. Translation: ABQ93266.1 .
RefSeqi WP_011959600.1. NC_009524.1.
YP_001279216.1. NC_009524.1.

3D structure databases

ProteinModelPortali A5WC75.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 349106.PsycPRwf_0311.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ93266 ; ABQ93266 ; PsycPRwf_0311 .
GeneIDi 5204520.
KEGGi prw:PsycPRwf_0311.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi LNKQFET.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci PPRW349106:GHZF-316-MONOMER.

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.
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. 2 hits.
TIGRFAMsi TIGR01035. hemA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PRwf-1.

Entry informationi

Entry nameiHEM1_PSYWF
AccessioniPrimary (citable) accession number: A5WC75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 10, 2007
Last modified: September 3, 2014
This is version 60 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

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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