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Q47Y92

- HEM1_COLP3

UniProt

Q47Y92 - HEM1_COLP3

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus)
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).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 sitei50 – 501NucleophileUniRule annotation
Sitei100 – 1001Important for activityUniRule annotation
Binding sitei110 – 1101SubstrateUniRule annotation
Binding sitei121 – 1211SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi190 – 1956NADPUniRule annotation

GO - Molecular functioni

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

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

BioCyciCPSY167879:GI48-3554-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
Ordered Locus Names:CPS_3554
OrganismiColwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus)
Taxonomic identifieri167879 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeColwellia
ProteomesiUP000000547: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Glutamyl-tRNA reductasePRO_1000004615Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi167879.CPS_3554.

Structurei

3D structure databases

ProteinModelPortaliQ47Y92.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni115 – 1173Substrate bindingUniRule annotation

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.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109650.
KOiK02492.
OMAiLAHKLTN.
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.
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.

Q47Y92-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSIVAVGINH KTAPVAVREK ISFNPDKLSI ALQEMLNAVQ CREVAILSTC
60 70 80 90 100
NRTELYLVQD GDFDVTQQRL IKWLESFHNV PASTILPSLY WHKDQQAVNH
110 120 130 140 150
MMRVACGLDS LVLGEPQILG QMKQAYSQAK AAGSMSLIMD RLFQRTFGVA
160 170 180 190 200
KQVRTETEIG ASAVSVAFAS VNLAKHIFGG LEKTKVLLVG AGETIELVAK
210 220 230 240 250
HLYENNVGKI TVANRTLARA ENMATKIGAD VITLAQIPEH MCNADIVISS
260 270 280 290 300
TGSTLPIIGK GMVEQALASR KHQPIFMVDL AVPRDIEEQV SELEDVFLYT
310 320 330 340 350
VDDLQGIIAK NIANRRKAAV QAESIVNSQS DNFMAWLRGL NTQDTVISYR
360 370 380 390 400
KQCLDNRDVL LEKAFIQLKN GKNSEAVLAE LANKLTNKFM HAPTSALQSA
410 420
AQGGELDKLI YLRDIFNIDS QE
Length:422
Mass (Da):46,447
Last modified:September 13, 2005 - v1
Checksum:iFAA4B2312F68FD8E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000083 Genomic DNA. Translation: AAZ26562.1.
RefSeqiYP_270228.1. NC_003910.7.

Genome annotation databases

EnsemblBacteriaiAAZ26562; AAZ26562; CPS_3554.
GeneIDi3520815.
KEGGicps:CPS_3554.
PATRICi21470039. VBIColPsy94388_3218.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000083 Genomic DNA. Translation: AAZ26562.1 .
RefSeqi YP_270228.1. NC_003910.7.

3D structure databases

ProteinModelPortali Q47Y92.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 167879.CPS_3554.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAZ26562 ; AAZ26562 ; CPS_3554 .
GeneIDi 3520815.
KEGGi cps:CPS_3554.
PATRICi 21470039. VBIColPsy94388_3218.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CPSY167879:GI48-3554-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.
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: 34H / ATCC BAA-681.

Entry informationi

Entry nameiHEM1_COLP3
AccessioniPrimary (citable) accession number: Q47Y92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 13, 2005
Last modified: October 29, 2014
This is version 72 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.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