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Q47Y92

- HEM1_COLP3

UniProt

Q47Y92 - HEM1_COLP3

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Protein
Glutamyl-tRNA reductase
Gene
hemA, CPS_3554
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) 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 sitei50 – 501Nucleophile By similarity
Sitei100 – 1001Important for activity By similarity
Binding sitei110 – 1101Substrate By similarity
Binding sitei121 – 1211Substrate By similarity

Regions

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

BioCyciCPSY167879:GI48-3554-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: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 reductaseUniRule annotation
PRO_1000004615Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi167879.CPS_3554.

Structurei

3D structure databases

ProteinModelPortaliQ47Y92.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni115 – 1173Substrate 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.
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

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MSIVAVGINH KTAPVAVREK ISFNPDKLSI ALQEMLNAVQ CREVAILSTC    50
NRTELYLVQD GDFDVTQQRL IKWLESFHNV PASTILPSLY WHKDQQAVNH 100
MMRVACGLDS LVLGEPQILG QMKQAYSQAK AAGSMSLIMD RLFQRTFGVA 150
KQVRTETEIG ASAVSVAFAS VNLAKHIFGG LEKTKVLLVG AGETIELVAK 200
HLYENNVGKI TVANRTLARA ENMATKIGAD VITLAQIPEH MCNADIVISS 250
TGSTLPIIGK GMVEQALASR KHQPIFMVDL AVPRDIEEQV SELEDVFLYT 300
VDDLQGIIAK NIANRRKAAV QAESIVNSQS DNFMAWLRGL NTQDTVISYR 350
KQCLDNRDVL LEKAFIQLKN GKNSEAVLAE LANKLTNKFM HAPTSALQSA 400
AQGGELDKLI YLRDIFNIDS QE 422
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.
RefSeqiWP_011044314.1. NC_003910.7.
YP_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 WP_011044314.1. NC_003910.7.
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: September 3, 2014
This is version 70 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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