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Q72C23

- HEM1_DESVH

UniProt

Q72C23 - HEM1_DESVH

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Protein

Glutamyl-tRNA reductase

Gene
hemA, DVU_1461
Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
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 sitei51 – 511Nucleophile By similarity
Sitei99 – 991Important for activity By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei120 – 1201Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADP By similarity

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

BioCyciDVUL882:GJIL-1492-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:DVU_1461
OrganismiDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Taxonomic identifieri882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
ProteomesiUP000002194: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Glutamyl-tRNA reductaseUniRule annotationPRO_0000114021Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi882.DVU1461.

Structurei

3D structure databases

ProteinModelPortaliQ72C23.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate binding By similarity
Regioni114 – 1163Substrate 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.
KOiK02492.
OMAiLAHKLTN.
OrthoDBiEOG6MWNBM.
PhylomeDBiQ72C23.

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.

Q72C23-1 [UniParc]FASTAAdd to Basket

« Hide

MERDIYLIGL NHRTAGVEVR ERFALTDCNV LEQGVVPIDD VVSEVLILST    50
CNRVEILAVG RGPEVVSRVL RGWSAARGQC EHDLAPYVYT HKGPEAIRHL 100
FRVASSLDSM VVGEPQILGQ LKDAYRKAIE RNCTRVILNR LLHKAFSVAK 150
RVRTETGVAS SAVSISYAAV ELAKRIFGEM NQYKAMLIGA GEMAELAATH 200
LLHAGISKIY VANRTFERGR ELARQFNGEA IHFEDLFERL ADADIIISST 250
GAHEAIIRAR DIKDVLRRRK HRPMFFIDIA VPRDIDPDVN NLDNVYLYDI 300
DDLKEVVEEN LAQRREEASK ALTIVEEETG KFGQWLRSLE LQPTIVDLIR 350
RSERIAQDEL ARTLKRLGPV DDETRDALEA MLSSMVRKLN HEPITFLKRR 400
HSEEDAGPRY IDIARRMFNL DDDNVPPDAH CDRRRHDEDN 440
Length:440
Mass (Da):50,045
Last modified:July 5, 2004 - v1
Checksum:iD166E5291B50E3BF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017285 Genomic DNA. Translation: AAS95939.1.
RefSeqiWP_010938754.1. NC_002937.3.
YP_010680.1. NC_002937.3.

Genome annotation databases

EnsemblBacteriaiAAS95939; AAS95939; DVU_1461.
GeneIDi2794879.
KEGGidvu:DVU1461.
PATRICi32062756. VBIDesVul119526_1360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017285 Genomic DNA. Translation: AAS95939.1 .
RefSeqi WP_010938754.1. NC_002937.3.
YP_010680.1. NC_002937.3.

3D structure databases

ProteinModelPortali Q72C23.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 882.DVU1461.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAS95939 ; AAS95939 ; DVU_1461 .
GeneIDi 2794879.
KEGGi dvu:DVU1461.
PATRICi 32062756. VBIDesVul119526_1360.

Phylogenomic databases

eggNOGi COG0373.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.
PhylomeDBi Q72C23.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci DVUL882:GJIL-1492-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: Hildenborough / ATCC 29579 / NCIMB 8303.

Entry informationi

Entry nameiHEM1_DESVH
AccessioniPrimary (citable) accession number: Q72C23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 5, 2004
Last modified: September 3, 2014
This is version 81 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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