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Q18F28

- HEM1_HALWD

UniProt

Q18F28 - HEM1_HALWD

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Protein
Glutamyl-tRNA reductase
Gene
hemA, HQ_3336A
Organism
Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)
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
Sitei93 – 931Important for activity By similarity
Binding sitei103 – 1031Substrate By similarity
Binding sitei114 – 1141Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi182 – 1876NADP 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

BioCyciHWAL362976:GJSR-2460-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:HQ_3336A
OrganismiHaloquadratum walsbyi (strain DSM 16790 / HBSQ001)
Taxonomic identifieri362976 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloquadratum
ProteomesiUP000001975: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454Glutamyl-tRNA reductaseUniRule annotation
PRO_0000335088Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi362976.HQ3336A.

Structurei

3D structure databases

ProteinModelPortaliQ18F28.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate binding By similarity
Regioni108 – 1103Substrate 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.
HOGENOMiHOG000109651.
KOiK02492.
OMAiEHMIEDE.

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.

Q18F28-1 [UniParc]FASTAAdd to Basket

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MNTGVICGVR VSHNRASVEE IELAGERDSR TIMETLLTRD GITESFAIQT    50
CNRSEAYVVA DGAVAGRRAL ASFAPDVRDG AVVDMSHEES LRHLLRVATG 100
LESLVLGEDQ ILGQFKRAIE VARGIGALGP MLEAGVTKAI HVGERARSET 150
SINEGAVSIG SAAVRLAGQS VGLNGRKALV IGAGEMGSLV AESLASTNIS 200
EVVIANRTIE NAESIAETIN SPAYAVSLDS LTEVITEASI IMTATGYGKY 250
LIEPTDIDGA GETFIIDLAQ PRNVHPATAD IENAIVQDID ALESITKETE 300
ASRQAAAREV DAMIDEEFDR LLESYKRQRA DEAISEMYEA AEHVKRREVE 350
TALEKLEKQG TLTDNQRETI SSMADTLINQ LLAAPTKSLR DAAAEDDWTT 400
IQTAMTLFDP NFGGDTPQPD RPDDIPRAAE RGDISGDDLP DDVPNHIAEK 450
VSDG 454
Length:454
Mass (Da):48,625
Last modified:July 25, 2006 - v1
Checksum:i2D20D329DCA6FDDC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM180088 Genomic DNA. Translation: CAJ53433.1.
RefSeqiWP_011572535.1. NC_008212.1.
YP_659025.1. NC_008212.1.

Genome annotation databases

EnsemblBacteriaiCAJ53433; CAJ53433; HQ_3336A.
GeneIDi4194102.
KEGGihwa:HQ3336A.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM180088 Genomic DNA. Translation: CAJ53433.1 .
RefSeqi WP_011572535.1. NC_008212.1.
YP_659025.1. NC_008212.1.

3D structure databases

ProteinModelPortali Q18F28.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 362976.HQ3336A.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAJ53433 ; CAJ53433 ; HQ_3336A .
GeneIDi 4194102.
KEGGi hwa:HQ3336A.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi EHMIEDE.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci HWAL362976:GJSR-2460-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. "The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity."
    Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., Pfeiffer F., Oesterhelt D.
    BMC Genomics 7:169-169(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 16790 / HBSQ001.

Entry informationi

Entry nameiHEM1_HALWD
AccessioniPrimary (citable) accession number: Q18F28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 25, 2006
Last modified: September 3, 2014
This is version 74 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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