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A6UR78

- HEM1_METVS

UniProt

A6UR78 - HEM1_METVS

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Mevan_1100
Organism
Methanococcus vannielii (strain SB / ATCC 35089 / DSM 1224)
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 sitei39 – 391Nucleophile By similarity
Sitei74 – 741Important for activity By similarity
Binding sitei84 – 841Substrate By similarity
Binding sitei95 – 951Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi163 – 1686NADP 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

BioCyciMVAN406327:GI04-1127-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:Mevan_1100
OrganismiMethanococcus vannielii (strain SB / ATCC 35089 / DSM 1224)
Taxonomic identifieri406327 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
ProteomesiUP000001107: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Glutamyl-tRNA reductaseUniRule annotation
PRO_1000004644Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi406327.Mevan_1100.

Structurei

3D structure databases

ProteinModelPortaliA6UR78.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 414Substrate binding By similarity
Regioni89 – 913Substrate 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.
OMAiMIICEEL.

Family and domain databases

Gene3Di1.10.1200.70. 1 hit.
3.40.50.720. 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.

A6UR78-1 [UniParc]FASTAAdd to Basket

« Hide

MLVIKADYKK YPLPVLESMR INEDEFYGKY DACIIVQTCN RIEAYFDEEI    50
NDIEKIIPDF KGFDVIKGKK ATLHFLNVAC GMDSMILGEN QILGQIKSSY 100
HKSKELKKTS KYLENLFLKA IHVGQRVRAE TKINEGGVSI GSAAVELAEM 150
KLGLKNRNVL LIGAGEIGTL VAKALIEKHI KAVIVANRTY ERAETLAKEL 200
KGMAVHFDKL KEAINFSDVI ICATSSPHYI LEKSDLLDVG NKIIIDIANP 250
RDVDDSVREL ENISLYTIDD LRNISDKNLQ KRLKEVPIVE NIIEEEYGIL 300
LKQIEKTNVE EVIKDFNTYI EDVRKKELEK AVRLCKNKSP DEIMENFSKA 350
FVKRITHDFV SYSLSVSKED LLNSIWWKK 379
Length:379
Mass (Da):43,233
Last modified:August 21, 2007 - v1
Checksum:i4DA687CEFAEC775E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000742 Genomic DNA. Translation: ABR55000.1.
RefSeqiWP_012065915.1. NC_009634.1.
YP_001323612.1. NC_009634.1.

Genome annotation databases

EnsemblBacteriaiABR55000; ABR55000; Mevan_1100.
GeneIDi5324539.
KEGGimvn:Mevan_1100.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000742 Genomic DNA. Translation: ABR55000.1 .
RefSeqi WP_012065915.1. NC_009634.1.
YP_001323612.1. NC_009634.1.

3D structure databases

ProteinModelPortali A6UR78.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 406327.Mevan_1100.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABR55000 ; ABR55000 ; Mevan_1100 .
GeneIDi 5324539.
KEGGi mvn:Mevan_1100.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci MVAN406327:GI04-1127-MONOMER.

Family and domain databases

Gene3Di 1.10.1200.70. 1 hit.
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: SB / ATCC 35089 / DSM 1224.

Entry informationi

Entry nameiHEM1_METVS
AccessioniPrimary (citable) accession number: A6UR78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: September 3, 2014
This is version 54 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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