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A6VI77

- HEM1_METM7

UniProt

A6VI77 - HEM1_METM7

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Protein
Glutamyl-tRNA reductase
Gene
hemA, MmarC7_1087
Organism
Methanococcus maripaludis (strain C7 / ATCC BAA-1331)
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
Sitei75 – 751Important for activity By similarity
Binding sitei85 – 851Substrate By similarity
Binding sitei96 – 961Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi164 – 1696NADP 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

BioCyciMMAR426368:GHHL-1118-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:MmarC7_1087
OrganismiMethanococcus maripaludis (strain C7 / ATCC BAA-1331)
Taxonomic identifieri426368 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
ProteomesiUP000002298: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382Glutamyl-tRNA reductaseUniRule annotation
PRO_1000004640Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi426368.MmarC7_1087.

Structurei

3D structure databases

ProteinModelPortaliA6VI77.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 414Substrate binding By similarity
Regioni90 – 923Substrate 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.

A6VI77-1 [UniParc]FASTAAdd to Basket

« Hide

MLVVKADYKK YPIPVLEKMR IDEDEFYKKY EACVVVQTCN RIEAYFDTEV    50
NSNVDDILKD FQGFDILKGK NATFHFLKVS CGMDSMILGE NQILGQIKTS 100
FQKAREFKKT SRYLDSLFLK AIHVGQRART ETKINEGGVS IGSAAVELAE 150
KNFGLTNRNV LLIGAGEIGT LVAKALVEKH IKAVIVANRT YERAETLAKE 200
LKGMAVHFDK LREAVNFSDV IICATSSPHY ILEKEDLIDV GNKIIIDIAN 250
PRDVDDSVRE LENIELYTID DLRNISDKNL QRRIEEIPTV EKIIEEEYDV 300
LMKQIEKINV EEVLKEFNTY IEEIRVKELE KAIKLSKSKD PEEIMENFSK 350
AFAKRITHDF VSYSLNTSKE DLMNSAWWKN GK 382
Length:382
Mass (Da):43,779
Last modified:August 21, 2007 - v1
Checksum:i88183D579031E9B7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000745 Genomic DNA. Translation: ABR66153.1.
RefSeqiWP_011977465.1. NC_009637.1.
YP_001330304.1. NC_009637.1.

Genome annotation databases

EnsemblBacteriaiABR66153; ABR66153; MmarC7_1087.
GeneIDi5329330.
KEGGimmz:MmarC7_1087.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000745 Genomic DNA. Translation: ABR66153.1 .
RefSeqi WP_011977465.1. NC_009637.1.
YP_001330304.1. NC_009637.1.

3D structure databases

ProteinModelPortali A6VI77.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 426368.MmarC7_1087.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABR66153 ; ABR66153 ; MmarC7_1087 .
GeneIDi 5329330.
KEGGi mmz:MmarC7_1087.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci MMAR426368:GHHL-1118-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: C7 / ATCC BAA-1331.

Entry informationi

Entry nameiHEM1_METM7
AccessioniPrimary (citable) accession number: A6VI77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: September 3, 2014
This is version 53 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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