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A6VI77

- HEM1_METM7

UniProt

A6VI77 - HEM1_METM7

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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 – 391NucleophileUniRule annotation
Sitei75 – 751Important for activityUniRule annotation
Binding sitei85 – 851SubstrateUniRule annotation
Binding sitei96 – 961SubstrateUniRule annotation

Regions

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

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

BioCyciMMAR426368:GHHL-1118-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
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 reductasePRO_1000004640Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi426368.MmarC7_1087.

Structurei

3D structure databases

ProteinModelPortaliA6VI77.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 414Substrate bindingUniRule annotation
Regioni90 – 923Substrate bindingUniRule annotation

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.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

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

        10         20         30         40         50
MLVVKADYKK YPIPVLEKMR IDEDEFYKKY EACVVVQTCN RIEAYFDTEV
60 70 80 90 100
NSNVDDILKD FQGFDILKGK NATFHFLKVS CGMDSMILGE NQILGQIKTS
110 120 130 140 150
FQKAREFKKT SRYLDSLFLK AIHVGQRART ETKINEGGVS IGSAAVELAE
160 170 180 190 200
KNFGLTNRNV LLIGAGEIGT LVAKALVEKH IKAVIVANRT YERAETLAKE
210 220 230 240 250
LKGMAVHFDK LREAVNFSDV IICATSSPHY ILEKEDLIDV GNKIIIDIAN
260 270 280 290 300
PRDVDDSVRE LENIELYTID DLRNISDKNL QRRIEEIPTV EKIIEEEYDV
310 320 330 340 350
LMKQIEKINV EEVLKEFNTY IEEIRVKELE KAIKLSKSKD PEEIMENFSK
360 370 380
AFAKRITHDF VSYSLNTSKE DLMNSAWWKN GK
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.
RefSeqiYP_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 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: October 29, 2014
This is version 55 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.UniRule annotation

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