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Q8PW60

- HEM1_METMA

UniProt

Q8PW60 - HEM1_METMA

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Protein

Glutamyl-tRNA reductase

Gene
hemA, MM_1741
Organism
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
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 sitei49 – 491Nucleophile By similarity
Sitei90 – 901Important for activity By similarity
Binding sitei100 – 1001Substrate By similarity
Binding sitei111 – 1111Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi180 – 1856NADP 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

BioCyciMMAZ192952:GCK2-1784-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:MM_1741
OrganismiMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Taxonomic identifieri192952 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
ProteomesiUP000000595: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Glutamyl-tRNA reductaseUniRule annotationPRO_0000114103Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi192952.MM_1741.

Structurei

3D structure databases

ProteinModelPortaliQ8PW60.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Substrate binding By similarity
Regioni105 – 1073Substrate 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.
OMAiLAHKLTN.

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.

Q8PW60-1 [UniParc]FASTAAdd to Basket

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MTEISSMVIS HKKAKVEEME SAWHGDLDGL LRNLYKHEYV YECVVLKTCN    50
RVEIYVVSPK SSSVLFSFAK EMGASTHIID FYGHDESLEH LLRLAGGLES 100
MIVGEDQILG QIKDLYAYSK KAGTTGKILE TAFEKAIQVG KRIRNETRIN 150
KGSVSIGSAA VDLAEDIFGG LTGKNVLVIG AGEIGVLVAK ALAEKDIEAI 200
YIANRTYKKA EEIAYELGGH AVRLDDIRDY LPGADVVISG TGAPHYILTR 250
EIVEEAIKCR ERKLLLIDIA NPRDIEESVV ELENVELCNI DNLRVISERT 300
LRMRKEEAKK AEAIIQEEIR LLNLQYKRQK ADRLISELYK QVYDVRLRER 350
QKAVNRLSSY HTIGDIETEV LDDLTRSIVN KILGEPTKVL RQAAELGNEE 400
FLDVVSRVFC LDKEKVRFEK IKQAKFDQIK PGCTKEQAEV KEEYAVKD 448
Length:448
Mass (Da):50,562
Last modified:October 1, 2002 - v1
Checksum:i0733780153168AD9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE008384 Genomic DNA. Translation: AAM31437.1.
RefSeqiNP_633765.1. NC_003901.1.

Genome annotation databases

EnsemblBacteriaiAAM31437; AAM31437; MM_1741.
GeneIDi1480083.
KEGGimma:MM_1741.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE008384 Genomic DNA. Translation: AAM31437.1 .
RefSeqi NP_633765.1. NC_003901.1.

3D structure databases

ProteinModelPortali Q8PW60.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 192952.MM_1741.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM31437 ; AAM31437 ; MM_1741 .
GeneIDi 1480083.
KEGGi mma:MM_1741.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci MMAZ192952:GCK2-1784-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 Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
    Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R.
    , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
    J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Entry informationi

Entry nameiHEM1_METMA
AccessioniPrimary (citable) accession number: Q8PW60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: October 1, 2002
Last modified: September 3, 2014
This is version 91 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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