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A9A8K3

- HEM1_METM6

UniProt

A9A8K3 - HEM1_METM6

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Protein

Glutamyl-tRNA reductase

Gene
hemA, MmarC6_0859
Organism
Methanococcus maripaludis (strain C6 / ATCC BAA-1332)
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. 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

BioCyciMMAR444158:GHN2-876-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:MmarC6_0859
OrganismiMethanococcus maripaludis (strain C6 / ATCC BAA-1332)
Taxonomic identifieri444158 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
ProteomesiUP000000791: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382Glutamyl-tRNA reductaseUniRule annotationPRO_1000093150Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi444158.MmarC6_0859.

Structurei

3D structure databases

ProteinModelPortaliA9A8K3.

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.

A9A8K3-1 [UniParc]FASTAAdd to Basket

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MLVVKADYKK YPIPVLEKMR IDEDEFYKKY EACVVVQTCN RIEAYFDTEV    50
NSDIDCILND FSGFDVLKGK TATFHFLRVS CGMESMILGE NQILGQIKTS 100
FQKARELKKT SRYLDGLFLK AIHVGQRART ETKINEGGVS IGSAAVELAE 150
KNFGLTNRNV LLIGAGEMGT LVAKALLEKH IKAVIVSNRT YERAETLAEE 200
LKGIAVHFDK LKEAINFSDV IICATSSPHY ILKKEDLNDV GNKIIIDIAN 250
PRDVDDAVRE FENIKLYTID DLRNISDKNI QKRVEEVPAV EKIINEEYEV 300
LMKQIEKINI EEVLKDFNSY VEEIRVKELE KAIKLSKTKN PEEIMENFSK 350
AFVKRITHDF VSYSINTSKE DLMNSAWWKN GK 382
Length:382
Mass (Da):43,638
Last modified:January 15, 2008 - v1
Checksum:iF42CF2F9564B848E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000867 Genomic DNA. Translation: ABX01676.1.
RefSeqiWP_012193631.1. NC_009975.1.
YP_001548908.1. NC_009975.1.

Genome annotation databases

EnsemblBacteriaiABX01676; ABX01676; MmarC6_0859.
GeneIDi5738024.
KEGGimmx:MmarC6_0859.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000867 Genomic DNA. Translation: ABX01676.1 .
RefSeqi WP_012193631.1. NC_009975.1.
YP_001548908.1. NC_009975.1.

3D structure databases

ProteinModelPortali A9A8K3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 444158.MmarC6_0859.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX01676 ; ABX01676 ; MmarC6_0859 .
GeneIDi 5738024.
KEGGi mmx:MmarC6_0859.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci MMAR444158:GHN2-876-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: C6 / ATCC BAA-1332.

Entry informationi

Entry nameiHEM1_METM6
AccessioniPrimary (citable) accession number: A9A8K3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: September 3, 2014
This is version 52 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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