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Q6M130

- HEM1_METMP

UniProt

Q6M130 - HEM1_METMP

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanococcus maripaludis (strain S2 / LL)
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

BioCyciMMAR267377:GJ77-101-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:MMP0088
OrganismiMethanococcus maripaludis (strain S2 / LL)
Taxonomic identifieri267377 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
ProteomesiUP000000590: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382Glutamyl-tRNA reductasePRO_0000114104Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi267377.MMP0088.

Structurei

3D structure databases

ProteinModelPortaliQ6M130.
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.

Q6M130-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLVVRADYKK YPIPVLEKMR IDEDEFYKKY DACVVVQTCN RIEAYFDTEV
60 70 80 90 100
NSDLNCILND FSGFDILKGK NATFHFLKVS CGMDSMILGE NQILGQIKTS
110 120 130 140 150
FQKARELKKT SRYLDSVFLK AIHVGQRART ETKINEGSVS IGSAAVELAE
160 170 180 190 200
KNFGLANKNV LLIGAGEIGT LVAKALMEKH IKAVIVANRT YERAETLAKE
210 220 230 240 250
LKGMAVHFDK LKEAINFSDV IICATSSPHY ILKKEDLIDV GNKIIIDIAN
260 270 280 290 300
PRDVDDAVRE FENINLYTID DLRNISDKNL QKRIEEVPAV EKIIDEEYDV
310 320 330 340 350
LMKQIEKINV EEVLKDFNNY IEEIRTKELE KAIKLSKTKN PEEIMENFSK
360 370 380
AFAKRITHDF VSYSINTSKE DLMNSAWWKN GK
Length:382
Mass (Da):43,612
Last modified:July 5, 2004 - v1
Checksum:iE73FD60D719A0C47
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX950229 Genomic DNA. Translation: CAF29644.1.
RefSeqiNP_987208.1. NC_005791.1.
WP_011170032.1. NC_005791.1.

Genome annotation databases

EnsemblBacteriaiCAF29644; CAF29644; MMP0088.
GeneIDi2762055.
KEGGimmp:MMP0088.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX950229 Genomic DNA. Translation: CAF29644.1 .
RefSeqi NP_987208.1. NC_005791.1.
WP_011170032.1. NC_005791.1.

3D structure databases

ProteinModelPortali Q6M130.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 267377.MMP0088.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAF29644 ; CAF29644 ; MMP0088 .
GeneIDi 2762055.
KEGGi mmp:MMP0088.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci MMAR267377:GJ77-101-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: S2 / LL.

Entry informationi

Entry nameiHEM1_METMP
AccessioniPrimary (citable) accession number: Q6M130
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 5, 2004
Last modified: October 1, 2014
This is version 78 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3