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Q2RJ25

- HEM1_MOOTA

UniProt

Q2RJ25 - HEM1_MOOTA

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Moth_1250
Organism
Moorella thermoacetica (strain ATCC 39073)
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 sitei50 – 501Nucleophile By similarity
Sitei99 – 991Important for activity By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei120 – 1201Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi190 – 1956NADP 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

BioCyciMTHE264732:GH0A-1303-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:Moth_1250
OrganismiMoorella thermoacetica (strain ATCC 39073)
Taxonomic identifieri264732 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella
ProteomesiUP000007053: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Glutamyl-tRNA reductaseUniRule annotation
PRO_1000004645Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi264732.Moth_1250.

Structurei

3D structure databases

ProteinModelPortaliQ2RJ25.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni114 – 1163Substrate 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.
OrthoDBiEOG6MWNBM.

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.
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.

Sequencei

Sequence statusi: Complete.

Q2RJ25-1 [UniParc]FASTAAdd to Basket

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MFVVAAGLNH RTAPVAIREQ LAFARHGLPP ALCRLKEEAG VEGCVILSTC    50
NRTEVYIACN QEEAGLKAAK NFLGRSCKLA LADLEGYLYT LNTHHAVRHL 100
FRVAAGLDSM ILGEDQVLAQ VAEAYQVARE TGTTNNVLNT LWQQAIYAGK 150
RVRTETRIDA NTVSVSYAAV ELARQVFHDE LDGRTVLVIG AGKMSTLAAR 200
YLKDKGVTTV LVSNRSYDRA VALAATIGGQ AVRLDALEDY LPRADIVISC 250
TAASHYILHR DQVARAVAAR PGVPLMLIDI AVPRDIEPAA GDLPGVKLYD 300
IDDLQQVVLA NLEERKKAAR QAEGIIAAEA EAFFQWLGSL YVVPTIVALK 350
EKAEAIKNAE VRRACNRLGQ LTTREQKIIT SMATTIVNQL LHDAIVNLKA 400
AALTPRGHLY VEALQELFEL RVDHTLPGPD MAVSVEGGRK Y 441
Length:441
Mass (Da):48,018
Last modified:January 24, 2006 - v1
Checksum:iC21A8082EE73A761
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000232 Genomic DNA. Translation: ABC19564.1.
RefSeqiWP_011392764.1. NC_007644.1.
YP_430107.1. NC_007644.1.

Genome annotation databases

EnsemblBacteriaiABC19564; ABC19564; Moth_1250.
GeneIDi3833045.
KEGGimta:Moth_1250.
PATRICi22639726. VBIMooThe6753_1342.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000232 Genomic DNA. Translation: ABC19564.1 .
RefSeqi WP_011392764.1. NC_007644.1.
YP_430107.1. NC_007644.1.

3D structure databases

ProteinModelPortali Q2RJ25.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 264732.Moth_1250.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABC19564 ; ABC19564 ; Moth_1250 .
GeneIDi 3833045.
KEGGi mta:Moth_1250.
PATRICi 22639726. VBIMooThe6753_1342.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci MTHE264732:GH0A-1303-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.
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.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39073.

Entry informationi

Entry nameiHEM1_MOOTA
AccessioniPrimary (citable) accession number: Q2RJ25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 24, 2006
Last modified: September 3, 2014
This is version 70 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, 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

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