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Q2RJ25

- HEM1_MOOTA

UniProt

Q2RJ25 - HEM1_MOOTA

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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 – 501NucleophileUniRule annotation
Sitei99 – 991Important for activityUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation
Binding sitei120 – 1201SubstrateUniRule annotation

Regions

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

BioCyciMTHE264732:GH0A-1303-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: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 reductasePRO_1000004645Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi264732.Moth_1250.

Structurei

3D structure databases

ProteinModelPortaliQ2RJ25.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni114 – 1163Substrate 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.
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

« Hide

        10         20         30         40         50
MFVVAAGLNH RTAPVAIREQ LAFARHGLPP ALCRLKEEAG VEGCVILSTC
60 70 80 90 100
NRTEVYIACN QEEAGLKAAK NFLGRSCKLA LADLEGYLYT LNTHHAVRHL
110 120 130 140 150
FRVAAGLDSM ILGEDQVLAQ VAEAYQVARE TGTTNNVLNT LWQQAIYAGK
160 170 180 190 200
RVRTETRIDA NTVSVSYAAV ELARQVFHDE LDGRTVLVIG AGKMSTLAAR
210 220 230 240 250
YLKDKGVTTV LVSNRSYDRA VALAATIGGQ AVRLDALEDY LPRADIVISC
260 270 280 290 300
TAASHYILHR DQVARAVAAR PGVPLMLIDI AVPRDIEPAA GDLPGVKLYD
310 320 330 340 350
IDDLQQVVLA NLEERKKAAR QAEGIIAAEA EAFFQWLGSL YVVPTIVALK
360 370 380 390 400
EKAEAIKNAE VRRACNRLGQ LTTREQKIIT SMATTIVNQL LHDAIVNLKA
410 420 430 440
AALTPRGHLY VEALQELFEL RVDHTLPGPD MAVSVEGGRK Y
Length:441
Mass (Da):48,018
Last modified:January 24, 2006 - v1
Checksum:iC21A8082EE73A761
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000232 Genomic DNA. Translation: ABC19564.1.
RefSeqiYP_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:
EMBLi
GenBanki
DDBJi
Links Updated
CP000232 Genomic DNA. Translation: ABC19564.1 .
RefSeqi 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: October 29, 2014
This is version 72 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