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Q0AC03

- HEM1_ALKEH

UniProt

Q0AC03 - HEM1_ALKEH

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Mlg_0279
Organism
Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1)
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
Sitei97 – 971Important for activity By similarity
Binding sitei107 – 1071Substrate By similarity
Binding sitei118 – 1181Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi187 – 1926NADP 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

BioCyciAEHR187272:GHAX-280-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:Mlg_0279
OrganismiAlkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1)
Taxonomic identifieri187272 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeAlkalilimnicola
ProteomesiUP000001962: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446Glutamyl-tRNA reductaseUniRule annotation
PRO_1000004591Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi187272.Mlg_0279.

Structurei

3D structure databases

ProteinModelPortaliQ0AC03.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni112 – 1143Substrate 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.
HOGENOMiHOG000109650.
KOiK02492.
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.

Q0AC03-1 [UniParc]FASTAAdd to Basket

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MSLFALGLNH KSAPVNIREQ IVFAPDAVTA ALQHLRAHTT AREAAILSTC    50
NRTELYVRMD DRAPEMLGEW LARYHRLDPE WLRDYLYLHE GAGAVRHLMR 100
VSAGLDSLVL GEPQILGQAK IAYQGAIDAG TMGRVLDRLF QHAFSVAKQV 150
RTDTGIGANP VSVAFAAVTL ARQIFDDFQN RTALLIGAGE TIELVARHLR 200
EQGLKNLIVA NRNLERARQL VELEGGEAIP LSEIPTRLPE ADVLVASTAS 250
PLPILGKGTV ERAVRKRRHR PMFMLDLAVP RDIEPEAGNL DDVYLYTVDD 300
LREVIAENRR SREEAAHQAE EIVQRQVDQF LSWRRAQQAV ASICDFRERG 350
HAHARELLQR ANRRLRCGEP PERVLAWLSH TLTNRLLHAP TVGLREAAEA 400
GDRERIELAR TLLQIENANE DTRESVDKEQ TGTTQGAARG DQRSTG 446
Length:446
Mass (Da):49,827
Last modified:October 17, 2006 - v1
Checksum:iB3DF51282454B406
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000453 Genomic DNA. Translation: ABI55634.1.
RefSeqiYP_741124.1. NC_008340.1.

Genome annotation databases

EnsemblBacteriaiABI55634; ABI55634; Mlg_0279.
GeneIDi4270497.
KEGGiaeh:Mlg_0279.
PATRICi20859716. VBIAlkEhr114327_0271.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000453 Genomic DNA. Translation: ABI55634.1 .
RefSeqi YP_741124.1. NC_008340.1.

3D structure databases

ProteinModelPortali Q0AC03.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 187272.Mlg_0279.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABI55634 ; ABI55634 ; Mlg_0279 .
GeneIDi 4270497.
KEGGi aeh:Mlg_0279.
PATRICi 20859716. VBIAlkEhr114327_0271.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci AEHR187272:GHAX-280-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 BAA-1101 / DSM 17681 / MLHE-1.

Entry informationi

Entry nameiHEM1_ALKEH
AccessioniPrimary (citable) accession number: Q0AC03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 66 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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