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A0LIM5

- HEM1_SYNFM

UniProt

A0LIM5 - HEM1_SYNFM

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Sfum_1590
Organism
Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB)
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 sitei51 – 511Nucleophile By similarity
Sitei101 – 1011Important for activity By similarity
Binding sitei111 – 1111Substrate By similarity
Binding sitei122 – 1221Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi191 – 1966NADP 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

BioCyciSFUM335543:GH6P-1621-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:Sfum_1590
OrganismiSyntrophobacter fumaroxidans (strain DSM 10017 / MPOB)
Taxonomic identifieri335543 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophobacteraceaeSyntrophobacter
ProteomesiUP000001784: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Glutamyl-tRNA reductaseUniRule annotation
PRO_0000335075Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi335543.Sfum_1590.

Structurei

3D structure databases

ProteinModelPortaliA0LIM5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate binding By similarity
Regioni116 – 1183Substrate 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.
OMAiHEVTGEY.
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.
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.

A0LIM5-1 [UniParc]FASTAAdd to Basket

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MCHIILLGMN HKTAPVEMRE RLAVACRQEV NPLRLLPRLE NVDELLFLST    50
CNRVEFLFTC RDRDGGLREV TALLRTYLGL DSTEGVENHV YAFRGMEAVR 100
HVFRVASSLD SMVVGEPQIL GQLKSAYREA TEWRTVKVIL NRLLHKTFSV 150
AKRVRSETCI GSNAVSISYA AVELAKKIFG SLQDKRVLLI GAGEMAELAA 200
EHLLAQGVRH MVVANRTLER AVDLAKRFRA ETTPFDHILN ALKNTDIVLS 250
STGAPEPILK YNDVRARMRE RRNKPLFFID IAVPRDIDPK INEIDNVYLY 300
DIDDLQGVID LNREERKREA ERAEHIIAGE TLKFQEWMAT LNVVPTIVAL 350
REKAETIRRS ELQRTLSHLP HMSEKDRLAV EALTEAIVKK LLHDPIVFLK 400
KKADRSTKDM YVDYTQQLFN LADGDDGEEA PAVTVQMASA GNDGTLLKTF 450
EPDKESPWRK S 461
Length:461
Mass (Da):52,306
Last modified:December 12, 2006 - v1
Checksum:i9D661EDF144D8680
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000478 Genomic DNA. Translation: ABK17277.1.
RefSeqiYP_845712.1. NC_008554.1.

Genome annotation databases

EnsemblBacteriaiABK17277; ABK17277; Sfum_1590.
GeneIDi4460125.
KEGGisfu:Sfum_1590.
PATRICi23848561. VBISynFum78438_1854.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000478 Genomic DNA. Translation: ABK17277.1 .
RefSeqi YP_845712.1. NC_008554.1.

3D structure databases

ProteinModelPortali A0LIM5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 335543.Sfum_1590.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABK17277 ; ABK17277 ; Sfum_1590 .
GeneIDi 4460125.
KEGGi sfu:Sfum_1590.
PATRICi 23848561. VBISynFum78438_1854.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci SFUM335543:GH6P-1621-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.
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: DSM 10017 / MPOB.

Entry informationi

Entry nameiHEM1_SYNFM
AccessioniPrimary (citable) accession number: A0LIM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 12, 2006
Last modified: September 3, 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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