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Q5YP69

- HEM1_NOCFA

UniProt

Q5YP69 - HEM1_NOCFA

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Protein
Glutamyl-tRNA reductase
Gene
hemA, NFA_51700
Organism
Nocardia farcinica (strain IFM 10152)
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 bindingi189 – 1946NADP 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

BioCyciNFAR247156:GJ9T-5241-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:NFA_51700
OrganismiNocardia farcinica (strain IFM 10152)
Taxonomic identifieri247156 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeNocardia
ProteomesiUP000006820: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 477477Glutamyl-tRNA reductaseUniRule annotation
PRO_0000335054Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi247156.nfa51700.

Structurei

3D structure databases

ProteinModelPortaliQ5YP69.

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.
KOiK02492.
OMAiPYLYVHY.
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.

Q5YP69-1 [UniParc]FASTAAdd to Basket

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MSVLLVGVSH RSAPVSVLEK VAITDADRPK LIDKMLASSH ISEAMIVSTC    50
NRVEVYAVVD AFHGGLAEVG ELLTRHSGLA MPDLTKHAYV RYSEAAAEHL 100
FAVASGLDSM VVGEQQVLSQ IRGAYATADA QQAVGRTLHE LAQHALRVGK 150
RVHSETGIDR AGASVVSVAL DRAAQVLGDL AGRTAVVVGA GAMGGLSVAH 200
LARAGIGRII VVNRTIERAR RLAETAASYG VESSALELDR LHEAMSAADV 250
VLSCTGAVGA VVTLADTHRA LADRDRAEFP AGDRPLVFCD LGLPRDVEPA 300
VAGLPGVAVI DIESLQRDPA AGAAADDTAA ARSIVAEELA KYLAGQRMAE 350
VTPTVAALRQ RAAEVVEAEL LRLDSRLPGL AEPERDEVAR TVRRVVDKLL 400
HAPTVRVKQL ASTPGGDSYA EALRELFELK PGAAQAVAAP MEITAIGPDR 450
TAGLADDFTP GHRLDFEQHL GEEGKPA 477
Length:477
Mass (Da):50,016
Last modified:November 23, 2004 - v1
Checksum:iECD6A35672A88F32
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006618 Genomic DNA. Translation: BAD60022.1.
RefSeqiWP_011211704.1. NC_006361.1.
YP_121386.1. NC_006361.1.

Genome annotation databases

EnsemblBacteriaiBAD60022; BAD60022; NFA_51700.
GeneIDi3109557.
KEGGinfa:nfa51700.
PATRICi22739927. VBINocFar94200_5182.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006618 Genomic DNA. Translation: BAD60022.1 .
RefSeqi WP_011211704.1. NC_006361.1.
YP_121386.1. NC_006361.1.

3D structure databases

ProteinModelPortali Q5YP69.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 247156.nfa51700.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD60022 ; BAD60022 ; NFA_51700 .
GeneIDi 3109557.
KEGGi nfa:nfa51700.
PATRICi 22739927. VBINocFar94200_5182.

Phylogenomic databases

eggNOGi COG0373.
KOi K02492.
OMAi PYLYVHY.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci NFAR247156:GJ9T-5241-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: IFM 10152.

Entry informationi

Entry nameiHEM1_NOCFA
AccessioniPrimary (citable) accession number: Q5YP69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 23, 2004
Last modified: September 3, 2014
This is version 79 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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