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A0JYN2

- HEM1_ARTS2

UniProt

A0JYN2 - HEM1_ARTS2

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Arth_2773
Organism
Arthrobacter sp. (strain FB24)
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 sitei48 – 481Nucleophile By similarity
Sitei100 – 1001Important for activity By similarity
Binding sitei110 – 1101Substrate By similarity
Binding sitei121 – 1211Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi192 – 1976NADP By similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
Complete GO annotation...

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

BioCyciASP290399:GHIF-2839-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:Arth_2773
OrganismiArthrobacter sp. (strain FB24)
Taxonomic identifieri290399 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter
ProteomesiUP000000754: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446Glutamyl-tRNA reductaseUniRule annotation
PRO_0000335010Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi290399.Arth_2773.

Structurei

3D structure databases

ProteinModelPortaliA0JYN2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate binding By similarity
Regioni115 – 1173Substrate 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.
HOGENOMiHOG000109649.
KOiK02492.

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.

A0JYN2-1 [UniParc]FASTAAdd to Basket

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MVLFSLVATH ADIDLETVAQ LSTGASELAT SALSGSPAVK GAVVLATCNR    50
FEIYGEAPHP DDVEAARAAL VAQISERTGL NEQLVSRSFN TRTGGEVSQH 100
LFAVSSGLDS AVVGEREIAG QVRRALINAQ HEGTASSGLV RLFQAASKTA 150
KDVGAQTALG SRGLSIVSVA LDLATDLSEN PDWSAKKAVV FGTGAYAGAT 200
MSLLRERGCT DISVFSSSGR AEGFVATRGG KALDSDTLPA AVAAADVMIG 250
CSGSDTRVEA EELARVRAGS AQTLIAIDLA LTHDFDPAVG ELDGVELLTL 300
ESVRLAAPQE QAESLAQASG IVTGAAAAFE QEREARSVDS AIVALRRHTM 350
NVLDAEMEKV RARHGCTAAA EEVEFALRRM VKQLLHVPTV RARELASNGQ 400
QEQYIAALDA LYGITVEQPA AAPAAECPVD HGRAGQAPAD VRRETA 446
Length:446
Mass (Da):46,394
Last modified:May 20, 2008 - v2
Checksum:iE50D8052A049F03E
GO

Sequence cautioni

The sequence ABK04152.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000454 Genomic DNA. Translation: ABK04152.1. Different initiation.
RefSeqiWP_011692613.1. NC_008541.1.
YP_832252.1. NC_008541.1.

Genome annotation databases

EnsemblBacteriaiABK04152; ABK04152; Arth_2773.
GeneIDi4444572.
KEGGiart:Arth_2773.
PATRICi21000939. VBIArtSp72239_3153.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000454 Genomic DNA. Translation: ABK04152.1 . Different initiation.
RefSeqi WP_011692613.1. NC_008541.1.
YP_832252.1. NC_008541.1.

3D structure databases

ProteinModelPortali A0JYN2.
ModBasei Search...

Protein-protein interaction databases

STRINGi 290399.Arth_2773.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABK04152 ; ABK04152 ; Arth_2773 .
GeneIDi 4444572.
KEGGi art:Arth_2773.
PATRICi 21000939. VBIArtSp72239_3153.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109649.
KOi K02492.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci ASP290399:GHIF-2839-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: FB24.

Entry informationi

Entry nameiHEM1_ARTS2
AccessioniPrimary (citable) accession number: A0JYN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: September 3, 2014
This is version 67 of the entry and version 2 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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