Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A0JYN2

- HEM1_ARTS2

UniProt

A0JYN2 - HEM1_ARTS2

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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 – 481NucleophileUniRule annotation
Sitei100 – 1001Important for activityUniRule annotation
Binding sitei110 – 1101SubstrateUniRule annotation
Binding sitei121 – 1211SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi192 – 1976NADPUniRule 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

BioCyciASP290399:GHIF-2839-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: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 reductasePRO_0000335010Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi290399.Arth_2773.

Structurei

3D structure databases

ProteinModelPortaliA0JYN2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate bindingUniRule annotation
Regioni115 – 1173Substrate 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.
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

« Hide

        10         20         30         40         50
MVLFSLVATH ADIDLETVAQ LSTGASELAT SALSGSPAVK GAVVLATCNR
60 70 80 90 100
FEIYGEAPHP DDVEAARAAL VAQISERTGL NEQLVSRSFN TRTGGEVSQH
110 120 130 140 150
LFAVSSGLDS AVVGEREIAG QVRRALINAQ HEGTASSGLV RLFQAASKTA
160 170 180 190 200
KDVGAQTALG SRGLSIVSVA LDLATDLSEN PDWSAKKAVV FGTGAYAGAT
210 220 230 240 250
MSLLRERGCT DISVFSSSGR AEGFVATRGG KALDSDTLPA AVAAADVMIG
260 270 280 290 300
CSGSDTRVEA EELARVRAGS AQTLIAIDLA LTHDFDPAVG ELDGVELLTL
310 320 330 340 350
ESVRLAAPQE QAESLAQASG IVTGAAAAFE QEREARSVDS AIVALRRHTM
360 370 380 390 400
NVLDAEMEKV RARHGCTAAA EEVEFALRRM VKQLLHVPTV RARELASNGQ
410 420 430 440
QEQYIAALDA LYGITVEQPA AAPAAECPVD HGRAGQAPAD VRRETA
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. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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...
MobiDBi 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: October 1, 2014
This is version 68 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.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