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A9WPH1

- HEM1_RENSM

UniProt

A9WPH1 - HEM1_RENSM

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Protein
Glutamyl-tRNA reductase
Gene
hemA, RSal33209_1218
Organism
Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235)
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 sitei41 – 411Nucleophile By similarity
Sitei90 – 901Important for activity By similarity
Binding sitei100 – 1001Substrate By similarity
Binding sitei111 – 1111Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi181 – 1866NADP 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

BioCyciRSAL288705:GHX1-1218-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:RSal33209_1218
OrganismiRenibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235)
Taxonomic identifieri288705 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeRenibacterium
ProteomesiUP000002007: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Glutamyl-tRNA reductaseUniRule annotation
PRO_0000335064Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi288705.RSal33209_1218.

Structurei

3D structure databases

ProteinModelPortaliA9WPH1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 434Substrate binding By similarity
Regioni105 – 1073Substrate 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.
OMAiPYLYVHY.

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.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A9WPH1-1 [UniParc]FASTAAdd to Basket

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MNVVVLFSLV ATHADIDLET VARLSAGSAA VSTSTVVLAT CNRFEIYSAA    50
ENPATARAEM EAALAHATGF APSLVSSSFK LLTGTDVAKH LFAVASGLDS 100
AVVGEREIAG QVRRALIDAQ TAFPVPGPLV RLFQTASRTA KDVGSQTALG 150
SQGRSIVSVA LDLAGDSSAT AWDQRKAVVF GTGAYAGVTM ALLRERGVSD 200
LSVYSSSGRA ADFVASRGGT AAESLEEALG SADLVIGCSG SDQRVSAETL 250
ADIRRRTGTA GEPLSVIDLA LSRDFDPAIT ELPGVELLTL ETVRLAAPSE 300
QESALLQTQV IVSRAAADFE LSIATRSVDT AIVALRKHTM AVLDAEMERV 350
RAQHGCTAAA EEVEFALRRM VKQLLHGPTV RARELAAAGQ QAEYIAALQS 400
LYGIELESPT PAAQPVESIP AVEPASCPVN HNAVDRSQSA 440
Length:440
Mass (Da):45,781
Last modified:February 5, 2008 - v1
Checksum:iD97066F78C188072
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000910 Genomic DNA. Translation: ABY22956.1.
RefSeqiWP_012244642.1. NC_010168.1.
YP_001624370.1. NC_010168.1.

Genome annotation databases

EnsemblBacteriaiABY22956; ABY22956; RSal33209_1218.
GeneIDi5822473.
KEGGirsa:RSal33209_1218.
PATRICi23075677. VBIRenSal21953_1259.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000910 Genomic DNA. Translation: ABY22956.1 .
RefSeqi WP_012244642.1. NC_010168.1.
YP_001624370.1. NC_010168.1.

3D structure databases

ProteinModelPortali A9WPH1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 288705.RSal33209_1218.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABY22956 ; ABY22956 ; RSal33209_1218 .
GeneIDi 5822473.
KEGGi rsa:RSal33209_1218.
PATRICi 23075677. VBIRenSal21953_1259.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109649.
KOi K02492.
OMAi PYLYVHY.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci RSAL288705:GHX1-1218-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.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests reductive evolution away from an environmental Arthrobacter ancestor."
    Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.
    J. Bacteriol. 190:6970-6982(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235.

Entry informationi

Entry nameiHEM1_RENSM
AccessioniPrimary (citable) accession number: A9WPH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: September 3, 2014
This is version 53 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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