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A5FDF9

- HEM12_FLAJ1

UniProt

A5FDF9 - HEM12_FLAJ1

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Protein
Glutamyl-tRNA reductase 2
Gene
hemA2, Fjoh_3752
Organism
Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) (Cytophaga johnsonae)
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 sitei58 – 581Nucleophile By similarity
Sitei103 – 1031Important for activity By similarity
Binding sitei113 – 1131Substrate By similarity
Binding sitei124 – 1241Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi193 – 1986NADP 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

BioCyciFJOH376686:GIXN-3818-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 2 (EC:1.2.1.70)
Short name:
GluTR 2
Gene namesi
Name:hemA2
Ordered Locus Names:Fjoh_3752
OrganismiFlavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) (Cytophaga johnsonae)
Taxonomic identifieri376686 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeFlavobacterium
ProteomesiUP000006694: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Glutamyl-tRNA reductase 2UniRule annotation
PRO_0000335033Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi376686.Fjoh_3752.

Structurei

3D structure databases

ProteinModelPortaliA5FDF9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 604Substrate binding By similarity
Regioni118 – 1203Substrate 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.
HOGENOMiHOG000251726.
KOiK02492.
OMAiKMLHGTM.
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.

A5FDF9-1 [UniParc]FASTAAdd to Basket

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MENFNMPRST TFYALGLSYK KADAVIRGKF SLDAQAQSDL LLQAKAEGIE    50
SLVVTSTCNR TEIYGFAHHP YELIKLLCEN SNGSIEEFQQ AAYIYKNEEA 100
VSHMFRVGTG LDSQILGDFE IISQIKTAFN NSKQEGLVNT FLDRLVNTVI 150
QASKKVKTET KISSGATSVS FASVQYIIRN VADIGSKNIL LFGTGKIGRN 200
TCENLVKHTK NSHITLINRT KNKAELLAGK LNVIVKDYAD LKQELHQADV 250
LVVATGAQNP TIDKASLALQ KPLLILDLSI PRNVDANVEE IPGVTLIHLD 300
ALSQITDDTL ERRKQHIPAA EAIIDDMKLE LNTWVNGRKC APTIHALKSK 350
LNDIVSAEFA FQKKKITHFD DAQMDLISSR IIQKLTNHFA SHLKNENTSV 400
DQSIEFIEKI FQIGQLAPNK TSSPIADKYK INLS 434
Length:434
Mass (Da):48,167
Last modified:June 12, 2007 - v1
Checksum:i0B3355EF5113ACFF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000685 Genomic DNA. Translation: ABQ06765.1.
RefSeqiWP_012025731.1. NC_009441.1.
YP_001196084.1. NC_009441.1.

Genome annotation databases

EnsemblBacteriaiABQ06765; ABQ06765; Fjoh_3752.
GeneIDi5089786.
KEGGifjo:Fjoh_3752.
PATRICi21902079. VBIFlaJoh53613_3882.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000685 Genomic DNA. Translation: ABQ06765.1 .
RefSeqi WP_012025731.1. NC_009441.1.
YP_001196084.1. NC_009441.1.

3D structure databases

ProteinModelPortali A5FDF9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 376686.Fjoh_3752.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ06765 ; ABQ06765 ; Fjoh_3752 .
GeneIDi 5089786.
KEGGi fjo:Fjoh_3752.
PATRICi 21902079. VBIFlaJoh53613_3882.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000251726.
KOi K02492.
OMAi KMLHGTM.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci FJOH376686:GIXN-3818-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. "Novel features of the polysaccharide-digesting gliding bacterium Flavobacterium johnsoniae as revealed by genome sequence analysis."
    McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G., Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R., Cheng Y.Q., Stein J.L.
    Appl. Environ. Microbiol. 75:6864-6875(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17061 / DSM 2064 / UW101.

Entry informationi

Entry nameiHEM12_FLAJ1
AccessioniPrimary (citable) accession number: A5FDF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: September 3, 2014
This is version 63 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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