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A5FLE3

- HEM11_FLAJ1

UniProt

A5FLE3 - HEM11_FLAJ1

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Protein
Glutamyl-tRNA reductase 1
Gene
hemA1, Fjoh_0942
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-963-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 1 (EC:1.2.1.70)
Short name:
GluTR 1
Gene namesi
Name:hemA1
Ordered Locus Names:Fjoh_0942
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 – 416416Glutamyl-tRNA reductase 1UniRule annotation
PRO_0000335032Add
BLAST

Proteomic databases

PRIDEiA5FLE3.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi376686.Fjoh_0942.

Structurei

3D structure databases

ProteinModelPortaliA5FLE3.

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.
OMAiSETNISC.
OrthoDBiEOG6QG8G0.

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.

A5FLE3-1 [UniParc]FASTAAdd to Basket

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MENNNVPKHL YFYSVGLSYK KADAEVRGQF SLDAVAKTRL LEQAKNDGIE    50
SLLVTSTCNR TEIYGFAEHP FQLIKLICDN SNGSVDAFQK VGFVYKNQEA 100
INHMFRVGTG LDSQILGDFE IISQIKTSFT HSKSMGLANA FMERLVNAVI 150
QASKRIKTET EISSGATSVS FASVQYILKN VEDISNKNIL LFGTGKIGRN 200
TCENLVKHTK NEHITLINRT KDKAEKLAGK LNLIVKDYSE LHLELQKADV 250
VVVATGAQNP TVDKAILNLK KPLLILDLSI PKNVNENVEE LEGVTLIHMD 300
YLSQLTDETL ENRKLHIPAA EAIIEEIKEE FVTWMKGRKF APTINALKEK 350
LNAIKASELD FQSKKIADFN EEQAEIISNR IIQKITTHFA NHLKDDDTMV 400
DESIEWIEKV FKIKAS 416
Length:416
Mass (Da):46,757
Last modified:June 12, 2007 - v1
Checksum:i3C213457520C9667
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000685 Genomic DNA. Translation: ABQ03976.1.
RefSeqiYP_001193295.1. NC_009441.1.

Genome annotation databases

EnsemblBacteriaiABQ03976; ABQ03976; Fjoh_0942.
GeneIDi5091356.
KEGGifjo:Fjoh_0942.
PATRICi21896167. VBIFlaJoh53613_0968.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000685 Genomic DNA. Translation: ABQ03976.1 .
RefSeqi YP_001193295.1. NC_009441.1.

3D structure databases

ProteinModelPortali A5FLE3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 376686.Fjoh_0942.

Proteomic databases

PRIDEi A5FLE3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ03976 ; ABQ03976 ; Fjoh_0942 .
GeneIDi 5091356.
KEGGi fjo:Fjoh_0942.
PATRICi 21896167. VBIFlaJoh53613_0968.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000251726.
KOi K02492.
OMAi SETNISC.
OrthoDBi EOG6QG8G0.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci FJOH376686:GIXN-963-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 nameiHEM11_FLAJ1
AccessioniPrimary (citable) accession number: A5FLE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: September 3, 2014
This is version 64 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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