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B2IA84

- HEM1_XYLF2

UniProt

B2IA84 - HEM1_XYLF2

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Protein
Glutamyl-tRNA reductase
Gene
hemA, XfasM23_2122
Organism
Xylella fastidiosa (strain M23)
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 sitei50 – 501Nucleophile By similarity
Sitei91 – 911Important for activity By similarity
Binding sitei101 – 1011Substrate By similarity
Binding sitei112 – 1121Substrate 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

BioCyciXFAS405441:GJJI-2172-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:XfasM23_2122
OrganismiXylella fastidiosa (strain M23)
Taxonomic identifieri405441 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella
ProteomesiUP000001698: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Glutamyl-tRNA reductaseUniRule annotation
PRO_1000093179Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi405441.XfasM23_2122.

Structurei

3D structure databases

ProteinModelPortaliB2IA84.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni106 – 1083Substrate 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.
HOGENOMiHOG000109650.
KOiK02492.
OMAiLAHKLTN.
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.

B2IA84-1 [UniParc]FASTAAdd to Basket

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MTLWVLGLNH QTAPMELRER ASFVGDALPR ALDSLRNLPN VNEAALLSTC    50
NRTELYAETT NAQMLLNWLE QHRPGLQNHL YQYRDAAAVR HLFRVATGLD 100
SMVLGESQIL GQVKDSWSMA RTHGTLGNTL DRLFQHSFSV AKHARTNTRI 150
GTNPVSIAST AVRLAQDAFS PLNESTVLLI GAGETIQLAA KHLSEGRVQR 200
LLIANRTHAK AQMLASQHGG YALPLTELNL HLAEADIIFS ATAAPTPIVT 250
QSNVESALHI RKRKPILLFD LAIPRDIETE VGTLTDAYLY TIDDLERAVE 300
ENRHSRREAA ETAEAIIELQ VKRYMDTLQA QAHQAPLRRL RTFGTTTRDE 350
LLTRARRQLA NGRPAEEVLE QLAHGLTNRL LHPPTAALRE AALANNTELV 400
RAAEQLFPEK PGYHHPTLQT TIVKTDETDP AS 432
Length:432
Mass (Da):47,966
Last modified:June 10, 2008 - v1
Checksum:i7335D2E946015C84
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001011 Genomic DNA. Translation: ACB93520.1.
RefSeqiYP_001830794.1. NC_010577.1.

Genome annotation databases

EnsemblBacteriaiACB93520; ACB93520; XfasM23_2122.
GeneIDi6203196.
KEGGixfn:XfasM23_2122.
PATRICi24146967. VBIXylFas85937_2636.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001011 Genomic DNA. Translation: ACB93520.1 .
RefSeqi YP_001830794.1. NC_010577.1.

3D structure databases

ProteinModelPortali B2IA84.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 405441.XfasM23_2122.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACB93520 ; ACB93520 ; XfasM23_2122 .
GeneIDi 6203196.
KEGGi xfn:XfasM23_2122.
PATRICi 24146967. VBIXylFas85937_2636.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci XFAS405441:GJJI-2172-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. "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23) causing almond leaf scorch disease in California."
    Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.
    J. Bacteriol. 192:4534-4534(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: M23.

Entry informationi

Entry nameiHEM1_XYLF2
AccessioniPrimary (citable) accession number: B2IA84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: September 3, 2014
This is version 49 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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