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Q11Y93

- HEM1_CYTH3

UniProt

Q11Y93 - HEM1_CYTH3

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Protein
Glutamyl-tRNA reductase
Gene
hemA, CHU_0333
Organism
Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469)
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 sitei52 – 521Nucleophile By similarity
Sitei101 – 1011Important for activity By similarity
Binding sitei111 – 1111Substrate By similarity
Binding sitei122 – 1221Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi191 – 1966NADP By similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
Complete GO annotation...

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

BioCyciCHUT269798:GJ83-343-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:CHU_0333
OrganismiCytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469)
Taxonomic identifieri269798 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesCytophagiaCytophagalesCytophagaceaeCytophaga
ProteomesiUP000001822: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 425425Glutamyl-tRNA reductaseUniRule annotation
PRO_0000335025Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi269798.CHU_0333.

Structurei

3D structure databases

ProteinModelPortaliQ11Y93.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 544Substrate binding By similarity
Regioni116 – 1183Substrate 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.
HOGENOMiHOG000109637.
KOiK02492.
OMAiVANGVHR.
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.
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.

Sequencei

Sequence statusi: Complete.

Q11Y93-1 [UniParc]FASTAAdd to Basket

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MISNFKSISL TYRKAPLEIR ERVALNEAEC KSLMLRIKDF TDTAELLILS    50
TCNRTEIYYT SNEDYSNDII KLLGVEKNIT GLIQQKEYFE IYNEQADAVL 100
HLFEVGIGLD SQVVGDMQIV NQVKYAYQWS ADLNLAGPFL HRLMHTIFFT 150
NKRVVQETAF RDGAASVSYA TVELSEELLS ATPNANILIV GLGEIGADVC 200
RNFKANTSFK NITLTNRSPL KSEALAAECG IEHVPFETLW EAVAKADLVI 250
SSVAKEEPLF TKEEIQKLSI LSHKYFIDLS VPRSVDARAE ELPGIIVYDI 300
DHIQNRSNEA LENRLNAIPH VRKIILDSIV EFNEWSKEME VSPTINKLKN 350
ALEQIRKEEL SRFVKQLSDE EAKKVDEITK SIMQKIIKLP VLQLKAACKR 400
GEAETLIDVL NDLFNLDKQP EQIRD 425
Length:425
Mass (Da):48,224
Last modified:August 22, 2006 - v1
Checksum:iFFB74CC964E8F1FA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000383 Genomic DNA. Translation: ABG57623.1.
RefSeqiYP_676963.1. NC_008255.1.

Genome annotation databases

EnsemblBacteriaiABG57623; ABG57623; CHU_0333.
GeneIDi4185515.
KEGGichu:CHU_0333.
PATRICi21591493. VBICytHut34013_0324.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000383 Genomic DNA. Translation: ABG57623.1 .
RefSeqi YP_676963.1. NC_008255.1.

3D structure databases

ProteinModelPortali Q11Y93.
ModBasei Search...

Protein-protein interaction databases

STRINGi 269798.CHU_0333.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABG57623 ; ABG57623 ; CHU_0333 .
GeneIDi 4185515.
KEGGi chu:CHU_0333.
PATRICi 21591493. VBICytHut34013_0324.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109637.
KOi K02492.
OMAi VANGVHR.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CHUT269798:GJ83-343-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.
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.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33406 / NCIMB 9469.

Entry informationi

Entry nameiHEM1_CYTH3
AccessioniPrimary (citable) accession number: Q11Y93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 22, 2006
Last modified: May 14, 2014
This is version 69 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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