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Q9PHX2

- HEM1_CAMJE

UniProt

Q9PHX2 - HEM1_CAMJE

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Cj0542
Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
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
Sitei97 – 971Important for activity By similarity
Binding sitei107 – 1071Substrate By similarity
Binding sitei118 – 1181Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi186 – 1916NADP 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

BioCyciCJEJ192222:GJTS-526-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:Cj0542
OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Taxonomic identifieri192222 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
ProteomesiUP000000799: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114002Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

IntActiQ9PHX2. 80 interactions.
STRINGi192222.Cj0542.

Structurei

3D structure databases

ProteinModelPortaliQ9PHX2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni112 – 1143Substrate 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.
HOGENOMiHOG000109651.
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.

Q9PHX2-1 [UniParc]FASTAAdd to Basket

« Hide

MYYCISFTHK NTDIALREKL SFSNEAKKGE FLKIISTHEN IEECLVISTC    50
NRVEIVAFVK MACAEFIVKS LALLCDVDKD ILLEKADIFE DSGAIHHLFS 100
VASSLDSLVV GETQIAGQLK DAFAFAVKNN FCGVHLSRAV HSAFKCAAKV 150
RNETQISKNS ISVASVAVAK AKELADLTQK KAVVIGAGEM GELAAKHLIA 200
AGAKVIILNR DLQKAKDLCE RLGVLSEYDS LENLKKYLNQ YEFFFSATNA 250
PNAIITNSLI EELSYKRYFF DIAVPRDIDI NENENISVFA VDDLEIVVQK 300
NLALREQEAR MAYGIIGRET SEFFRYLNDL ALMPIIKAIR LQAKEYADKQ 350
LEIALKKGYL KKSDKEEARK LIHQVFKAFL HTPTVNLKHL QGKMQSDTVI 400
NAMRYVFDLQ NNLEGLNQYK CEFDMENNDE IY 432
Length:432
Mass (Da):48,697
Last modified:October 1, 2000 - v1
Checksum:i5BB55DF90CBA3F22
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL111168 Genomic DNA. Translation: CAL34688.1.
PIRiF81400.
RefSeqiYP_002343973.1. NC_002163.1.

Genome annotation databases

EnsemblBacteriaiCAL34688; CAL34688; Cj0542.
GeneIDi904868.
KEGGicje:Cj0542.
PATRICi20058024. VBICamJej33762_0534.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL111168 Genomic DNA. Translation: CAL34688.1 .
PIRi F81400.
RefSeqi YP_002343973.1. NC_002163.1.

3D structure databases

ProteinModelPortali Q9PHX2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9PHX2. 80 interactions.
STRINGi 192222.Cj0542.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAL34688 ; CAL34688 ; Cj0542 .
GeneIDi 904868.
KEGGi cje:Cj0542.
PATRICi 20058024. VBICamJej33762_0534.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CJEJ192222:GJTS-526-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCTC 11168.

Entry informationi

Entry nameiHEM1_CAMJE
AccessioniPrimary (citable) accession number: Q9PHX2
Secondary accession number(s): Q0PAX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: October 1, 2000
Last modified: September 3, 2014
This is version 98 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, Reference 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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