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A0Q2B3

- HEM1_CLONN

UniProt

A0Q2B3 - HEM1_CLONN

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Protein
Glutamyl-tRNA reductase
Gene
hemA, NT01CX_0264
Organism
Clostridium novyi (strain NT)
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 sitei49 – 491Nucleophile By similarity
Sitei96 – 961Important for activity By similarity
Binding sitei106 – 1061Substrate By similarity
Binding sitei117 – 1171Substrate 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

BioCyciCNOV386415:GH98-1830-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:NT01CX_0264
OrganismiClostridium novyi (strain NT)
Taxonomic identifieri386415 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000008220: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411Glutamyl-tRNA reductaseUniRule annotation
PRO_1000057573Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi386415.NT01CX_0264.

Structurei

3D structure databases

ProteinModelPortaliA0Q2B3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Substrate binding By similarity
Regioni111 – 1133Substrate 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.

A0Q2B3-1 [UniParc]FASTAAdd to Basket

« Hide

MNLAVIGINY NNTPIDIREK VSFSKSQKYK ACTYLIKKGI SEIIIVSTCN    50
RSEIYICSDE IDSHINEVVN FYKIFFNVES VNEYIFIKKD KEAVSHIYNV 100
SAGLDSMILG EDQILGQVKE ALRYSMENKF SRKVLNKLFR EAITSAKKIK 150
SELKISETPI SMVYIAIKLL EKNIGTLKGK KACIIGAGDM GRLALKHLIN 200
EELEEIFVAN RTYNNVIDLL KEFPKIKLID YEKKYEILDN VDILITATAA 250
PHLIIKKEQL QNIKQELYIM DLALPRDVEK SAGDIENIHL YDVDDFKNIS 300
DSNKIKREEL SLIAKDSIDS YVNEFNQWMK SLKVDNTIKD LNNRCRDIKD 350
EYLGYITKKI DLNERDKEIL EKMLFGALKK VVKEPILNLK ELKDEDEINK 400
YIKSVNELFK F 411
Length:411
Mass (Da):47,552
Last modified:January 9, 2007 - v1
Checksum:i73DD962E0BF8AB48
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000382 Genomic DNA. Translation: ABK60902.1.
RefSeqiYP_878765.1. NC_008593.1.

Genome annotation databases

EnsemblBacteriaiABK60902; ABK60902; NT01CX_0264.
GeneIDi4541260.
KEGGicno:NT01CX_0264.
PATRICi19481076. VBICloNov112828_1800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000382 Genomic DNA. Translation: ABK60902.1 .
RefSeqi YP_878765.1. NC_008593.1.

3D structure databases

ProteinModelPortali A0Q2B3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 386415.NT01CX_0264.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABK60902 ; ABK60902 ; NT01CX_0264 .
GeneIDi 4541260.
KEGGi cno:NT01CX_0264.
PATRICi 19481076. VBICloNov112828_1800.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CNOV386415:GH98-1830-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: NT.

Entry informationi

Entry nameiHEM1_CLONN
AccessioniPrimary (citable) accession number: A0Q2B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 9, 2007
Last modified: September 3, 2014
This is version 60 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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