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A0Q2B3

- HEM1_CLONN

UniProt

A0Q2B3 - HEM1_CLONN

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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 – 491NucleophileUniRule annotation
Sitei96 – 961Important for activityUniRule annotation
Binding sitei106 – 1061SubstrateUniRule annotation
Binding sitei117 – 1171SubstrateUniRule annotation

Regions

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

GO - Molecular functioni

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

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 reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
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 reductasePRO_1000057573Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi386415.NT01CX_0264.

Structurei

3D structure databases

ProteinModelPortaliA0Q2B3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Substrate bindingUniRule annotation
Regioni111 – 1133Substrate bindingUniRule annotation

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.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

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

        10         20         30         40         50
MNLAVIGINY NNTPIDIREK VSFSKSQKYK ACTYLIKKGI SEIIIVSTCN
60 70 80 90 100
RSEIYICSDE IDSHINEVVN FYKIFFNVES VNEYIFIKKD KEAVSHIYNV
110 120 130 140 150
SAGLDSMILG EDQILGQVKE ALRYSMENKF SRKVLNKLFR EAITSAKKIK
160 170 180 190 200
SELKISETPI SMVYIAIKLL EKNIGTLKGK KACIIGAGDM GRLALKHLIN
210 220 230 240 250
EELEEIFVAN RTYNNVIDLL KEFPKIKLID YEKKYEILDN VDILITATAA
260 270 280 290 300
PHLIIKKEQL QNIKQELYIM DLALPRDVEK SAGDIENIHL YDVDDFKNIS
310 320 330 340 350
DSNKIKREEL SLIAKDSIDS YVNEFNQWMK SLKVDNTIKD LNNRCRDIKD
360 370 380 390 400
EYLGYITKKI DLNERDKEIL EKMLFGALKK VVKEPILNLK ELKDEDEINK
410
YIKSVNELFK F
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.
RefSeqiWP_011722752.1. NC_008593.1.
YP_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 WP_011722752.1. NC_008593.1.
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: October 29, 2014
This is version 62 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.UniRule annotation

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