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B8G2M3

- HEM1_DESHD

UniProt

B8G2M3 - HEM1_DESHD

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Protein

Glutamyl-tRNA reductase

Gene
hemA, Dhaf_3355
Organism
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
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
Sitei99 – 991Important for activity By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei120 – 1201Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADP By similarity

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

BioCyciDHAF272564:GCV8-3428-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:Dhaf_3355
OrganismiDesulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Taxonomic identifieri272564 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfitobacterium
ProteomesiUP000007726: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Glutamyl-tRNA reductaseUniRule annotationPRO_1000190519Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi272564.Dhaf_3355.

Structurei

3D structure databases

ProteinModelPortaliB8G2M3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni114 – 1163Substrate 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.
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.

B8G2M3-1 [UniParc]FASTAAdd to Basket

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MFPITIGLNH KTAPVEIREK VSFHPSEINK ALMELNELSA LNGIVLLSTC    50
NRLEIYAATP EVELGVSVIK KFLARHGKLR EEDINQYLYV HTLYDSVRHL 100
FRVVAGLDSM VMGETQILGQ VAEAYEKSSQ LNLSNKIIHA IFQNALAVGK 150
RVRSETQIDQ HPTSVSYTAV ELAKQTFGDV QGKSILILGA GEMSALTAKH 200
LVASGADTVL VSNRSMQRAQ ALAEEFSGRA IPYEELDTAL AEADIVISAT 250
AAAHFVIKPE RMRRVMEQRR QRALLLIDIA VPRDIHPNVG ELEGVTLFDI 300
DDLRGVVDSH QKAREEAALQ AGRILEEEMG RFVKWHNSLY VVPTIVALQR 350
RGEEVREIML KSALNKLGPI DEKQEKIIRS MANSIVTHLL HAPIANLKEA 400
ANTSQGHLYT EILQNLFDLD GNELSPHAGW SVHHAASHHS NQG 443
Length:443
Mass (Da):49,112
Last modified:March 3, 2009 - v1
Checksum:i291F27415A7B1C5A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001336 Genomic DNA. Translation: ACL21373.1.
RefSeqiYP_002459809.1. NC_011830.1.

Genome annotation databases

EnsemblBacteriaiACL21373; ACL21373; Dhaf_3355.
GeneIDi7260372.
KEGGidhd:Dhaf_3355.
PATRICi21664671. VBIDesHaf15223_3495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001336 Genomic DNA. Translation: ACL21373.1 .
RefSeqi YP_002459809.1. NC_011830.1.

3D structure databases

ProteinModelPortali B8G2M3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272564.Dhaf_3355.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACL21373 ; ACL21373 ; Dhaf_3355 .
GeneIDi 7260372.
KEGGi dhd:Dhaf_3355.
PATRICi 21664671. VBIDesHaf15223_3495.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci DHAF272564:GCV8-3428-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. "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive anaerobe capable of dehalogenation and metal reduction."
    Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L., Tiedje J.M.
    BMC Microbiol. 12:21-21(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DCB-2 / DSM 10664.

Entry informationi

Entry nameiHEM1_DESHD
AccessioniPrimary (citable) accession number: B8G2M3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 43 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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