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A5D3L4

- HEM1_PELTS

UniProt

A5D3L4 - HEM1_PELTS

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Protein
Glutamyl-tRNA reductase
Gene
hemA, PTH_0971
Organism
Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)
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. 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

BioCyciPTHE370438:GCGQ-1007-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:PTH_0971
OrganismiPelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)
Taxonomic identifieri370438 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaePelotomaculum
ProteomesiUP000006556: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Glutamyl-tRNA reductaseUniRule annotation
PRO_1000075416Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi370438.PTH_0971.

Structurei

3D structure databases

ProteinModelPortaliA5D3L4.

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.
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.

A5D3L4-1 [UniParc]FASTAAdd to Basket

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MLILVVGLNH RTAPVEVREK LSFSAKSLQG ALAQLKSYPV IEGCAILSTC    50
NRTEIYAATL EMDDGLNAIW DFLSRWSGVG ISEIKNFTYS HTLYDTIRHL 100
FRVAAGLDSM ILGETQILGQ VREAYQRAIE YESTNRVLNT LFQQAITVGK 150
RVRTETGIDR NAVSISYAAV ELARQHLGSL DGRSVLVIGA GKMSELTARH 200
LVANGVSSVI VSNRSFERAV ALAEQFRGRA VRFDELYRCM EAADIVISCT 250
AASHCVVKAE EVSRVMDKRR GRAIFMVDIA VPRDIEAEVG NLAGVTLFDI 300
DDLKNVIDQN LAERKQAAVK AEEIIEEELD GFMKWLGMQF VVPTISALKK 350
WGDEIKQKEL CRALNRLGNI SEHDRKVICS MANSIVNQIL HVPVAQLKSY 400
ALTTEGHLYT EILQNLFNLD VPGQKPKKQP APAGIKEPVL AKKG 444
Length:444
Mass (Da):49,167
Last modified:June 12, 2007 - v1
Checksum:iCE7874AB66E30749
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009389 Genomic DNA. Translation: BAF59152.1.
RefSeqiWP_012032142.1. NC_009454.1.
YP_001211521.1. NC_009454.1.

Genome annotation databases

EnsemblBacteriaiBAF59152; BAF59152; PTH_0971.
GeneIDi5140131.
KEGGipth:PTH_0971.
PATRICi22908973. VBIPelThe8413_1091.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009389 Genomic DNA. Translation: BAF59152.1 .
RefSeqi WP_012032142.1. NC_009454.1.
YP_001211521.1. NC_009454.1.

3D structure databases

ProteinModelPortali A5D3L4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 370438.PTH_0971.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAF59152 ; BAF59152 ; PTH_0971 .
GeneIDi 5140131.
KEGGi pth:PTH_0971.
PATRICi 22908973. VBIPelThe8413_1091.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci PTHE370438:GCGQ-1007-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. "The genome of Pelotomaculum thermopropionicum reveals niche-associated evolution in anaerobic microbiota."
    Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.
    Genome Res. 18:442-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 13744 / JCM 10971 / SI.

Entry informationi

Entry nameiHEM1_PELTS
AccessioniPrimary (citable) accession number: A5D3L4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: September 3, 2014
This is version 58 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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