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C5BSZ7

- HEM1_TERTT

UniProt

C5BSZ7 - HEM1_TERTT

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Protein

Glutamyl-tRNA reductase

Gene
hemA, TERTU_3845
Organism
Teredinibacter turnerae (strain ATCC 39867 / T7901)
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
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. 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

BioCyciTTUR377629:GHSU-3486-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:TERTU_3845
OrganismiTeredinibacter turnerae (strain ATCC 39867 / T7901)
Taxonomic identifieri377629 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadales genera incertae sedisTeredinibacter
ProteomesiUP000009080: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 415415Glutamyl-tRNA reductaseUniRule annotationPRO_1000202648Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi377629.TERTU_3845.

Structurei

3D structure databases

ProteinModelPortaliC5BSZ7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate 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.
HOGENOMiHOG000109650.
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.

C5BSZ7-1 [UniParc]FASTAAdd to Basket

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MTLLALGINH NTATLDVREK VAFSPAELEV ALCALRESGL AEEVAILSTC    50
NRTEIYCETG AEAQHLLVWL AEHKAASAQE LQHAHYARWG DDAARHMMAV 100
ASGLDSLVLG EPQILGQMKS CYAVAREAGV LGRGLHDAFQ RVFAVAKRVR 150
SETAIGENPV SVAYAAVSLA QQIFSDLKQD TALLIGAGET IELVARHLKN 200
QGIKKLIVAN RTLENAHALA KEFAAEAILL ADIPEYLPTA DIVISSTASQ 250
LPLLGKGAVE VALKKRKHKP MFMVDIAVPR DIEPQVGDLA DVYLFTVDDL 300
KEVIDENKKS REEAAKTART IIDEGVERYQ LDQRALSAVE LVKDFRQQTE 350
AVRDQEVQKA LNALRSGADP EELLLTLSRN LTNKFMHQPT TALKRASSEG 400
REQLLQDFKS LFGLD 415
Length:415
Mass (Da):45,460
Last modified:July 28, 2009 - v1
Checksum:i1D364AB2607CC17C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001614 Genomic DNA. Translation: ACR14420.1.
RefSeqiYP_003075142.1. NC_012997.1.

Genome annotation databases

EnsemblBacteriaiACR14420; ACR14420; TERTU_3845.
GeneIDi8211329.
KEGGittu:TERTU_3845.
PATRICi23874533. VBITerTur118718_3590.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001614 Genomic DNA. Translation: ACR14420.1 .
RefSeqi YP_003075142.1. NC_012997.1.

3D structure databases

ProteinModelPortali C5BSZ7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 377629.TERTU_3845.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACR14420 ; ACR14420 ; TERTU_3845 .
GeneIDi 8211329.
KEGGi ttu:TERTU_3845.
PATRICi 23874533. VBITerTur118718_3590.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci TTUR377629:GHSU-3486-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: ATCC 39867 / T7901.

Entry informationi

Entry nameiHEM1_TERTT
AccessioniPrimary (citable) accession number: C5BSZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: September 3, 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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