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C5BSZ7

- HEM1_TERTT

UniProt

C5BSZ7 - HEM1_TERTT

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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 – 501NucleophileUniRule 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

BioCyciTTUR377629:GHSU-3486-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: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 reductasePRO_1000202648Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi377629.TERTU_3845.

Structurei

3D structure databases

ProteinModelPortaliC5BSZ7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

« Hide

        10         20         30         40         50
MTLLALGINH NTATLDVREK VAFSPAELEV ALCALRESGL AEEVAILSTC
60 70 80 90 100
NRTEIYCETG AEAQHLLVWL AEHKAASAQE LQHAHYARWG DDAARHMMAV
110 120 130 140 150
ASGLDSLVLG EPQILGQMKS CYAVAREAGV LGRGLHDAFQ RVFAVAKRVR
160 170 180 190 200
SETAIGENPV SVAYAAVSLA QQIFSDLKQD TALLIGAGET IELVARHLKN
210 220 230 240 250
QGIKKLIVAN RTLENAHALA KEFAAEAILL ADIPEYLPTA DIVISSTASQ
260 270 280 290 300
LPLLGKGAVE VALKKRKHKP MFMVDIAVPR DIEPQVGDLA DVYLFTVDDL
310 320 330 340 350
KEVIDENKKS REEAAKTART IIDEGVERYQ LDQRALSAVE LVKDFRQQTE
360 370 380 390 400
AVRDQEVQKA LNALRSGADP EELLLTLSRN LTNKFMHQPT TALKRASSEG
410
REQLLQDFKS LFGLD
Length:415
Mass (Da):45,460
Last modified:July 28, 2009 - v1
Checksum:i1D364AB2607CC17C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: October 1, 2014
This is version 44 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