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A1TTC3

- HEM1_ACIAC

UniProt

A1TTC3 - HEM1_ACIAC

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Aave_3663
Organism
Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli)
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 sitei56 – 561Nucleophile By similarity
Sitei103 – 1031Important for activity By similarity
Binding sitei113 – 1131Substrate By similarity
Binding sitei124 – 1241Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi193 – 1986NADP 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

BioCyciACIT397945:GI5W-3706-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:Aave_3663
OrganismiAcidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli)
Taxonomic identifieri397945 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax
ProteomesiUP000002596: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Glutamyl-tRNA reductaseUniRule annotation
PRO_0000335001Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi397945.Aave_3663.

Structurei

3D structure databases

ProteinModelPortaliA1TTC3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 584Substrate binding By similarity
Regioni118 – 1203Substrate 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.

A1TTC3-1 [UniParc]FASTAAdd to Basket

« Hide

MAVWALGINH TTAPLDLRGR FAFAIDQIAP TLQGLRQSLG GATRHPQVET    50
AILSTCNRTE IYCAGQQPAL DHTLDWLAHS GGVSPSLLRS HSYTLEESLV 100
ARHAFRVASG LDSMVLGEAQ ILGQMKDAVR AAETAGALGT TLNQLFQRSF 150
AVAKEVRTST EIGAHSISMA AAAVRLAGQL FEDLTEIRIL FVGAGEMIEL 200
AATHFAAKNP KSLAIANRTL ERGEKLASRF GGEVMRLADL PDRLHEFDAV 250
VSCTASSLPI IGLGAVERAL KKRRHRPMFM VDLAVPRDIE PEVKALEDIY 300
LYTVDDLASV VQTAQASRQA AVAQAEAIID AGVQSFMHWM DQRSPVGGVV 350
PLIQQIHAQA DEWRALEIAR AKKLIARGED MDAVLEALSR GLTQKMLHGT 400
LAELRAGDAD TRAQTAQTVS RLFLRSQSRS GL 432
Length:432
Mass (Da):46,734
Last modified:February 6, 2007 - v1
Checksum:iF1AF378B845BE924
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000512 Genomic DNA. Translation: ABM34211.1.
RefSeqiWP_011796705.1. NC_008752.1.
YP_971985.1. NC_008752.1.

Genome annotation databases

EnsemblBacteriaiABM34211; ABM34211; Aave_3663.
GeneIDi4665154.
KEGGiaav:Aave_3663.
PATRICi20682495. VBIAciCit38535_3716.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000512 Genomic DNA. Translation: ABM34211.1 .
RefSeqi WP_011796705.1. NC_008752.1.
YP_971985.1. NC_008752.1.

3D structure databases

ProteinModelPortali A1TTC3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 397945.Aave_3663.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM34211 ; ABM34211 ; Aave_3663 .
GeneIDi 4665154.
KEGGi aav:Aave_3663.
PATRICi 20682495. VBIAciCit38535_3716.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci ACIT397945:GI5W-3706-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. "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.
    , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AAC00-1.

Entry informationi

Entry nameiHEM1_ACIAC
AccessioniPrimary (citable) accession number: A1TTC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 6, 2007
Last modified: September 3, 2014
This is version 67 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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