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Q0VS78

- HEM1_ALCBS

UniProt

Q0VS78 - HEM1_ALCBS

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Protein

Glutamyl-tRNA reductase

Gene
hemA, ABO_0522
Organism
Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573)
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

BioCyciABOR393595:GHRI-539-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:ABO_0522
OrganismiAlcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573)
Taxonomic identifieri393595 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesAlcanivoracaceaeAlcanivorax
ProteomesiUP000008871: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418Glutamyl-tRNA reductaseUniRule annotationPRO_1000004590Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi393595.ABO_0522.

Structurei

3D structure databases

ProteinModelPortaliQ0VS78.

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.

Q0VS78-1 [UniParc]FASTAAdd to Basket

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MNLVAVGVNH TTADVELRER LAFSTQQAEV ALASLREMPG VREAALLSTC    50
NRTELYCLTD DVTPNFAQWL ASSRNLSVER LSTVLYQHTG EQALEHMMRV 100
AGGLDSLVLG EPQILGQMRE AYARAHEAGL LNGELSRLFQ EVFSVAKRIR 150
TETGIGANPV SVAYAAVSFA RHIFADLKKS RALLIGAGEM IELVARHLSE 200
QQVQEITIAN RTQERASELA AAVGGRGISL EELPVALERA DILISCTAAP 250
LPIMGKGMVE RALKKRRHRP MFMVDIAVPR DIEPEVGELG DVYLYTVDHL 300
QEAIQENVRS RQQAAQEASE LIRDAIVRHR RQRREQDAVK VLRDYREQRK 350
AMAESELEKA LQQLRNGGDA EQVLRRFQHS LVNKWLHSPS VTLRKMAADG 400
RAEALLLARE LLLDDDQS 418
Length:418
Mass (Da):46,630
Last modified:September 5, 2006 - v1
Checksum:i09415E69BADCE528
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM286690 Genomic DNA. Translation: CAL15970.1.
RefSeqiYP_692242.1. NC_008260.1.

Genome annotation databases

EnsemblBacteriaiCAL15970; CAL15970; ABO_0522.
GeneIDi4212665.
KEGGiabo:ABO_0522.
PATRICi20838687. VBIAlcBor124741_0544.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM286690 Genomic DNA. Translation: CAL15970.1 .
RefSeqi YP_692242.1. NC_008260.1.

3D structure databases

ProteinModelPortali Q0VS78.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 393595.ABO_0522.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAL15970 ; CAL15970 ; ABO_0522 .
GeneIDi 4212665.
KEGGi abo:ABO_0522.
PATRICi 20838687. VBIAlcBor124741_0544.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci ABOR393595:GHRI-539-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: SK2 / ATCC 700651 / DSM 11573.

Entry informationi

Entry nameiHEM1_ALCBS
AccessioniPrimary (citable) accession number: Q0VS78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: September 3, 2014
This is version 71 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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