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Q0VS78

- HEM1_ALCBS

UniProt

Q0VS78 - HEM1_ALCBS

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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

BioCyciABOR393595:GHRI-539-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: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 reductasePRO_1000004590Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi393595.ABO_0522.

Structurei

3D structure databases

ProteinModelPortaliQ0VS78.
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.

Q0VS78-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNLVAVGVNH TTADVELRER LAFSTQQAEV ALASLREMPG VREAALLSTC
60 70 80 90 100
NRTELYCLTD DVTPNFAQWL ASSRNLSVER LSTVLYQHTG EQALEHMMRV
110 120 130 140 150
AGGLDSLVLG EPQILGQMRE AYARAHEAGL LNGELSRLFQ EVFSVAKRIR
160 170 180 190 200
TETGIGANPV SVAYAAVSFA RHIFADLKKS RALLIGAGEM IELVARHLSE
210 220 230 240 250
QQVQEITIAN RTQERASELA AAVGGRGISL EELPVALERA DILISCTAAP
260 270 280 290 300
LPIMGKGMVE RALKKRRHRP MFMVDIAVPR DIEPEVGELG DVYLYTVDHL
310 320 330 340 350
QEAIQENVRS RQQAAQEASE LIRDAIVRHR RQRREQDAVK VLRDYREQRK
360 370 380 390 400
AMAESELEKA LQQLRNGGDA EQVLRRFQHS LVNKWLHSPS VTLRKMAADG
410
RAEALLLARE LLLDDDQS
Length:418
Mass (Da):46,630
Last modified:September 5, 2006 - v1
Checksum:i09415E69BADCE528
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM286690 Genomic DNA. Translation: CAL15970.1.
RefSeqiWP_011587808.1. NC_008260.1.
YP_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:
EMBLi
GenBanki
DDBJi
Links Updated
AM286690 Genomic DNA. Translation: CAL15970.1 .
RefSeqi WP_011587808.1. NC_008260.1.
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: November 26, 2014
This is version 73 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