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A5GLB0

- HEM1_SYNPW

UniProt

A5GLB0 - HEM1_SYNPW

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Synechococcus sp. (strain WH7803)
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
Sitei99 – 991Important for activityUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation
Binding sitei120 – 1201SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi198 – 2036NADPUniRule annotation

GO - Molecular functioni

  1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
  2. NADP binding Source: InterPro

GO - Biological processi

  1. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
UPA00668.

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:SynWH7803_1299
OrganismiSynechococcus sp. (strain WH7803)
Taxonomic identifieri32051 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001566: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 438438Glutamyl-tRNA reductasePRO_1000004711Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi32051.SynWH7803_1299.

Structurei

3D structure databases

ProteinModelPortaliA5GLB0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni114 – 1163Substrate 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.
HOGENOMiHOG000109651.
KOiK02492.
OMAiGLSIHTT.
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.

A5GLB0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHIAVVGLSH RTAPVEVREK LSIPEQTMEE SLQNLRGHDQ VLEASILSTC
60 70 80 90 100
NRLEIYTLVR NPELGISAVR EFLSSHSGLE TGDLKPHLFA YHHEDAVGHL
110 120 130 140 150
LRVAAGLDSL VLGEGQILSQ VKKMMRLGQE HKSLGPILNR LLTQAVSTGK
160 170 180 190 200
RVRSETNLGT GAVSISSAAV ELAQLKLGQS RGLDELVTLE DEQVAVVGAG
210 220 230 240 250
RMSRLLLQHL QAKGASGVVV LNRTVARAEA LAADFPTLPV QCRPLKDLDH
260 270 280 290 300
CLSTCSLIFT STAADDPIID AERLSKLNRR SSLRLIDIGV PRNIAADVEG
310 320 330 340 350
IGGVDAHDVD DLKEVVERNQ EARQQVAREA QGLLDGEARQ FLEWWDSLEA
360 370 380 390 400
VPTINRLRSS MESIRSEELM KALSRMGPDF SARERKVVEA LSKGIINKIL
410 420 430
HTPVTALRSP QPRSDRQNAL SVVERLFDLQ ADEDSVQN
Length:438
Mass (Da):48,011
Last modified:June 12, 2007 - v1
Checksum:iE1DC6427527CD9F1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CT971583 Genomic DNA. Translation: CAK23725.1.
RefSeqiWP_011933204.1. NC_009481.1.
YP_001225022.1. NC_009481.1.

Genome annotation databases

EnsemblBacteriaiCAK23725; CAK23725; SynWH7803_1299.
GeneIDi5145979.
KEGGisyx:SynWH7803_1299.
PATRICi23828742. VBISynSp43824_1332.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CT971583 Genomic DNA. Translation: CAK23725.1 .
RefSeqi WP_011933204.1. NC_009481.1.
YP_001225022.1. NC_009481.1.

3D structure databases

ProteinModelPortali A5GLB0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 32051.SynWH7803_1299.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAK23725 ; CAK23725 ; SynWH7803_1299 .
GeneIDi 5145979.
KEGGi syx:SynWH7803_1299.
PATRICi 23828742. VBISynSp43824_1332.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi GLSIHTT.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
UPA00668 .

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. Genoscope
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: WH7803.

Entry informationi

Entry nameiHEM1_SYNPW
AccessioniPrimary (citable) accession number: A5GLB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: October 1, 2014
This is version 59 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