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P28463

- HEM1_SYNY3

UniProt

P28463 - HEM1_SYNY3

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).1 Publication

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

Enzyme regulationi

Feedback inhibition by heme.

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 bindingi188 – 1936NADPUniRule 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:slr1808
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
ProteomesiUP000001425: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427Glutamyl-tRNA reductasePRO_0000114079Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi1148.slr1808.

Structurei

3D structure databases

ProteinModelPortaliP28463.
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.
InParanoidiP28463.
OMAiAITCGKK.
PhylomeDBiP28463.

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.

P28463-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNIAVVGLSH KTAPVEIREK LSIQEAKLEE ALTHLRSYPH IEEVTVISTC
60 70 80 90 100
NRLEIYAVVT DTEKGVVEIT QFLSETGNIP LATLRRYLFT LLHEDAVRHL
110 120 130 140 150
MRVAAGLESL VLGEGQILAQ VRTTHKLGQK YKGVGRLLDR LFKQAITAGR
160 170 180 190 200
RVRTETDIGT GAVSISSAAV ELVHRQVDLS SQKTVIIGAG KMACLLVKHL
210 220 230 240 250
LAKGATDITI VNRSQRRSQD LANQFPQAQL TLCPLTDMFT AIAAGDIVFT
260 270 280 290 300
STGATEPILN CENLTGCVIN RKSLMLVDIS VPRNVAADVH AMEQVRAFNV
310 320 330 340 350
DDLKEVVAQN QASRRQMARQ AEALLEEEIA AFDLWWRSLE TVPTISSLRS
360 370 380 390 400
KVEDIREQEL EKALSRLGSE FAEKHQEVIE ALTRGIVNKI LHEPMVQLRA
410 420
QQDIEARKQC LRSLKMLFDL EVEEQFG
Length:427
Mass (Da):47,526
Last modified:December 1, 1992 - v1
Checksum:i5F5D9D744A900D7D
GO

Sequence cautioni

The sequence BAA17738.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84218 Genomic DNA. Translation: AAA27289.1.
X65963 Genomic DNA. Translation: CAA46779.1.
BA000022 Genomic DNA. Translation: BAA17738.1. Different initiation.
PIRiS77180.
RefSeqiYP_007450940.1. NC_020286.1.

Genome annotation databases

EnsemblBacteriaiBAA17738; BAA17738; BAA17738.
PATRICi23839406. VBISynSp132158_1267.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84218 Genomic DNA. Translation: AAA27289.1 .
X65963 Genomic DNA. Translation: CAA46779.1 .
BA000022 Genomic DNA. Translation: BAA17738.1 . Different initiation.
PIRi S77180.
RefSeqi YP_007450940.1. NC_020286.1.

3D structure databases

ProteinModelPortali P28463.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 1148.slr1808.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAA17738 ; BAA17738 ; BAA17738 .
PATRICi 23839406. VBISynSp132158_1267.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
InParanoidi P28463.
OMAi AITCGKK.
PhylomeDBi P28463.

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

« Hide 'large scale' publications
  1. "Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression."
    Verkamp E., Jahn M., Jahn D., Kumar A.M., Soell D.
    J. Biol. Chem. 267:8275-8280(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "Identification of a hemA gene from Synechocystis by complementation of an E. coli hemA mutant."
    Grimm B.
    Hereditas 117:195-197(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
    Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
    , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / Kazusa.

Entry informationi

Entry nameiHEM1_SYNY3
AccessioniPrimary (citable) accession number: P28463
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 26, 2014
This is version 120 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
  3. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

External Data

Dasty 3