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A1SE01

- HEM11_NOCSJ

UniProt

A1SE01 - HEM11_NOCSJ

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Protein

Glutamyl-tRNA reductase 1

Gene

hemA1

Organism
Nocardioides sp. (strain BAA-499 / JS614)
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 bindingi189 – 1946NADPUniRule 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

BioCyciNSP196162:GH4V-505-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 1UniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTR 1UniRule annotation
Gene namesi
Name:hemA1UniRule annotation
Ordered Locus Names:Noca_0494
OrganismiNocardioides sp. (strain BAA-499 / JS614)
Taxonomic identifieri196162 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaeNocardioidaceaeNocardioides
ProteomesiUP000000640: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Glutamyl-tRNA reductase 1PRO_0000335055Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi196162.Noca_0494.

Structurei

3D structure databases

ProteinModelPortaliA1SE01.
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.
HOGENOMiHOG000109649.
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.
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.

Sequencei

Sequence statusi: Complete.

A1SE01-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVLVVGISH KSAPVALLEQ LALDGPGLHK LIDDVAASEH VTEATVIATC
60 70 80 90 100
NRLEIYAEVD RFHGSVEEVS RLVVDRAGER TEAMLPHLYV HYDDGAVSHL
110 120 130 140 150
FQVVAGLDSM AVGEGQILGQ TRAALNAGQE IGTVGPALNV LFQQALRVGK
160 170 180 190 200
RARAETGIDR AAPSLVSAAL DRSRATVGEL SGKRVLVVGA GSMAGLATST
210 220 230 240 250
VAARGTASVT VVNRTSGNAD RLAEEYGARS ATLAELAAEL AVADVVISCT
260 270 280 290 300
GATGTLITRD MVAAATVDGR ELSILDLALP HDVDPTVADL PGVSLVGLTD
310 320 330 340 350
LADELRDSDA GQEVEAVRQI VTQEVAAFLS ARRQASVTPT VVALRSMATS
360 370 380 390 400
VVEAEMERLT SRVPGLDDDI RAEVLHTVRR VADKLLHQPT VRVRELANET
410 420 430
GAVSYAAALA ELFALDQEAV DAVTRPEGLT
Length:430
Mass (Da):44,973
Last modified:February 6, 2007 - v1
Checksum:i206566D654A5AD26
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000509 Genomic DNA. Translation: ABL80036.1.
RefSeqiWP_011753986.1. NC_008699.1.
YP_921723.1. NC_008699.1.

Genome annotation databases

EnsemblBacteriaiABL80036; ABL80036; Noca_0494.
GeneIDi4597393.
KEGGinca:Noca_0494.
PATRICi22743003. VBINocSp122728_0767.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000509 Genomic DNA. Translation: ABL80036.1 .
RefSeqi WP_011753986.1. NC_008699.1.
YP_921723.1. NC_008699.1.

3D structure databases

ProteinModelPortali A1SE01.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196162.Noca_0494.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL80036 ; ABL80036 ; Noca_0494 .
GeneIDi 4597393.
KEGGi nca:Noca_0494.
PATRICi 22743003. VBINocSp122728_0767.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109649.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci NSP196162:GH4V-505-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.
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.
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of chromosome 1 of Nocardioides sp. JS614."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.
    , Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J., Richardson P.
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BAA-499 / JS614.

Entry informationi

Entry nameiHEM11_NOCSJ
AccessioniPrimary (citable) accession number: A1SE01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 6, 2007
Last modified: October 1, 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.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