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Protein

Glutamyl-tRNA reductase 2

Gene

hemA2

Organism
Nocardioides sp. (strain BAA-499 / JS614)
Status
Reviewed-Annotation score: 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 sitei51 – 511NucleophileUniRule annotation
Sitei99 – 991Important for activityUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation
Binding sitei120 – 1201SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi190 – 1956NADPUniRule 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-1991-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 2UniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTR 2UniRule annotation
Gene namesi
Name:hemA2UniRule annotation
Ordered Locus Names:Noca_1962
OrganismiNocardioides sp. (strain BAA-499 / JS614)
Taxonomic identifieri196162 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaeNocardioidaceaeNocardioides
ProteomesiUP000000640: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Glutamyl-tRNA reductase 2PRO_0000335056Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi196162.Noca_1962.

Structurei

3D structure databases

ProteinModelPortaliA1SI37.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate 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.
OMAiYSNTRIG.
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.

A1SI37-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MSRLTCLAFP GRSIPMAVLE RLSVAARELP ASVRALRAVP GVDQVLVLST
60 70 80 90 100
CERTEVYAWW TDEADPAALL RALAGQRGLG PEPLLEHAVG LTGREAVQHL
110 120 130 140 150
LRVTAGLDSF VRGESDIVGQ VRAAVQAARA EGAVGLEVQR LVDAAVNTSR
160 170 180 190 200
RVHRSTGAGL AAGSVASTAV AAVAGLLPDG LAGRDLLVVG TGQVAVSVVA
210 220 230 240 250
AAREAGARLT VCGRDPERAA AIAPAGARVL GLDDLPGALL DADAVVFGTS
260 270 280 290 300
SPERLLRAGD LGPGLSEHRS GRELVVVDLC VPRNVDPDVR GVPGVRLLDL
310 320 330 340 350
TDLRGAAVPG RRPSAPAPAA LELAEQIVAQ EVDRFLHWWV DRAAAEPVRR
360 370 380 390 400
LRADVEACVR EEVARATRGL SPDLEPLVAE GIRRAVQHLA HGPTRRLLDA
410 420 430 440
AAAGEDEVVA LLAGLFAPSA EEDQAVPAYS PQPIGNTSNA AASATPRR
Length:448
Mass (Da):46,537
Last modified:February 6, 2007 - v1
Checksum:iD6E37EAE8352C2A1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000509 Genomic DNA. Translation: ABL81472.1.
RefSeqiWP_011755419.1. NC_008699.1.
YP_923159.1. NC_008699.1.

Genome annotation databases

EnsemblBacteriaiABL81472; ABL81472; Noca_1962.
GeneIDi4599868.
KEGGinca:Noca_1962.
PATRICi22745969. VBINocSp122728_2233.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000509 Genomic DNA. Translation: ABL81472.1.
RefSeqiWP_011755419.1. NC_008699.1.
YP_923159.1. NC_008699.1.

3D structure databases

ProteinModelPortaliA1SI37.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196162.Noca_1962.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABL81472; ABL81472; Noca_1962.
GeneIDi4599868.
KEGGinca:Noca_1962.
PATRICi22745969. VBINocSp122728_2233.

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109649.
KOiK02492.
OMAiYSNTRIG.
OrthoDBiEOG6MWNBM.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
BioCyciNSP196162:GH4V-1991-MONOMER.

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.
ProtoNetiSearch...

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 nameiHEM12_NOCSJ
AccessioniPrimary (citable) accession number: A1SI37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 6, 2007
Last modified: January 7, 2015
This is version 68 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.