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A1SI37

- HEM12_NOCSJ

UniProt

A1SI37 - HEM12_NOCSJ

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Protein
Glutamyl-tRNA reductase 2
Gene
hemA2, Noca_1962
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) By similarity.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 – 511Nucleophile By similarity
Sitei99 – 991Important for activity By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei120 – 1201Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi190 – 1956NADP By similarity

GO - Molecular functioni

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

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 2 (EC:1.2.1.70)
Short name:
GluTR 2
Gene namesi
Name:hemA2
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 2UniRule annotation
PRO_0000335056Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi196162.Noca_1962.

Structurei

3D structure databases

ProteinModelPortaliA1SI37.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate binding By similarity
Regioni114 – 1163Substrate binding By similarity

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 By similarity.UniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109649.
KOiK02492.
OMAiNTSRRVH.
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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MSRLTCLAFP GRSIPMAVLE RLSVAARELP ASVRALRAVP GVDQVLVLST    50
CERTEVYAWW TDEADPAALL RALAGQRGLG PEPLLEHAVG LTGREAVQHL 100
LRVTAGLDSF VRGESDIVGQ VRAAVQAARA EGAVGLEVQR LVDAAVNTSR 150
RVHRSTGAGL AAGSVASTAV AAVAGLLPDG LAGRDLLVVG TGQVAVSVVA 200
AAREAGARLT VCGRDPERAA AIAPAGARVL GLDDLPGALL DADAVVFGTS 250
SPERLLRAGD LGPGLSEHRS GRELVVVDLC VPRNVDPDVR GVPGVRLLDL 300
TDLRGAAVPG RRPSAPAPAA LELAEQIVAQ EVDRFLHWWV DRAAAEPVRR 350
LRADVEACVR EEVARATRGL SPDLEPLVAE GIRRAVQHLA HGPTRRLLDA 400
AAAGEDEVVA LLAGLFAPSA EEDQAVPAYS PQPIGNTSNA AASATPRR 448
Length:448
Mass (Da):46,537
Last modified:February 6, 2007 - v1
Checksum:iD6E37EAE8352C2A1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CP000509 Genomic DNA. Translation: ABL81472.1 .
RefSeqi WP_011755419.1. NC_008699.1.
YP_923159.1. NC_008699.1.

3D structure databases

ProteinModelPortali A1SI37.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196162.Noca_1962.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL81472 ; ABL81472 ; Noca_1962 .
GeneIDi 4599868.
KEGGi nca:Noca_1962.
PATRICi 22745969. VBINocSp122728_2233.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci NSP196162:GH4V-1991-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 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: September 3, 2014
This is version 66 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 By similarity.

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3