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A3MXT2

- HEM12_PYRCJ

UniProt

A3MXT2 - HEM12_PYRCJ

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Protein

Glutamyl-tRNA reductase 2

Gene
hemA2, Pcal_2034
Organism
Pyrobaculum calidifontis (strain JCM 11548 / VA1)
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 sitei48 – 481Nucleophile By similarity
Sitei88 – 881Important for activity By similarity
Binding sitei98 – 981Substrate By similarity
Binding sitei109 – 1091Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi177 – 1826NADP By similarity

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

BioCyciPCAL410359:GIX2-2083-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:Pcal_2034
OrganismiPyrobaculum calidifontis (strain JCM 11548 / VA1)
Taxonomic identifieri410359 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
ProteomesiUP000001431: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391Glutamyl-tRNA reductase 2UniRule annotationPRO_0000335099Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi410359.Pcal_2034.

Structurei

3D structure databases

ProteinModelPortaliA3MXT2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate binding By similarity
Regioni103 – 1053Substrate 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.
HOGENOMiHOG000112880.
KOiK02492.
OMAiMIICEEL.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMiSSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A3MXT2-1 [UniParc]FASTAAdd to Basket

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MDFLAPLSAV VLTYREVGGD ALGALAEEMR KCAEELAKAT PMFVLHTCGR    50
VEVYLYGASE EEVARVAARY RRFAEGVKVL RGAEAARHLF AVAAGLDSML 100
IGETDILGQL EEAYDRQVKA GYTRGLLKTV VERAVRVGKR VRTETGISRG 150
PRGLGSLAVM YVSRMLDLRE ASVAVLGAGA VGAGLAMELA ARGVKRLVVL 200
NRTYEKAVEV ANRVGGEARP LTEEEVEKCL AECDVVFSSV HTLQPVIKRV 250
PPEARVKVIV DLGVPSSVVP NLPVAVVKIE DLRELAEEYN RERAGEVEKA 300
WAIVDEEVAR LPRLLARRYV EEATSAIMAQ AMAAAEEEGK RAGCDTAVLA 350
AKTTVKRTLL PLITKLKEMA ENGKAEEAAK LIQLLQEALQ S 391
Length:391
Mass (Da):42,346
Last modified:April 3, 2007 - v1
Checksum:i6A6F2690806753F0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000561 Genomic DNA. Translation: ABO09449.1.
RefSeqiWP_011850707.1. NC_009073.1.
YP_001056915.1. NC_009073.1.

Genome annotation databases

EnsemblBacteriaiABO09449; ABO09449; Pcal_2034.
GeneIDi4908889.
KEGGipcl:Pcal_2034.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000561 Genomic DNA. Translation: ABO09449.1 .
RefSeqi WP_011850707.1. NC_009073.1.
YP_001056915.1. NC_009073.1.

3D structure databases

ProteinModelPortali A3MXT2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 410359.Pcal_2034.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABO09449 ; ABO09449 ; Pcal_2034 .
GeneIDi 4908889.
KEGGi pcl:Pcal_2034.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000112880.
KOi K02492.
OMAi MIICEEL.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci PCAL410359:GIX2-2083-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view ]
Pfami PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
SUPFAMi SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCM 11548 / VA1.

Entry informationi

Entry nameiHEM12_PYRCJ
AccessioniPrimary (citable) accession number: A3MXT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 3, 2007
Last modified: September 3, 2014
This is version 62 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

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