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A3MXT2

- HEM12_PYRCJ

UniProt

A3MXT2 - HEM12_PYRCJ

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Protein

Glutamyl-tRNA reductase 2

Gene

hemA2

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).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 – 481NucleophileUniRule annotation
Sitei88 – 881Important for activityUniRule annotation
Binding sitei98 – 981SubstrateUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi177 – 1826NADPUniRule 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

BioCyciPCAL410359:GIX2-2083-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: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 2PRO_0000335099Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi410359.Pcal_2034.

Structurei

3D structure databases

ProteinModelPortaliA3MXT2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate bindingUniRule annotation
Regioni103 – 1053Substrate 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.
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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        10         20         30         40         50
MDFLAPLSAV VLTYREVGGD ALGALAEEMR KCAEELAKAT PMFVLHTCGR
60 70 80 90 100
VEVYLYGASE EEVARVAARY RRFAEGVKVL RGAEAARHLF AVAAGLDSML
110 120 130 140 150
IGETDILGQL EEAYDRQVKA GYTRGLLKTV VERAVRVGKR VRTETGISRG
160 170 180 190 200
PRGLGSLAVM YVSRMLDLRE ASVAVLGAGA VGAGLAMELA ARGVKRLVVL
210 220 230 240 250
NRTYEKAVEV ANRVGGEARP LTEEEVEKCL AECDVVFSSV HTLQPVIKRV
260 270 280 290 300
PPEARVKVIV DLGVPSSVVP NLPVAVVKIE DLRELAEEYN RERAGEVEKA
310 320 330 340 350
WAIVDEEVAR LPRLLARRYV EEATSAIMAQ AMAAAEEEGK RAGCDTAVLA
360 370 380 390
AKTTVKRTLL PLITKLKEMA ENGKAEEAAK LIQLLQEALQ S
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.
RefSeqiYP_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 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: October 29, 2014
This is version 64 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

Documents

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

External Data

Dasty 3