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Q3ACT4

- HEM1_CARHZ

UniProt

Q3ACT4 - HEM1_CARHZ

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008)
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

BioCyciCHYD246194:GJCN-1206-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
Ordered Locus Names:CHY_1207
OrganismiCarboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008)
Taxonomic identifieri246194 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeCarboxydothermus
ProteomesiUP000002706: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449Glutamyl-tRNA reductasePRO_1000004606Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi246194.CHY_1207.

Structurei

3D structure databases

ProteinModelPortaliQ3ACT4.
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.
HOGENOMiHOG000109651.
KOiK02492.
OMAiHEVTGEY.
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.
IPR018214. GluRdtase_CS.
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.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3ACT4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYLVVVGVNH RTAPVEVREK LSFSDHQLKD AFSALLSYPS IDGSVILSTC
60 70 80 90 100
NRTEVYVASL DVDTGLKVVR EFLANWAGLS LSDIKNYTYN YTLYDAVHHL
110 120 130 140 150
FRVASGLDSM ILGETQILGQ VRDAFLKASS LKASNKILNT LFQHAITVGK
160 170 180 190 200
KVRTETGIDK NPVSISYAAV QLACSFFGSL KDKKALLIGA GKMSSLTAKH
210 220 230 240 250
LSYYGIKEII VANRSFEKAE QFAREFNGIA VPFAKIYDIL AEVDLVISCT
260 270 280 290 300
GAPHLIIHKE QLELVIGNRQ HPLYLIDIAV PRDIDPEIAK LPNVFLYDID
310 320 330 340 350
KLQNVVTKNL EERKKLAEMA ENIIETELKA FIEWHSTQFV VPTIVALKKK
360 370 380 390 400
AEEIKQKELT KALNKLGNIS EREKNIVCAL AHTILNQLLH TPIVKLKQYA
410 420 430 440
LTPQGHLYTE ILQNLFDLQV EGERPKNFTH PREEMEESDE KRSYCGESR
Length:449
Mass (Da):50,498
Last modified:November 22, 2005 - v1
Checksum:i035209EE115F03D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000141 Genomic DNA. Translation: ABB15744.1.
RefSeqiWP_011344126.1. NC_007503.1.
YP_360050.1. NC_007503.1.

Genome annotation databases

EnsemblBacteriaiABB15744; ABB15744; CHY_1207.
GeneIDi3727853.
KEGGichy:CHY_1207.
PATRICi21275550. VBICarHyd26463_1156.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000141 Genomic DNA. Translation: ABB15744.1 .
RefSeqi WP_011344126.1. NC_007503.1.
YP_360050.1. NC_007503.1.

3D structure databases

ProteinModelPortali Q3ACT4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 246194.CHY_1207.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB15744 ; ABB15744 ; CHY_1207 .
GeneIDi 3727853.
KEGGi chy:CHY_1207.
PATRICi 21275550. VBICarHyd26463_1156.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi HEVTGEY.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CHYD246194:GJCN-1206-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.
IPR018214. GluRdtase_CS.
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.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Z-2901 / DSM 6008.

Entry informationi

Entry nameiHEM1_CARHZ
AccessioniPrimary (citable) accession number: Q3ACT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 22, 2005
Last modified: October 29, 2014
This is version 72 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