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A9B543

- HEM1_HERA2

UniProt

A9B543 - HEM1_HERA2

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Haur_3544
Organism
Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785)
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
Sitei96 – 961Important for activity By similarity
Binding sitei106 – 1061Substrate By similarity
Binding sitei117 – 1171Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi185 – 1906NADP 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

BioCyciHAUR316274:GHYA-3581-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:Haur_3544
OrganismiHerpetosiphon aurantiacus (strain ATCC 23779 / DSM 785)
Taxonomic identifieri316274 [NCBI]
Taxonomic lineageiBacteriaChloroflexiChloroflexiaHerpetosiphonalesHerpetosiphonaceaeHerpetosiphon
ProteomesiUP000000787: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 414414Glutamyl-tRNA reductaseUniRule annotation
PRO_1000093146Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi316274.Haur_3544.

Structurei

3D structure databases

ProteinModelPortaliA9B543.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate binding By similarity
Regioni111 – 1133Substrate 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.
OMAiLNKQFET.
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.

A9B543-1 [UniParc]FASTAAdd to Basket

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MQLVVVGAHQ RTAPISIRER IAFAEAELAQ ALSSLRQIAV EGFILSTCNR    50
VELYALVEEA DGGRSLRQFL AQQRSIDLDE LMPHVYTYLD EDAVRHLFRV 100
ASGLDSMALG EAQILSQIKT AYNAAQQTEL LGTTMHRLIQ AALTTGKLVR 150
TETQLAHAQL SVVSVGLSLA RQHLDLTNRS VVIIGAGRTG ELALKHYLEY 200
TSNITVLSRT FERAARLAEH HKVAAKPISE LAAVLQASDV VISCTSSPEL 250
MLDFEQAQLL QAQRQRQWVL LDLAVPRDID RHVGALPEVW LYDVDDMQAI 300
CERNRASKAA EVAGAEAIVE RELIKWQEWW LTQAVLPTIR ALRAHAEAIR 350
LAELERTLAR LDLSEQQQQA VSALTSAIIN KLLHQPMRAI KDTAASPQLA 400
HAAQQLFRLD FEAI 414
Length:414
Mass (Da):45,982
Last modified:January 15, 2008 - v1
Checksum:iF5117B3104B853BD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000875 Genomic DNA. Translation: ABX06180.1.
RefSeqiYP_001546308.1. NC_009972.1.

Genome annotation databases

EnsemblBacteriaiABX06180; ABX06180; Haur_3544.
GeneIDi5735403.
KEGGihau:Haur_3544.
PATRICi22124249. VBIHerAur93466_3644.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000875 Genomic DNA. Translation: ABX06180.1 .
RefSeqi YP_001546308.1. NC_009972.1.

3D structure databases

ProteinModelPortali A9B543.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 316274.Haur_3544.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX06180 ; ABX06180 ; Haur_3544 .
GeneIDi 5735403.
KEGGi hau:Haur_3544.
PATRICi 22124249. VBIHerAur93466_3644.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci HAUR316274:GHYA-3581-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. "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.
    , Kim E., Bryant D.A., Richardson P.
    Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 23779 / DSM 785.

Entry informationi

Entry nameiHEM1_HERA2
AccessioniPrimary (citable) accession number: A9B543
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: September 3, 2014
This is version 56 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