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A9B543

- HEM1_HERA2

UniProt

A9B543 - HEM1_HERA2

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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
Sitei96 – 961Important for activityUniRule annotation
Binding sitei106 – 1061SubstrateUniRule annotation
Binding sitei117 – 1171SubstrateUniRule annotation

Regions

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

BioCyciHAUR316274:GHYA-3581-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: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 reductasePRO_1000093146Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi316274.Haur_3544.

Structurei

3D structure databases

ProteinModelPortaliA9B543.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate bindingUniRule annotation
Regioni111 – 1133Substrate 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.
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

« Hide

        10         20         30         40         50
MQLVVVGAHQ RTAPISIRER IAFAEAELAQ ALSSLRQIAV EGFILSTCNR
60 70 80 90 100
VELYALVEEA DGGRSLRQFL AQQRSIDLDE LMPHVYTYLD EDAVRHLFRV
110 120 130 140 150
ASGLDSMALG EAQILSQIKT AYNAAQQTEL LGTTMHRLIQ AALTTGKLVR
160 170 180 190 200
TETQLAHAQL SVVSVGLSLA RQHLDLTNRS VVIIGAGRTG ELALKHYLEY
210 220 230 240 250
TSNITVLSRT FERAARLAEH HKVAAKPISE LAAVLQASDV VISCTSSPEL
260 270 280 290 300
MLDFEQAQLL QAQRQRQWVL LDLAVPRDID RHVGALPEVW LYDVDDMQAI
310 320 330 340 350
CERNRASKAA EVAGAEAIVE RELIKWQEWW LTQAVLPTIR ALRAHAEAIR
360 370 380 390 400
LAELERTLAR LDLSEQQQQA VSALTSAIIN KLLHQPMRAI KDTAASPQLA
410
HAAQQLFRLD FEAI
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: October 1, 2014
This is version 57 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