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Q6AB02

- HEM1_PROAC

UniProt

Q6AB02 - HEM1_PROAC

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Protein

Glutamyl-tRNA reductase

Gene
hemA, PPA0307
Organism
Propionibacterium acnes (strain KPA171202 / DSM 16379)
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 sitei42 – 421Nucleophile By similarity
Binding sitei102 – 1021Substrate By similarity
Binding sitei113 – 1131Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi181 – 1866NADP 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

BioCyciPACN267747:GHO9-308-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:PPA0307
OrganismiPropionibacterium acnes (strain KPA171202 / DSM 16379)
Taxonomic identifieri267747 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium
ProteomesiUP000000603: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Glutamyl-tRNA reductaseUniRule annotationPRO_0000335059Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi267747.PPA0307.

Structurei

3D structure databases

ProteinModelPortaliQ6AB02.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 444Substrate binding By similarity
Regioni107 – 1093Substrate 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.
OMAiPYLYVHY.
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.
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.

Sequencei

Sequence statusi: Complete.

Q6AB02-1 [UniParc]FASTAAdd to Basket

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MTVDHAEQGL GVVSEAAAQV DGLGLALTDH PQIRGALVLS TCNRVCLIVE    50
TSPEAVAQGF DEAALRRCIA DHGANVLAES AQLVCENDAV WRLFRVAAGM 100
ESMVFGEREV AGQMKRALSE ARREQTVSYT IGHVVEEALK TSRHVATETA 150
LAAEGRTVVA VGLDLVAQRM DLDGARVLVM GTGSYAGASC AQLSSRGVAE 200
IQVHSASGRA AGFARRHRVS EALDIDAALA QADLVVTCRG SGVPALSAEA 250
ARRAVDARRG RDLMVLDLAI SGDVEEPVPA GVEVIDLETI RQAVPASAEA 300
ERAAAEHIIA TGVRHFAVDL ERRRMAPAVV ALRDVISDLV TAELERLPEE 350
GSVPVDEVAA SLRRLAASMA HIPSARARMA SEQGLGDRWL NSLSDVLGID 400
VDIAAPVIDM SSFANADCMT CPVTGLRVED LATDAAPRGE ERTS 444
Length:444
Mass (Da):46,740
Last modified:September 13, 2004 - v1
Checksum:i5A500F3FE40A90AD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017283 Genomic DNA. Translation: AAT82064.1.
RefSeqiYP_055022.1. NC_006085.1.

Genome annotation databases

EnsemblBacteriaiAAT82064; AAT82064; PPA0307.
GeneIDi2932189.
KEGGipac:PPA0307.
PATRICi23035267. VBIProAcn64440_0318.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017283 Genomic DNA. Translation: AAT82064.1 .
RefSeqi YP_055022.1. NC_006085.1.

3D structure databases

ProteinModelPortali Q6AB02.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 267747.PPA0307.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAT82064 ; AAT82064 ; PPA0307 .
GeneIDi 2932189.
KEGGi pac:PPA0307.
PATRICi 23035267. VBIProAcn64440_0318.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci PACN267747:GHO9-308-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.
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.
ProtoNeti Search...

Publicationsi

  1. "The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
    Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
    Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KPA171202 / DSM 16379.

Entry informationi

Entry nameiHEM1_PROAC
AccessioniPrimary (citable) accession number: Q6AB02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 13, 2004
Last modified: May 14, 2014
This is version 73 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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