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Q6AB02

- HEM1_PROAC

UniProt

Q6AB02 - HEM1_PROAC

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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 – 421NucleophileUniRule annotation
Binding sitei102 – 1021SubstrateUniRule annotation
Binding sitei113 – 1131SubstrateUniRule annotation

Regions

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

BioCyciPACN267747:GHO9-308-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: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 reductasePRO_0000335059Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi267747.PPA0307.

Structurei

3D structure databases

ProteinModelPortaliQ6AB02.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 444Substrate bindingUniRule annotation
Regioni107 – 1093Substrate 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.
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

« Hide

        10         20         30         40         50
MTVDHAEQGL GVVSEAAAQV DGLGLALTDH PQIRGALVLS TCNRVCLIVE
60 70 80 90 100
TSPEAVAQGF DEAALRRCIA DHGANVLAES AQLVCENDAV WRLFRVAAGM
110 120 130 140 150
ESMVFGEREV AGQMKRALSE ARREQTVSYT IGHVVEEALK TSRHVATETA
160 170 180 190 200
LAAEGRTVVA VGLDLVAQRM DLDGARVLVM GTGSYAGASC AQLSSRGVAE
210 220 230 240 250
IQVHSASGRA AGFARRHRVS EALDIDAALA QADLVVTCRG SGVPALSAEA
260 270 280 290 300
ARRAVDARRG RDLMVLDLAI SGDVEEPVPA GVEVIDLETI RQAVPASAEA
310 320 330 340 350
ERAAAEHIIA TGVRHFAVDL ERRRMAPAVV ALRDVISDLV TAELERLPEE
360 370 380 390 400
GSVPVDEVAA SLRRLAASMA HIPSARARMA SEQGLGDRWL NSLSDVLGID
410 420 430 440
VDIAAPVIDM SSFANADCMT CPVTGLRVED LATDAAPRGE ERTS
Length:444
Mass (Da):46,740
Last modified:September 13, 2004 - v1
Checksum:i5A500F3FE40A90AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 76 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