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A0LRF2

- HEM1_ACIC1

UniProt

A0LRF2 - HEM1_ACIC1

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Protein

Glutamyl-tRNA reductase

Gene
hemA, Acel_0238
Organism
Acidothermus cellulolyticus (strain ATCC 43068 / 11B)
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 sitei50 – 501Nucleophile By similarity
Sitei99 – 991Important for activity By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei120 – 1201Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADP 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

BioCyciACEL351607:GIXW-246-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:Acel_0238
OrganismiAcidothermus cellulolyticus (strain ATCC 43068 / 11B)
Taxonomic identifieri351607 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeAcidothermaceaeAcidothermus
ProteomesiUP000008221: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Glutamyl-tRNA reductaseUniRule annotationPRO_0000335000Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi351607.Acel_0238.

Structurei

3D structure databases

ProteinModelPortaliA0LRF2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni114 – 1163Substrate 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.
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.

A0LRF2-1 [UniParc]FASTAAdd to Basket

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MSLLVVGVSH RGTPLSLLER AVLDSDQATK LLDDLVGSPV VREGMVLSTC    50
NRVEIYACVE KFHPALTLIS ELLSRHGNVN FDEIAGHVHV HYDDRAVQHL 100
FAVAAGLDSM LIGEHQVVGQ VRDAFRLAQE RGYAGRDLHA IVQDALHAAR 150
RVRAETRIDS AGQTLVDVGL QILSERLGPL AGRRALVIGA GAMASVAVAA 200
LTRVGITGLT VASRTLRRAT ALAQRYNGQA AALEKLADLL AETDVVVSCT 250
GSVHPVVDAA TLTKAVAGRT NPLGILDIAL PHDVDPDVDR LPNVIRVDLE 300
TLRPVLENTA SSADVRHARH ILDEEFDAHV ARRAAVGVVP TVVALRDKAA 350
RVVAAELRRL EKRLPELDPR QFEEIRTTVH RVVDKLLHAP TVRVQELAGL 400
AGPDSYSEAL RTLFDLDPAQ PVAISAPQPS TDSPARAAYQ PTDEAATDAE 450
PRRDDAEPPS AAAAQDAGRE SRP 473
Length:473
Mass (Da):50,720
Last modified:December 12, 2006 - v1
Checksum:iBBBB567B837D1ABF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000481 Genomic DNA. Translation: ABK52012.1.
RefSeqiYP_871998.1. NC_008578.1.

Genome annotation databases

EnsemblBacteriaiABK52012; ABK52012; Acel_0238.
GeneIDi4485376.
KEGGiace:Acel_0238.
PATRICi20670822. VBIAciCel132453_0262.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000481 Genomic DNA. Translation: ABK52012.1 .
RefSeqi YP_871998.1. NC_008578.1.

3D structure databases

ProteinModelPortali A0LRF2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 351607.Acel_0238.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABK52012 ; ABK52012 ; Acel_0238 .
GeneIDi 4485376.
KEGGi ace:Acel_0238.
PATRICi 20670822. VBIAciCel132453_0262.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci ACEL351607:GIXW-246-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: ATCC 43068 / 11B.

Entry informationi

Entry nameiHEM1_ACIC1
AccessioniPrimary (citable) accession number: A0LRF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 12, 2006
Last modified: September 3, 2014
This is version 63 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