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Q7NLA8

- HEM1_GLOVI

UniProt

Q7NLA8 - HEM1_GLOVI

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Protein

Glutamyl-tRNA reductase

Gene
hemA, glr1218
Organism
Gloeobacter violaceus (strain PCC 7421)
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. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciGVIO251221:GH9A-1228-MONOMER.
UniPathwayiUPA00251; UER00316.
UPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:glr1218
OrganismiGloeobacter violaceus (strain PCC 7421)
Taxonomic identifieri251221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaGloeobacteriaGloeobacteralesGloeobacter
ProteomesiUP000000557: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Glutamyl-tRNA reductaseUniRule annotationPRO_0000114029Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi251221.gvip168.

Structurei

3D structure databases

ProteinModelPortaliQ7NLA8.

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.
KOiK02492.
OMAiLAHKLTN.
OrthoDBiEOG6MWNBM.
PhylomeDBiQ7NLA8.

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.

Q7NLA8-1 [UniParc]FASTAAdd to Basket

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MQIAVIGLSH RTAPVEIRER VSIAEGQVPE YVSRLRSCSQ VAECAILSTC    50
NRLEIYTVLR DSEHGLREVT RFLAESKGVL LPTLQRHLFV LLHQDAVMHL 100
MRVAAGLDSI VLGEGQILAQ VKMTQSLAQQ GKGVDRVLNQ LFKTAITAGK 150
RVRSDTNIGT GAVSVSSAAV EMALRKKGPL HNQRCLVVGA GKMGELLVRH 200
LLAKGARQII VLNRSLEKAA QMVEQFGLML PVATVDELTN YVPCSDLIFT 250
CTGATEPLLT LEKMSSLRRD QSLMIFDIAV PRNVATEVDE LPNVQLFNVD 300
HLKQVVEENR AYRQLMVTQC EEILLEQLDE FLDWWRGLEA VPTINQLRQK 350
VETIREQELE KALSRLGTEF AEKHQGIIDS LTRAIVNKIL HDPMVQLRAQ 400
RDIEARRRAL QTLQTLFNLE AQSNPEPPTL 430
Length:430
Mass (Da):48,136
Last modified:December 15, 2003 - v1
Checksum:i5491B16BF167B368
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000045 Genomic DNA. Translation: BAC89159.1.
RefSeqiNP_924164.1. NC_005125.1.

Genome annotation databases

EnsemblBacteriaiBAC89159; BAC89159; BAC89159.
GeneIDi2598886.
KEGGigvi:gvip168.
PATRICi22041849. VBIGloVio86258_1243.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000045 Genomic DNA. Translation: BAC89159.1 .
RefSeqi NP_924164.1. NC_005125.1.

3D structure databases

ProteinModelPortali Q7NLA8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 251221.gvip168.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC89159 ; BAC89159 ; BAC89159 .
GeneIDi 2598886.
KEGGi gvi:gvip168.
PATRICi 22041849. VBIGloVio86258_1243.

Phylogenomic databases

eggNOGi COG0373.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.
PhylomeDBi Q7NLA8.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
UPA00668 .
BioCyci GVIO251221:GH9A-1228-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: PCC 7421.

Entry informationi

Entry nameiHEM1_GLOVI
AccessioniPrimary (citable) accession number: Q7NLA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: September 3, 2014
This is version 88 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, 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

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