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Q6LNB3

- HEM1_PHOPR

UniProt

Q6LNB3 - HEM1_PHOPR

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Protein
Glutamyl-tRNA reductase
Gene
hemA, PBPRA2846
Organism
Photobacterium profundum (Photobacterium sp. (strain SS9))
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
Sitei97 – 971Important for activity By similarity
Binding sitei107 – 1071Substrate By similarity
Binding sitei118 – 1181Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi187 – 1926NADP By similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP

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

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:PBPRA2846
OrganismiPhotobacterium profundum (Photobacterium sp. (strain SS9))
Taxonomic identifieri74109 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium
ProteomesiUP000000593: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 420420Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114054Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi298386.PBPRA2846.

Structurei

3D structure databases

ProteinModelPortaliQ6LNB3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni112 – 1143Substrate 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.
HOGENOMiHOG000109650.
KOiK02492.
OMAiLAHKLTN.
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.

Q6LNB3-1 [UniParc]FASTAAdd to Basket

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MTLLALGINH NTASVDLREK VAFSPDKLKE ALQQLESHPE VTSSIIVSTC    50
NRTEVYCDVT HSGPGVMIDW LAKFHRLSAE EILPSLYFHE EQAAARHLMR 100
VACGLDSLVL GEPQILGQVK QSYYSSQEYD AIHGTLEKLF HKTFTVAKRV 150
RTETDIGGNA VSVAYAACTL AKQIFESLSD TTVLLVGAGE TIELVSRHLV 200
EQGCNKLIVA NRTKERAANL AEEFGAEVIG LPEIPEHLHR ADIVISSTAS 250
PLPIVGKGMV EKAIKARRHQ PMLFVDIAVP RDVEAEVGDL NDVYLYTVDD 300
LHSIIEKNRE QRKVAAIQAE AIISEESAAF MSWLRSLEAV DSIRQYRCFA 350
DDIKNDMLSR SLQAIANGVA PEKVLVELSN KLTNKLIHAP TRAMQQAAHN 400
GEPEKLSVIR ETLGLDSIKD 420
Length:420
Mass (Da):46,335
Last modified:July 5, 2004 - v1
Checksum:iCC8F8571ACED3576
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR378672 Genomic DNA. Translation: CAG21213.1.
RefSeqiYP_131015.1. NC_006370.1.

Genome annotation databases

EnsemblBacteriaiCAG21213; CAG21213; PBPRA2846.
GeneIDi3122003.
KEGGippr:PBPRA2846.
PATRICi22936722. VBIPhoPro109272_3039.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR378672 Genomic DNA. Translation: CAG21213.1 .
RefSeqi YP_131015.1. NC_006370.1.

3D structure databases

ProteinModelPortali Q6LNB3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 298386.PBPRA2846.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAG21213 ; CAG21213 ; PBPRA2846 .
GeneIDi 3122003.
KEGGi ppr:PBPRA2846.
PATRICi 22936722. VBIPhoPro109272_3039.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .

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: SS9.

Entry informationi

Entry nameiHEM1_PHOPR
AccessioniPrimary (citable) accession number: Q6LNB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 5, 2004
Last modified: September 3, 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 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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