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P95525

- HEM1_PASMU

UniProt

P95525 - HEM1_PASMU

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Protein
Glutamyl-tRNA reductase
Gene
hemA, gltX1, PM0684
Organism
Pasteurella multocida (strain Pm70)
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
Sitei104 – 1041Important for activity By similarity
Binding sitei114 – 1141Substrate By similarity
Binding sitei125 – 1251Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi199 – 2046NADP 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

BioCyciPMUL272843:GC8W-709-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Synonyms:gltX1
Ordered Locus Names:PM0684
OrganismiPasteurella multocida (strain Pm70)
Taxonomic identifieri272843 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
ProteomesiUP000000809: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114052Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi272843.PM0684.

Structurei

3D structure databases

ProteinModelPortaliP95525.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni119 – 1213Substrate 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.

P95525-1 [UniParc]FASTAAdd to Basket

« Hide

MTILVIGINH KTASVAIREK VAFSAEKRVE ALAQIQQQAL AESAVILSTC    50
NRTEVYFHHK AIPPQEAESW TARCMQWFAE IHQLSLDALA GCLYSQQNQQ 100
AVLHLMRVAC GLDSLVLGEP QILGQVKDAY QLSKMYYQGQ NQPLSSEFSR 150
LFQKTFSVAK RVRTETNIGG NAVSVAYGAC SLARQIFDSL KTLNVLLVGA 200
GETIELTCRH LLRHGVQRIM IANRTFERAQ HLVTKLDGAE NVQVLALTQL 250
QEGLNQADIV ISSTGSPTIL ITQDMVKIAQ KARCDLPMLL VDIAVPRDIE 300
ESVGELDSIY HYTVDDLQTI IQRNLVEREK ASAQAWVIIQ QECADFFEWL 350
KVHQFSNLIR SYRENAEDIR QILLEKALLA LRQGEDSEAV LQALSYKLTN 400
KLLHSPTQVM NAMVKTGNST GLALFSSTLK SDVE 434
Length:434
Mass (Da):48,408
Last modified:April 27, 2001 - v2
Checksum:i648A624862C5E164
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 722TA → AT in CAA71452. 1 Publication
Sequence conflicti91 – 911G → D in CAA71452. 1 Publication
Sequence conflicti135 – 1351M → P in CAA71452. 1 Publication
Sequence conflicti171 – 1711N → S in CAA71452. 1 Publication
Sequence conflicti282 – 2821A → V in CAA71452. 1 Publication
Sequence conflicti326 – 3261V → A in CAA71452. 1 Publication
Sequence conflicti344 – 3441A → V in CAA71452. 1 Publication
Sequence conflicti379 – 3791L → F in CAA71452. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10430 Genomic DNA. Translation: CAA71452.1.
AE004439 Genomic DNA. Translation: AAK02768.1.
RefSeqiNP_245621.1. NC_002663.1.
WP_010906790.1. NC_002663.1.

Genome annotation databases

EnsemblBacteriaiAAK02768; AAK02768; PM0684.
GeneIDi1244031.
KEGGipmu:PM0684.
PATRICi22870562. VBIPasMul88067_0692.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10430 Genomic DNA. Translation: CAA71452.1 .
AE004439 Genomic DNA. Translation: AAK02768.1 .
RefSeqi NP_245621.1. NC_002663.1.
WP_010906790.1. NC_002663.1.

3D structure databases

ProteinModelPortali P95525.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272843.PM0684.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK02768 ; AAK02768 ; PM0684 .
GeneIDi 1244031.
KEGGi pmu:PM0684.
PATRICi 22870562. VBIPasMul88067_0692.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci PMUL272843:GC8W-709-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

« Hide 'large scale' publications
  1. Castrillon R.T.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 2.5.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Pm70.

Entry informationi

Entry nameiHEM1_PASMU
AccessioniPrimary (citable) accession number: P95525
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 27, 2001
Last modified: September 3, 2014
This is version 105 of the entry and version 2 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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