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B8F4X6

- HEM1_HAEPS

UniProt

B8F4X6 - HEM1_HAEPS

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Protein
Glutamyl-tRNA reductase
Gene
hemA, HAPS_0733
Organism
Haemophilus parasuis serovar 5 (strain SH0165)
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
Sitei108 – 1081Important for activity By similarity
Binding sitei118 – 1181Substrate By similarity
Binding sitei129 – 1291Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi203 – 2086NADP 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

BioCyciHPAR557723:GH24-733-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:HAPS_0733
OrganismiHaemophilus parasuis serovar 5 (strain SH0165)
Taxonomic identifieri557723 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000006743: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 435435Glutamyl-tRNA reductaseUniRule annotation
PRO_1000190531Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi557723.HAPS_0733.

Structurei

3D structure databases

ProteinModelPortaliB8F4X6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni123 – 1253Substrate 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.

B8F4X6-1 [UniParc]FASTAAdd to Basket

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MTILALGINH KTASVSLREK VAFVEDKRQR AFEQIRDQSL AESVVILSTC    50
NRTELYFHQP KIPPQEEHPD NIAWREQCFN WFAEIHQLDK EELSEAYYFK 100
QNLEAARHLM SVACGLDSLI LGEPQILGQV KQAYQESEEF YHSQGSGVST 150
NLSRLFQKTF ATAKRVRSET EIGSSAVSVA YAACGLARQI FDDFTKLRFL 200
LVGAGETIEL VARHLINHGA KNIMIANRTH IRAEMLAVKL DIPMQILSLS 250
ALQIGLNQAD VVICSTGSPD ILITKEMVEQ AQKQRRFDPM LLIDIAVPRD 300
IDEKAGELDS IYAYSVDDLQ NIIQQNIAQR QQAAEQAKEI VIEEAKDFFV 350
WLKQQQSTNL IKHYRQNAEE IRLDLLEKAL SALQQGQDCE KVLNELSYKL 400
TNQLLHIPTQ ALQAMAKNSN VKGLQSFSKA LKLEE 435
Length:435
Mass (Da):49,238
Last modified:March 3, 2009 - v1
Checksum:iCFD2AF608E68117E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001321 Genomic DNA. Translation: ACL32378.1.
RefSeqiYP_002475326.1. NC_011852.1.

Genome annotation databases

EnsemblBacteriaiACL32378; ACL32378; HAPS_0733.
GeneIDi7278248.
KEGGihap:HAPS_0733.
PATRICi20193737. VBIHaePar127548_0733.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001321 Genomic DNA. Translation: ACL32378.1 .
RefSeqi YP_002475326.1. NC_011852.1.

3D structure databases

ProteinModelPortali B8F4X6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 557723.HAPS_0733.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACL32378 ; ACL32378 ; HAPS_0733 .
GeneIDi 7278248.
KEGGi hap:HAPS_0733.
PATRICi 20193737. VBIHaePar127548_0733.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci HPAR557723:GH24-733-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. "Complete genome sequence of Haemophilus parasuis SH0165."
    Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R., Jin M., Jin Q., Chen H.
    J. Bacteriol. 191:1359-1360(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SH0165.

Entry informationi

Entry nameiHEM1_HAEPS
AccessioniPrimary (citable) accession number: B8F4X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: September 3, 2014
This is version 45 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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