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B0UU02

- HEM1_HISS2

UniProt

B0UU02 - HEM1_HISS2

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Protein

Glutamyl-tRNA reductase

Gene
hemA, HSM_1279
Organism
Histophilus somni (strain 2336) (Haemophilus somnus)
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 bindingi201 – 2066NADP 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

BioCyciHSOM228400:GHWT-1314-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:HSM_1279
OrganismiHistophilus somni (strain 2336) (Haemophilus somnus)
Taxonomic identifieri228400 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
ProteomesiUP000008543: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 433433Glutamyl-tRNA reductaseUniRule annotationPRO_1000093141Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi228400.HSM_1279.

Structurei

3D structure databases

ProteinModelPortaliB0UU02.

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.
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.

B0UU02-1 [UniParc]FASTAAdd to Basket

« Hide

MTILVLGINH KTASVALREK VAFSDEKRLL ALKQIKQTQL AECAVILSTC    50
NRTEVYLHNK NVGPQNDEVW LDSCVQWFAD IHQVDLEELK SCLYSQQNLQ 100
ASRHLMRVAS GLDSLILGEP QILGQVKQAY QMSEEYYSLH SDIGMMSTEL 150
SRLFQKTFAT AKRVRTETHI GESAVSVAYA ACSLARQIFD SLRNLNILLV 200
GAGETIELVS RHLLRHGVNG LAIANRTLSR AEKLVEKLET TQKIDIFSLD 250
RLSEGLKRAD IVITSTGSPH VLISRNLIEQ AQQMRHYKPM LIVDIAVPRD 300
VEESAGEIES VYHYTVDDLH NIIQHNINQR EQASQQAEHI IQQESADFFE 350
WLKVHQFSNL IRNYRESAEI IRQDLLEKAL QALQNGENTE QVLQELSHKL 400
TKKLIHQPTQ AMQTMVKAGN TEGLQAFSHA VKS 433
Length:433
Mass (Da):49,006
Last modified:April 8, 2008 - v1
Checksum:i1CED8845C5397A13
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000947 Genomic DNA. Translation: ACA31008.1.
RefSeqiWP_012340438.1. NC_010519.1.
YP_001784601.1. NC_010519.1.

Genome annotation databases

EnsemblBacteriaiACA31008; ACA31008; HSM_1279.
GeneIDi6107144.
KEGGihsm:HSM_1279.
PATRICi20199764. VBIHaeSom93646_1352.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000947 Genomic DNA. Translation: ACA31008.1 .
RefSeqi WP_012340438.1. NC_010519.1.
YP_001784601.1. NC_010519.1.

3D structure databases

ProteinModelPortali B0UU02.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 228400.HSM_1279.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACA31008 ; ACA31008 ; HSM_1279 .
GeneIDi 6107144.
KEGGi hsm:HSM_1279.
PATRICi 20199764. VBIHaeSom93646_1352.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci HSOM228400:GHWT-1314-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: 2336.

Entry informationi

Entry nameiHEM1_HISS2
AccessioniPrimary (citable) accession number: B0UU02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: September 3, 2014
This is version 53 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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