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B0UU02

- HEM1_HISS2

UniProt

B0UU02 - HEM1_HISS2

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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 – 501NucleophileUniRule annotation
Sitei104 – 1041Important for activityUniRule annotation
Binding sitei114 – 1141SubstrateUniRule annotation
Binding sitei125 – 1251SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi201 – 2066NADPUniRule annotation

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 reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
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 reductasePRO_1000093141Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi228400.HSM_1279.

Structurei

3D structure databases

ProteinModelPortaliB0UU02.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni119 – 1213Substrate bindingUniRule annotation

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.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

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

        10         20         30         40         50
MTILVLGINH KTASVALREK VAFSDEKRLL ALKQIKQTQL AECAVILSTC
60 70 80 90 100
NRTEVYLHNK NVGPQNDEVW LDSCVQWFAD IHQVDLEELK SCLYSQQNLQ
110 120 130 140 150
ASRHLMRVAS GLDSLILGEP QILGQVKQAY QMSEEYYSLH SDIGMMSTEL
160 170 180 190 200
SRLFQKTFAT AKRVRTETHI GESAVSVAYA ACSLARQIFD SLRNLNILLV
210 220 230 240 250
GAGETIELVS RHLLRHGVNG LAIANRTLSR AEKLVEKLET TQKIDIFSLD
260 270 280 290 300
RLSEGLKRAD IVITSTGSPH VLISRNLIEQ AQQMRHYKPM LIVDIAVPRD
310 320 330 340 350
VEESAGEIES VYHYTVDDLH NIIQHNINQR EQASQQAEHI IQQESADFFE
360 370 380 390 400
WLKVHQFSNL IRNYRESAEI IRQDLLEKAL QALQNGENTE QVLQELSHKL
410 420 430
TKKLIHQPTQ AMQTMVKAGN TEGLQAFSHA VKS
Length:433
Mass (Da):49,006
Last modified:April 8, 2008 - v1
Checksum:i1CED8845C5397A13
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000947 Genomic DNA. Translation: ACA31008.1.
RefSeqiYP_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:
EMBLi
GenBanki
DDBJi
Links Updated
CP000947 Genomic DNA. Translation: ACA31008.1 .
RefSeqi 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: October 29, 2014
This is version 55 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.UniRule annotation

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