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B7HQM6

- HEM1_BACC7

UniProt

B7HQM6 - HEM1_BACC7

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Protein
Glutamyl-tRNA reductase
Gene
hemA, BCAH187_A4602
Organism
Bacillus cereus (strain AH187)
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
Sitei99 – 991Important for activity By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei120 – 1201Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADP 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

BioCyciBCER405534:GHXM-4534-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:BCAH187_A4602
OrganismiBacillus cereus (strain AH187)
Taxonomic identifieri405534 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002214: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Glutamyl-tRNA reductaseUniRule annotation
PRO_1000190504Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi405534.BCAH187_A4602.

Structurei

3D structure databases

ProteinModelPortaliB7HQM6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni114 – 1163Substrate 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.
HOGENOMiHOG000109651.
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.

B7HQM6-1 [UniParc]FASTAAdd to Basket

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MHILVVSVNY RTAPVEFREK LTFQAAELEQ AMTTLQNQKS VLENVIVSTC    50
NRTEVYAVVD QLHTGRYYIK KFLADWFQLE IEEVAPYLTI FEQDGAIDHL 100
FRVTCGLDSM VVGETQILGQ IKDSFLEAQQ VKATGTIFNE LFKQVITLAK 150
RAHSETTIGE SAMSVSYAAV ELGKKIFGEL TDCHVLILGA GKMGELALQN 200
LYGSGARKVT VMNRTLSKAE IMAEKYMGHA KPLSELQCAL LEADILISST 250
GASDYVITKE MMTKVEKMRS GRPLFMVDIA VPRDIDPAID ELEGSFLYDI 300
DDLQGVVEAN RAERLKEAEK IQFMIEEEIV VFKTWLSTLG VVPLISALRD 350
KALAIQSETM ESLERKIPTL SDRERKVISK HTKSIINQLL KDPILVAKEI 400
AAEEGADEKL ALFAKIFDLE MEDVESRAEE VEHKRAWTPS VPSL 444
Length:444
Mass (Da):49,727
Last modified:February 10, 2009 - v1
Checksum:iC3D715531F43EBC1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001177 Genomic DNA. Translation: ACJ81830.1.
RefSeqiYP_002340528.1. NC_011658.1.

Genome annotation databases

EnsemblBacteriaiACJ81830; ACJ81830; BCAH187_A4602.
GeneIDi7076075.
KEGGibcr:BCAH187_A4602.
PATRICi18834631. VBIBacCer120511_4785.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001177 Genomic DNA. Translation: ACJ81830.1 .
RefSeqi YP_002340528.1. NC_011658.1.

3D structure databases

ProteinModelPortali B7HQM6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 405534.BCAH187_A4602.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACJ81830 ; ACJ81830 ; BCAH187_A4602 .
GeneIDi 7076075.
KEGGi bcr:BCAH187_A4602.
PATRICi 18834631. VBIBacCer120511_4785.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci BCER405534:GHXM-4534-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. "Genome sequence of Bacillus cereus AH187."
    Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B., Okstad O.A., Ravel J., Sutton G.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AH187.

Entry informationi

Entry nameiHEM1_BACC7
AccessioniPrimary (citable) accession number: B7HQM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: September 3, 2014
This is version 48 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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