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A9VIU0

- HEM1_BACWK

UniProt

A9VIU0 - HEM1_BACWK

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Protein
Glutamyl-tRNA reductase
Gene
hemA, BcerKBAB4_4311
Organism
Bacillus weihenstephanensis (strain KBAB4)
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

BioCyciBWEI315730:GHRU-4427-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:BcerKBAB4_4311
OrganismiBacillus weihenstephanensis (strain KBAB4)
Taxonomic identifieri315730 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002154: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Glutamyl-tRNA reductaseUniRule annotation
PRO_1000093114Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi315730.BcerKBAB4_4311.

Structurei

3D structure databases

ProteinModelPortaliA9VIU0.

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.

A9VIU0-1 [UniParc]FASTAAdd to Basket

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MHILVVSVNY RTAPVEFREK LTFQAAELEQ AMNTLQNQKS VLENVIVSTC    50
NRTEIYAVVD QLHTGRYYIK KFLADWFQLE IEEVAPYLSI FEQDGAIDHL 100
FRVTCGLDSM VVGETQILGQ IKDSFLEAQQ VKATGTIFNE LFKQVVTLAK 150
RAHSETTIGE SAMSVSYAAV ELGKKIFGDL TDCHVLILGA GKMGELALQN 200
LYGSGARKVT VMNRTLTKAE VMAEKYMGHA KPLSELQCAL LEADILISST 250
GASEYVITKE MMTKVERMRS GRPLFMVDIA VPRDIDPAID ELEGSFLYDI 300
DDLQGVVEAN RAERLKEAEK IQFMIEEEMV LFKTWLSTLG VVPLISALRD 350
KALAIQSDTM ESLERKIPNL SDREKKVISK HTKSIINQLL KDPILVAKEL 400
AVEEGAGEKL ALFAKIFDLE VEEAGNTEEV EHKRAWTPSV PSL 443
Length:443
Mass (Da):49,510
Last modified:February 5, 2008 - v1
Checksum:iC31E4BD2D08CF6E0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000903 Genomic DNA. Translation: ABY45470.1.
RefSeqiYP_001647098.1. NC_010184.1.

Genome annotation databases

EnsemblBacteriaiABY45470; ABY45470; BcerKBAB4_4311.
GeneIDi5844524.
KEGGibwe:BcerKBAB4_4311.
PATRICi19013290. VBIBacWei55973_4960.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000903 Genomic DNA. Translation: ABY45470.1 .
RefSeqi YP_001647098.1. NC_010184.1.

3D structure databases

ProteinModelPortali A9VIU0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 315730.BcerKBAB4_4311.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABY45470 ; ABY45470 ; BcerKBAB4_4311 .
GeneIDi 5844524.
KEGGi bwe:BcerKBAB4_4311.
PATRICi 19013290. VBIBacWei55973_4960.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci BWEI315730:GHRU-4427-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: KBAB4.

Entry informationi

Entry nameiHEM1_BACWK
AccessioniPrimary (citable) accession number: A9VIU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: September 3, 2014
This is version 57 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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