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A8FFV4

- HEM1_BACP2

UniProt

A8FFV4 - HEM1_BACP2

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Bacillus pumilus (strain SAFR-032)
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
Sitei99 – 991Important for activityUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation
Binding sitei120 – 1201SubstrateUniRule annotation

Regions

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

BioCyciBPUM315750:GH6N-2515-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:BPUM_2458
OrganismiBacillus pumilus (strain SAFR-032)
Taxonomic identifieri315750 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001355: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 455455Glutamyl-tRNA reductasePRO_1000057570Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi315750.BPUM_2458.

Structurei

3D structure databases

ProteinModelPortaliA8FFV4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni114 – 1163Substrate 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.
HOGENOMiHOG000109651.
KOiK02492.
OMAiAITCGKK.
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.

A8FFV4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHILVVGLDY KTAPVEIREQ LSFEPSELGT AMSKLKEEKS ILENIVISTC
60 70 80 90 100
NRTEIYAVVD QLHTGRFYIK RFLADWFGLE KEDVSPYLKF YENDGAVEHL
110 120 130 140 150
FRVACGLDSM VIGETQILGQ VRSSFKVAQE EKTIGTVFNY LFKQAVTVAK
160 170 180 190 200
RSHAETDIAS NAVSVSYAAV ELAKKIFGRL SDKHVLILGA GKMGELAAQN
210 220 230 240 250
LQGQGIGQVT VINRTYEKAK ELAGRFSGEP KSLNQLEKTL SEADILISST
260 270 280 290 300
GAKQFVITKE MVESANKKRK GRPLFMVDIA VPRDLDPAIS EVEGAFLYDI
310 320 330 340 350
DDLEGIVAAN LKERRAVAEQ VELLIEAEIV EFKQWLNTLG VVPVISALRE
360 370 380 390 400
KALTIQADTM QSIERKLPNL THREMKLLNK HTKSIINQML KDPILKAKEI
410 420 430 440 450
AAEPNAEEKL LLFKEIFDLQ VEDEEQKVEP VQVEQGSFQL FKPNMAQGFA

TVASE
Length:455
Mass (Da):50,817
Last modified:November 13, 2007 - v1
Checksum:i8F3B7A3B560BA362
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000813 Genomic DNA. Translation: ABV63121.1.
RefSeqiWP_012010780.1. NC_009848.1.
YP_001487681.1. NC_009848.1.

Genome annotation databases

EnsemblBacteriaiABV63121; ABV63121; BPUM_2458.
GeneIDi5621727.
KEGGibpu:BPUM_2458.
PATRICi18968838. VBIBacPum16546_2514.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000813 Genomic DNA. Translation: ABV63121.1 .
RefSeqi WP_012010780.1. NC_009848.1.
YP_001487681.1. NC_009848.1.

3D structure databases

ProteinModelPortali A8FFV4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 315750.BPUM_2458.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABV63121 ; ABV63121 ; BPUM_2458 .
GeneIDi 5621727.
KEGGi bpu:BPUM_2458.
PATRICi 18968838. VBIBacPum16546_2514.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci BPUM315750:GH6N-2515-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: SAFR-032.

Entry informationi

Entry nameiHEM1_BACP2
AccessioniPrimary (citable) accession number: A8FFV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: November 26, 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