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B2SZ26

- HEM1_BURPP

UniProt

B2SZ26 - HEM1_BURPP

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Protein

Glutamyl-tRNA reductase

Gene
hemA, Bphyt_3521
Organism
Burkholderia phytofirmans (strain DSM 17436 / PsJN)
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 sitei56 – 561Nucleophile 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 bindingi194 – 1996NADP 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

BioCyciBPHY398527:GJEX-3573-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:Bphyt_3521
OrganismiBurkholderia phytofirmans (strain DSM 17436 / PsJN)
Taxonomic identifieri398527 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia
ProteomesiUP000001739: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Glutamyl-tRNA reductaseUniRule annotationPRO_1000093120Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi398527.Bphyt_3521.

Structurei

3D structure databases

ProteinModelPortaliB2SZ26.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 584Substrate 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.
OMAiLNKQFET.
OrthoDBiEOG6C2WN5.

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.

B2SZ26-1 [UniParc]FASTAAdd to Basket

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MQLLTIGINH HTAPVALRER VAFPLEQIKP ALETFKSIWL GPSARTAPEA    50
AILSTCNRTE LYCATDDQAA REAAIQWLSR YHNLPIDELA PHVYALPQSE 100
AVRHAFRVAS GLDSMVLGET QIVGQMKDAV RTASEAGALG TYLNQLFQRT 150
FAVAKEVRST TEIGAQSVSM AAAAVRLAQR IFDKVSNQRV LFIGAGEMIE 200
LCATHFAAQQ PRELVVANRT AERGTRLAER FNGRAIPLSE LPSRMHEFDI 250
IVSCTASTLP IIGLGAVERA VKARRHRPIF MVDLAVPRDI EPEVGQLEDV 300
FLYTVDDLGA IVREGNASRQ AAVAQAEAII ETRVQNFMQW LDARSIVPVI 350
RHMHTQADVL RRAEVERAQK MLARGDDPAA VLEALSQSLT NKLIHGPTHA 400
LNRASSENRD KLIELMSGFY KHSGSTER 428
Length:428
Mass (Da):47,203
Last modified:July 1, 2008 - v1
Checksum:i6BC92868E31AF409
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001052 Genomic DNA. Translation: ACD17911.1.
RefSeqiWP_012434472.1. NC_010681.1.
YP_001897135.1. NC_010681.1.

Genome annotation databases

EnsemblBacteriaiACD17911; ACD17911; Bphyt_3521.
GeneIDi6282849.
KEGGibpy:Bphyt_3521.
PATRICi19217617. VBIBurPhy117947_7549.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001052 Genomic DNA. Translation: ACD17911.1 .
RefSeqi WP_012434472.1. NC_010681.1.
YP_001897135.1. NC_010681.1.

3D structure databases

ProteinModelPortali B2SZ26.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 398527.Bphyt_3521.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACD17911 ; ACD17911 ; Bphyt_3521 .
GeneIDi 6282849.
KEGGi bpy:Bphyt_3521.
PATRICi 19217617. VBIBurPhy117947_7549.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi LNKQFET.
OrthoDBi EOG6C2WN5.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci BPHY398527:GJEX-3573-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. "Complete sequence of chromosome 1 of Burkholderia phytofirmans PsJN."
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.
    , Nowak J., Sessitsch A., Lazarovits G., Compant S., Barka E., Tiedje J.
    Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 17436 / PsJN.

Entry informationi

Entry nameiHEM1_BURPP
AccessioniPrimary (citable) accession number: B2SZ26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: September 3, 2014
This is version 47 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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