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B0JKN4

- HEM1_MICAN

UniProt

B0JKN4 - HEM1_MICAN

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Protein

Glutamyl-tRNA reductase

Gene
hemA, MAE_30010
Organism
Microcystis aeruginosa (strain NIES-843)
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. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
  2. NADP binding Source: InterPro

GO - Biological processi

  1. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMAER449447:GHO8-3021-MONOMER.
UniPathwayiUPA00251; UER00316.
UPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:MAE_30010
OrganismiMicrocystis aeruginosa (strain NIES-843)
Taxonomic identifieri449447 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesMicrocystis
ProteomesiUP000001510: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Glutamyl-tRNA reductaseUniRule annotationPRO_1000093151Add
BLAST

Proteomic databases

PaxDbiB0JKN4.
PRIDEiB0JKN4.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi449447.MAE_30010.

Structurei

3D structure databases

ProteinModelPortaliB0JKN4.

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.

B0JKN4-1 [UniParc]FASTAAdd to Basket

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MNIAVVGLSH KTAPVEIREK LSIPEAKIES ALTHLKGYPH IQEVAIISTC    50
NRLEIYAVVT DTEKGVVEIT QFLAEIGHIP LNVLRRYLFT LLHQDAVRHL 100
LRVSAGLESL VLGEGQILAQ VKNTHKLAQK YNTISQLLDR LFKQAMTAGK 150
RVRTETSIGT GAVSISSAAV ELAHAKVTDL SSKKIAIIGA GKMSRLLVTH 200
LLAKGSQQIA IINRSQRRAQ ELAREFPHLP LQLYGLEEMM TTVAASDIVF 250
TSTGATEPIL TKTLLTEVTI TANSLMLIDI SVPRNVHTDV KELAQVQAFN 300
VDDLKAVVAA NQESRRQMAR EAEALLEQEV EAFELWWRSL DTVPTISCLR 350
SKIEDIREQE LEKALSRLGT EFAEKHQEVI EAMTRGIVNK ILHEPMVQLR 400
AQQDIEARKR CLQSLQMLFN LSVGEEYS 428
Length:428
Mass (Da):47,653
Last modified:March 18, 2008 - v1
Checksum:iBE438F8A34BF9BF3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009552 Genomic DNA. Translation: BAG02823.1.
RefSeqiYP_001658015.1. NC_010296.1.

Genome annotation databases

EnsemblBacteriaiBAG02823; BAG02823; MAE_30010.
GeneIDi5863817.
KEGGimar:MAE_30010.
PATRICi22630833. VBIMicAer59304_2739.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009552 Genomic DNA. Translation: BAG02823.1 .
RefSeqi YP_001658015.1. NC_010296.1.

3D structure databases

ProteinModelPortali B0JKN4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 449447.MAE_30010.

Proteomic databases

PaxDbi B0JKN4.
PRIDEi B0JKN4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAG02823 ; BAG02823 ; MAE_30010 .
GeneIDi 5863817.
KEGGi mar:MAE_30010.
PATRICi 22630833. VBIMicAer59304_2739.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
UPA00668 .
BioCyci MAER449447:GHO8-3021-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: NIES-843.

Entry informationi

Entry nameiHEM1_MICAN
AccessioniPrimary (citable) accession number: B0JKN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 18, 2008
Last modified: September 3, 2014
This is version 50 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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