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B7KI42

- HEM1_CYAP7

UniProt

B7KI42 - HEM1_CYAP7

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Protein

Glutamyl-tRNA reductase

Gene
hemA, PCC7424_5179
Organism
Cyanothece sp. (strain PCC 7424) (Synechococcus sp. (strain ATCC 29155))
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

BioCyciCSP65393:GJP7-5235-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:PCC7424_5179
OrganismiCyanothece sp. (strain PCC 7424) (Synechococcus sp. (strain ATCC 29155))
Taxonomic identifieri65393 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece
ProteomesiUP000002384: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Glutamyl-tRNA reductaseUniRule annotationPRO_1000190515Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi65393.PCC7424_5179.

Structurei

3D structure databases

ProteinModelPortaliB7KI42.

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.

B7KI42-1 [UniParc]FASTAAdd to Basket

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MNIAVVGLSH KTAPVEVREK LSIPEAKLEE VLAHLKSYPH IQEVAILSTC    50
NRLEIYAVVT ETEQGIIEIS QFLSEKGHIP LHHLRRHLFI LLHQDAVRHL 100
MRVAAGLESL VLGEGQILAQ VKNTHKLAQK YGGIGRLLDR LFKQAMTAGK 150
RVRSETSIGT GAVSISSAAV ELAQMKVIDI CVCRVTIIGA GKMSRLLVQH 200
LLSKGVSKIA IVNRSLRRAQ ELAGLFPEAQ LQLHPLEEMI NAVSVSDIVF 250
TSTGATEPIL NRSNLESIIA VNQSLMLVDI SVPRNVDADV QQLEQIQSYN 300
VDDLKAVVAA NQESRRRLAQ EAEGLLEEEV ESFELWWRSL DTVPTISCLR 350
DKVETIREQE LEKALSRLGT EFAEKHQEVI EALTRGIVNK ILHEPMVQLR 400
AQQDIEARKR CLQSLQMLFD LDIEEQYT 428
Length:428
Mass (Da):47,869
Last modified:February 10, 2009 - v1
Checksum:iCABFD48D14A1FA70
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001291 Genomic DNA. Translation: ACK73529.1.
RefSeqiWP_015957108.1. NC_011729.1.
YP_002380397.1. NC_011729.1.

Genome annotation databases

EnsemblBacteriaiACK73529; ACK73529; PCC7424_5179.
GeneIDi7109511.
KEGGicyc:PCC7424_5179.
PATRICi21559398. VBICyaSp136448_5290.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001291 Genomic DNA. Translation: ACK73529.1 .
RefSeqi WP_015957108.1. NC_011729.1.
YP_002380397.1. NC_011729.1.

3D structure databases

ProteinModelPortali B7KI42.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 65393.PCC7424_5179.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACK73529 ; ACK73529 ; PCC7424_5179 .
GeneIDi 7109511.
KEGGi cyc:PCC7424_5179.
PATRICi 21559398. VBICyaSp136448_5290.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
UPA00668 .
BioCyci CSP65393:GJP7-5235-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. "Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
    Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
    MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7424.

Entry informationi

Entry nameiHEM1_CYAP7
AccessioniPrimary (citable) accession number: B7KI42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: September 3, 2014
This is version 46 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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