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O08393

- HEM1_NOSS1

UniProt

O08393 - HEM1_NOSS1

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Nostoc sp. (strain PCC 7120 / UTEX 2576)
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. 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

UniPathwayiUPA00251; UER00316.
UPA00668.

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:alr1042
OrganismiNostoc sp. (strain PCC 7120 / UTEX 2576)
Taxonomic identifieri103690 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
ProteomesiUP000002483: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Glutamyl-tRNA reductasePRO_0000113986Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi103690.alr1042.

Structurei

3D structure databases

ProteinModelPortaliO08393.
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.
OMAiGLSIHTT.
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.

O08393 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNIAVVGLSH KTAPVEIREK LSIPEPQTES AIAQLTSYPH IDEVAILSTC
60 70 80 90 100
NRLEIYIVAG ETDHGIREVT QFLSEHSKLP VHSLRQHLFV LLHEDAVMHI
110 120 130 140 150
MRVAAGLDSL VLGEGQILAQ VKNTHKLGQQ YNGIKTILNR LFKQALTAGK
160 170 180 190 200
RVRTETSIGT GAVSISSAAV ELAQIKAENL AACRVTILGA GKMSRLLVQH
210 220 230 240 250
LVSKGATQIS IVNRSRERAQ ELAKQFSEHP IRTHLLPEMM TVIAESHLVF
260 270 280 290 300
TSTSATEPIL DRAKLEMVLA PNQPLMLFDI SVPRNVHTDV NELVNVQAFN
310 320 330 340 350
VDDLKAVVAQ NYESRRKMAQ EAERLLEEEI EAFDIWWRSL ETVSTISSLR
360 370 380 390 400
SKIETIREQE LEKALSRLGS EFGDKHQEVI EALTRGIVNK ILHDPMVQLR
410 420
AQQDVEARRR CMQTLQMLFN LDVGEQFS
Length:428
Mass (Da):47,909
Last modified:January 23, 2002 - v2
Checksum:i06A470955F9D3C64
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331A → G in AAB58164. 1 PublicationCurated
Sequence conflicti48 – 481S → G in AAB58164. 1 PublicationCurated
Sequence conflicti174 – 1741Q → E in AAB58164. 1 PublicationCurated
Sequence conflicti280 – 2801I → V in AAB58164. 1 PublicationCurated
Sequence conflicti374 – 3807DKHQEVI → EQTSRGV in AAB58164. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U97695 Genomic DNA. Translation: AAB58164.1.
BA000019 Genomic DNA. Translation: BAB72999.1.
PIRiAG1936.
RefSeqiNP_485085.1. NC_003272.1.
WP_010995216.1. NC_003272.1.

Genome annotation databases

EnsemblBacteriaiBAB72999; BAB72999; BAB72999.
GeneIDi1104636.
KEGGiana:alr1042.
PATRICi22771984. VBINosSp37423_1476.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U97695 Genomic DNA. Translation: AAB58164.1 .
BA000019 Genomic DNA. Translation: BAB72999.1 .
PIRi AG1936.
RefSeqi NP_485085.1. NC_003272.1.
WP_010995216.1. NC_003272.1.

3D structure databases

ProteinModelPortali O08393.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 103690.alr1042.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB72999 ; BAB72999 ; BAB72999 .
GeneIDi 1104636.
KEGGi ana:alr1042.
PATRICi 22771984. VBINosSp37423_1476.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
UPA00668 .

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

« Hide 'large scale' publications
  1. "Cloning and characterization of hemA, a gene encoding glutamyl tRNA reductase in the cyanobacterium Anabaena sp. strain 7120."
    Woelfle M.A., Haselkorn R.
    Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7120 / UTEX 2576.

Entry informationi

Entry nameiHEM1_NOSS1
AccessioniPrimary (citable) accession number: O08393
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2002
Last modified: October 1, 2014
This is version 107 of the entry and version 2 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