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Q8R687

- HEM1_FUSNN

UniProt

Q8R687 - HEM1_FUSNN

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
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 sitei52 – 521NucleophileUniRule annotation
Binding sitei99 – 991SubstrateUniRule annotation
Binding sitei110 – 1101SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi179 – 1846NADPUniRule 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

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:FN0646
OrganismiFusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
Taxonomic identifieri190304 [NCBI]
Taxonomic lineageiBacteriaFusobacteriaFusobacterialesFusobacteriaceaeFusobacterium
ProteomesiUP000002521: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Glutamyl-tRNA reductasePRO_0000114027Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi190304.FN0646.

Structurei

3D structure databases

ProteinModelPortaliQ8R687.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 544Substrate bindingUniRule annotation
Regioni104 – 1063Substrate 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.
HOGENOMiHOG000109108.
InParanoidiQ8R687.
KOiK02492.
OMAiAETEIQG.
OrthoDBiEOG6MWNBM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMiSSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R687-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLDLENIIVI GVSHENLSLL ERENFMRTRP KYIIERLYTE KKINAYINLS
60 70 80 90 100
TCLRTEFYIE LNSNIKAKEI KNLFSVDMIV KSRVEAIEYL FKVGCGFYSV
110 120 130 140 150
IKGEDQILAQ VKGAYAEALE NEHSSKFLNI IFNKSIELGK KFRTKSMIAH
160 170 180 190 200
NALSLEAISL KFIKSKFPNI EDKNIFILGI GELAQDILTL LTKEQLKNIY
210 220 230 240 250
IANRTYHKAE QIKKEFDIVN IVDYREKYPK MIEADVIISA TSAPHIVVEY
260 270 280 290 300
DKFVAQMKEN KDYLFIDLAV PRDVDERLAN FKNIEIYNLD DIWEVYHLNS
310 320
MNRDKLLEDY SYLIDEQMEK LIKTLNYYK
Length:329
Mass (Da):38,592
Last modified:June 1, 2002 - v1
Checksum:i675E1B115629E9E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009951 Genomic DNA. Translation: AAL94842.1.
RefSeqiNP_603543.1. NC_003454.1.
WP_011016556.1. NC_003454.1.

Genome annotation databases

EnsemblBacteriaiAAL94842; AAL94842; FN0646.
GeneIDi993220.
KEGGifnu:FN0646.
PATRICi21951055. VBIFusNuc122357_1210.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009951 Genomic DNA. Translation: AAL94842.1 .
RefSeqi NP_603543.1. NC_003454.1.
WP_011016556.1. NC_003454.1.

3D structure databases

ProteinModelPortali Q8R687.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 190304.FN0646.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL94842 ; AAL94842 ; FN0646 .
GeneIDi 993220.
KEGGi fnu:FN0646.
PATRICi 21951055. VBIFusNuc122357_1210.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109108.
InParanoidi Q8R687.
KOi K02492.
OMAi AETEIQG.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view ]
Pfami PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
SUPFAMi 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: ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131.

Entry informationi

Entry nameiHEM1_FUSNN
AccessioniPrimary (citable) accession number: Q8R687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: June 1, 2002
Last modified: November 26, 2014
This is version 88 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

Caution

Lacks the conserved histidine residue in position 89 which is potentially part of the active site; it is replaced by a tyrosine residue.Curated

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