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A3CU63

- HEM1_METMJ

UniProt

A3CU63 - HEM1_METMJ

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Memar_0980
Organism
Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)
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 sitei52 – 521Nucleophile By similarity
Sitei89 – 891Important for activity By similarity
Binding sitei99 – 991Substrate By similarity
Binding sitei110 – 1101Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi179 – 1846NADP By similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP

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

BioCyciMMAR368407:GH7L-998-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:Memar_0980
OrganismiMethanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)
Taxonomic identifieri368407 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanomicrobiaceaeMethanoculleus
ProteomesiUP000002146: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 423423Glutamyl-tRNA reductaseUniRule annotation
PRO_0000335092Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi368407.Memar_0980.

Structurei

3D structure databases

ProteinModelPortaliA3CU63.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 544Substrate binding By similarity
Regioni104 – 1063Substrate 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.
OMAiHEVTGEY.

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.

A3CU63-1 [UniParc]FASTAAdd to Basket

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MPELFTIPLA LAGISHHAAD IATLEAFRFP DEAAFLHEAR ERFRGVLLLQ    50
TCNRIEVLVQ GDARSLEGFL QEKGRHGFTV IEGEAVPRHL LELAAGIDSL 100
IVGEDQILGQ LKQALAAAEE AGTCCSAIGL CIKKAVHAGV RVRRQTQINR 150
GAVSVGSAAV TLAENLLGTL RDRHILVVGS GEMGVLVAQA LAARGLTAIY 200
VANRTYERAV MLADKIGGRA VNFKDLYRYI ALSDVVISCT AAPHPVIRTE 250
DIRAVMEERL WPLDTHPRHL ILIDIAQPRD VEEGVRSIEG VHLFTIDDLR 300
NVNDATMESR RSEADRARGI IDEEAEHFVR LLRRAAADET LALLYTWAES 350
IRARERDRAL ARLRERDDRT AEVIDDLTHA LTNKILSDVT TAIRACAECG 400
DITTAEALMR AITRGEPCFQ NEE 423
Length:423
Mass (Da):46,577
Last modified:March 20, 2007 - v1
Checksum:iE6C88D544AB01966
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000562 Genomic DNA. Translation: ABN56913.1.
RefSeqiWP_011843824.1. NC_009051.1.
YP_001046895.1. NC_009051.1.

Genome annotation databases

EnsemblBacteriaiABN56913; ABN56913; Memar_0980.
GeneIDi4847471.
KEGGimem:Memar_0980.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000562 Genomic DNA. Translation: ABN56913.1 .
RefSeqi WP_011843824.1. NC_009051.1.
YP_001046895.1. NC_009051.1.

3D structure databases

ProteinModelPortali A3CU63.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 368407.Memar_0980.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABN56913 ; ABN56913 ; Memar_0980 .
GeneIDi 4847471.
KEGGi mem:Memar_0980.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi HEVTGEY.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci MMAR368407:GH7L-998-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: ATCC 35101 / DSM 1498 / JR1.

Entry informationi

Entry nameiHEM1_METMJ
AccessioniPrimary (citable) accession number: A3CU63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 20, 2007
Last modified: September 3, 2014
This is version 62 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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