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C5CB93

- HEM1_MICLC

UniProt

C5CB93 - HEM1_MICLC

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus)
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 sitei46 – 461NucleophileUniRule annotation
Sitei97 – 971Important for activityUniRule annotation
Binding sitei107 – 1071SubstrateUniRule annotation
Binding sitei118 – 1181SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi196 – 2016NADPUniRule 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

BioCyciMLUT465515:GHH6-1521-MONOMER.
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:Mlut_15240
OrganismiMicrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus)
Taxonomic identifieri465515 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeMicrococcus
ProteomesiUP000000738: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Glutamyl-tRNA reductasePRO_1000202638Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi465515.Mlut_15240.

Structurei

3D structure databases

ProteinModelPortaliC5CB93.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 484Substrate bindingUniRule annotation
Regioni112 – 1143Substrate 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.
HOGENOMiHOG000109649.
KOiK02492.
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.
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.

Sequencei

Sequence statusi: Complete.

C5CB93-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTVFSLVASH HDLDLDTVAR LSAGATGVGP ALPGSGAAGA VVLATCNRVE
60 70 80 90 100
IYAEADGAGV EAARAGLLSA VAASTSLPDE DVHAAFRTLD ADATARHLFE
110 120 130 140 150
VGVGLDSAVV GEREIAGQVR RALTAAQEAG TASGPLVRLF ESATRTAKDV
160 170 180 190 200
GSHTALGAAG RSVVSVALDL AEELRGLTDA AAQRDFWAGA TILLIGTGAY
210 220 230 240 250
AGTTLAQLAD RGATTVGVHS ASGRAEQFVA DRGGWALALG GEAVAGAVAE
260 270 280 290 300
ADVIIGSSGG ERQISPERLQ ELREGGRRPL TVVDLALSRD FDPAVADLPD
310 320 330 340 350
VDLITLESVR LAAPEQAQVA VAEARALVDD AVEEYRAAQR GRSADAAIKA
360 370 380 390 400
LRRHTLGVLD RELERVRARH GCTAAAEEVE FALRRMVNQL LHEPSVRAKR
410 420 430 440 450
LAAEGRLDRY EDALEAVFGI EAPGRPASEV GTVEAACPAH EDEGGAARIA
Length:450
Mass (Da):46,363
Last modified:July 28, 2009 - v1
Checksum:iF15E233FC31F3069
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001628 Genomic DNA. Translation: ACS31016.1.
RefSeqiWP_010080565.1. NZ_CABC01000132.1.
YP_002957570.1. NC_012803.1.

Genome annotation databases

EnsemblBacteriaiACS31016; ACS31016; Mlut_15240.
GeneIDi7986020.
KEGGimlu:Mlut_15240.
PATRICi22623682. VBIMicLut29563_1460.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001628 Genomic DNA. Translation: ACS31016.1 .
RefSeqi WP_010080565.1. NZ_CABC01000132.1.
YP_002957570.1. NC_012803.1.

3D structure databases

ProteinModelPortali C5CB93.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 465515.Mlut_15240.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACS31016 ; ACS31016 ; Mlut_15240 .
GeneIDi 7986020.
KEGGi mlu:Mlut_15240.
PATRICi 22623682. VBIMicLut29563_1460.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109649.
KOi K02492.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci MLUT465515:GHH6-1521-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.
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.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230.

Entry informationi

Entry nameiHEM1_MICLC
AccessioniPrimary (citable) accession number: C5CB93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: November 26, 2014
This is version 42 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

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