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P28462

- HEM1_CHLP8

UniProt

P28462 - HEM1_CHLP8

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Cpar_0738
Organism
Chlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 263 / NCIB 8327))
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).1 Publication

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

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

BioCyciCPAR517417:GH95-766-MONOMER.
BRENDAi1.2.1.70. 1348.
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:Cpar_0738
OrganismiChlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 263 / NCIB 8327))
Taxonomic identifieri517417 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
ProteomesiUP000008811: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114009Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi517417.Cpar_0738.

Structurei

3D structure databases

ProteinModelPortaliP28462.

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.
OMAiKSNANHV.
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.

P28462-1 [UniParc]FASTAAdd to Basket

« Hide

MNIISVGVNH KTAPIEIRER IALSEVQNKE FVTDLVSSGL ASEAMVVSTC    50
NRTELYVVPG MPEVNCDYLK DYIISYKDAR NAVRPEHFFN RFYCGTARHL 100
FEVSSAIDSL VLGEGQILGQ VKDAYRIAAE VGTAGILLTR LCHTAFSVAK 150
KVKTRTKLME GAVSVSYAAV ELAQKIFSNL SMKKVLLIGA GETGELAAKH 200
MYAKNARNIV ITNRTQSKAE ALAEELGTNR VLPYESYKEH LHEFDIIITA 250
VSTKEYILNA AEMQQSMAKR RLKPVIILDL GLPRNVDPEV GALQNMFLKD 300
IDALKHIIDK NLERRRAELP KVKSIIDEEL IGFGQWINTL KVRPTIVDLQ 350
SKFIEIKEKE LERYRHKVSE EELKRMEHLT DRILKKILHH PIKMLKAPVD 400
TADNIPSKVN LVRNIFDLEE PNQSLQ 426
Length:426
Mass (Da):48,142
Last modified:October 14, 2008 - v3
Checksum:iD169328D709EF697
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti144 – 1452TA → SP in AAC61856. 1 Publication
Sequence conflicti144 – 1452TA → SP in AAA23112. 1 Publication
Sequence conflicti191 – 22333GETGE…AEALA → VKQSWQQSTCTPRTPGTSSS PTGRNPRPRAC in AAC61856. 1 Publication
Add
BLAST
Sequence conflicti191 – 22333GETGE…AEALA → VKQSWQQSTCTPRTPGTSSS PTGRNPRPRAC in AAA23112. 1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M96364 Genomic DNA. Translation: AAA23112.1.
AF080069 Genomic DNA. Translation: AAC61856.1.
CP001099 Genomic DNA. Translation: ACF11155.1.
PIRiA48359.
RefSeqiWP_012501988.1. NC_011027.1.
YP_001998355.1. NC_011027.1.

Genome annotation databases

EnsemblBacteriaiACF11155; ACF11155; Cpar_0738.
GeneIDi6419665.
KEGGicpc:Cpar_0738.
PATRICi21364734. VBIChlPar72705_0737.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M96364 Genomic DNA. Translation: AAA23112.1 .
AF080069 Genomic DNA. Translation: AAC61856.1 .
CP001099 Genomic DNA. Translation: ACF11155.1 .
PIRi A48359.
RefSeqi WP_012501988.1. NC_011027.1.
YP_001998355.1. NC_011027.1.

3D structure databases

ProteinModelPortali P28462.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 517417.Cpar_0738.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACF11155 ; ACF11155 ; Cpar_0738 .
GeneIDi 6419665.
KEGGi cpc:Cpar_0738.
PATRICi 21364734. VBIChlPar72705_0737.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CPAR517417:GH95-766-MONOMER.
BRENDAi 1.2.1.70. 1348.

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. "Structure and expression of the Chlorobium vibrioforme hemA gene."
    Majumdar D., Avissar Y.J., Wyche J.H., Beale S.I.
    Arch. Microbiol. 156:281-289(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Glutamyl-tRNA reductase of Chlorobium vibrioforme is a dissociable homodimer that contains one tightly bound heme per subunit."
    Srivastava A., Beale S.I.
    J. Bacteriol. 187:4444-4450(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO C-TERMINUS, FUNCTION, HEME BINDING, SUBUNIT.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCIB 8327.

Entry informationi

Entry nameiHEM1_CHLP8
AccessioniPrimary (citable) accession number: P28462
Secondary accession number(s): B3QMK2, O87494
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 14, 2008
Last modified: September 3, 2014
This is version 107 of the entry and version 3 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.
Was shown to bind heme, but the precise role of heme is unclear.

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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