SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A7GYU7

- HEM1_CAMC5

UniProt

A7GYU7 - HEM1_CAMC5

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamyl-tRNA reductase

Gene
hemA, Ccur92_10850, CCV52592_0764
Organism
Campylobacter curvus (strain 525.92)
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 sitei51 – 511Nucleophile By similarity
Sitei100 – 1001Important for activity By similarity
Binding sitei110 – 1101Substrate By similarity
Binding sitei121 – 1211Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi190 – 1956NADP By similarity

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

BioCyciCCUR360105:GJ9P-1184-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:Ccur92_10850
ORF Names:CCV52592_0764
OrganismiCampylobacter curvus (strain 525.92)
Taxonomic identifieri360105 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
ProteomesiUP000006380: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Glutamyl-tRNA reductaseUniRule annotationPRO_0000335020Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi360105.CCV52592_0764.

Structurei

3D structure databases

ProteinModelPortaliA7GYU7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate binding By similarity
Regioni115 – 1173Substrate 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.
OMAiLAHKLTN.
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.
IPR018073. Prot_inh_cystat_CS.
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.

A7GYU7-1 [UniParc]FASTAAdd to Basket

« Hide

MHYLNISFTY KNTDISVREK LAFDSDEKKD QILRLLKSSK NIIECMVLST    50
CNRVEVLAYT NDIKSAMTHI IRCLTVYSGV FEDELFERAD IYEDSGAVHH 100
LFAVASSLDS LVVGETQIVG QLKNAFKFAF DNASSGEHIS RLVHYACKCA 150
ARVRNETQIS KNPISVSSVA VAKAKEIFGT LENKTAVVIG AGEMGELAAK 200
HLITSGANVI IINRSSDHVE ELVENLGDKA SWDSILKLKE YINKYDLIFS 250
STSAPHAIIT GELIEPQEFR RYFFDIAVPR DIDLVNTDKI SVYSVDSLEE 300
MVRRNLALRE EQAQTAYSIV GQSTNEFLKF LKDNISIPLI KTIRKKAEIC 350
AEAELEKALK KGYLKHSDKE EAAKLIHQVF KAFLHSPTIN LKSLASKNDA 400
EQIAGGIKFL FDIKEENLEN LTKDIDEI 428
Length:428
Mass (Da):47,977
Last modified:September 11, 2007 - v1
Checksum:i6B0B44CB6ABDABD0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000767 Genomic DNA. Translation: EAT99944.1.
RefSeqiYP_001408389.1. NC_009715.1.

Genome annotation databases

EnsemblBacteriaiEAT99944; EAT99944; CCV52592_0764.
GeneIDi5407303.
KEGGiccv:CCV52592_0764.
PATRICi20032676. VBICamCur47627_1145.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000767 Genomic DNA. Translation: EAT99944.1 .
RefSeqi YP_001408389.1. NC_009715.1.

3D structure databases

ProteinModelPortali A7GYU7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 360105.CCV52592_0764.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai EAT99944 ; EAT99944 ; CCV52592_0764 .
GeneIDi 5407303.
KEGGi ccv:CCV52592_0764.
PATRICi 20032676. VBICamCur47627_1145.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CCUR360105:GJ9P-1184-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.
IPR018073. Prot_inh_cystat_CS.
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. "Genome sequence of Campylobacter curvus 525.92 isolated from human feces."
    Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E.
    Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 525.92.

Entry informationi

Entry nameiHEM1_CAMC5
AccessioniPrimary (citable) accession number: A7GYU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 11, 2007
Last modified: September 3, 2014
This is version 60 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

Similar proteinsi