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.

A0RNT0

- HEM1_CAMFF

UniProt

A0RNT0 - HEM1_CAMFF

(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, CFF8240_0688
Organism
Campylobacter fetus subsp. fetus (strain 82-40)
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. NADP binding Source: InterPro
  2. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
Complete GO annotation...

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

BioCyciCFET360106:GHTH-687-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:CFF8240_0688
OrganismiCampylobacter fetus subsp. fetus (strain 82-40)
Taxonomic identifieri360106 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
ProteomesiUP000000760: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Glutamyl-tRNA reductaseUniRule annotation
PRO_1000057571Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi360106.CFF8240_0688.

Structurei

3D structure databases

ProteinModelPortaliA0RNT0.

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.
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.

A0RNT0-1 [UniParc]FASTAAdd to Basket

« Hide

MHYVSISFTH KNTDIGVREK LSFSDNNRRR EILRLIGAND SIAESMALST    50
CNRVEIFAYV LDTQSSIRHI LNSISILTLV PFEALELRAD IYEDQGAIHH 100
LFAVASSLDS LVVGETQIAG QLKEAFKFAY DNEDCGVNIS SAMHFAFKCA 150
AEVRALTTIS KNPVSVSSVA VAKAKEIYGN IGGMSAVVIG AGEMSRLAAQ 200
HLINAEVNVI IINRDEIKAQ TLAKELGELA SYASFDKLSE YINRYRLIFS 250
ATGAPNAIIT NEIIEQKDFH RYFFDIAVPR DIDIEEDEYI HVYAVDDLEE 300
IVRTNLALRE EQASIAYSIV GKSTTSFFKW RLSEGSTPAI KALRLKAKDI 350
ACKEIEKAVK KGYLKCSDQD EASKLVHQVF KAFLHTPSVR LKEKNSDDIL 400
KALEYLFDIK IQKDENLEGN LK 422
Length:422
Mass (Da):47,142
Last modified:January 9, 2007 - v1
Checksum:i9A2B9A3FE3EC3FAB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000487 Genomic DNA. Translation: ABK82043.1.
RefSeqiYP_891863.1. NC_008599.1.

Genome annotation databases

EnsemblBacteriaiABK82043; ABK82043; CFF8240_0688.
GeneIDi4539153.
KEGGicff:CFF8240_0688.
PATRICi20035894. VBICamFet25865_0663.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000487 Genomic DNA. Translation: ABK82043.1 .
RefSeqi YP_891863.1. NC_008599.1.

3D structure databases

ProteinModelPortali A0RNT0.
ModBasei Search...

Protein-protein interaction databases

STRINGi 360106.CFF8240_0688.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABK82043 ; ABK82043 ; CFF8240_0688 .
GeneIDi 4539153.
KEGGi cff:CFF8240_0688.
PATRICi 20035894. VBICamFet25865_0663.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CFET360106:GHTH-687-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. "Sequence of Campylobacter fetus subsp. fetus 82-40."
    Fouts D.E., Nelson K.E.
    Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 82-40.

Entry informationi

Entry nameiHEM1_CAMFF
AccessioniPrimary (citable) accession number: A0RNT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 9, 2007
Last modified: September 3, 2014
This is version 61 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