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A7I1R7

- HEM1_CAMHC

UniProt

A7I1R7 - HEM1_CAMHC

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Protein
Glutamyl-tRNA reductase
Gene
hemA, CHAB381_0896
Organism
Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A)
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

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

BioCyciCHOM360107:GHCX-900-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:CHAB381_0896
OrganismiCampylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A)
Taxonomic identifieri360107 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
ProteomesiUP000002407: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Glutamyl-tRNA reductaseUniRule annotation
PRO_1000057572Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi360107.CHAB381_0896.

Structurei

3D structure databases

ProteinModelPortaliA7I1R7.

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.

A7I1R7-1 [UniParc]FASTAAdd to Basket

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MNYMSVSFTH KNTDIIVREK LSFANDVKKR EILKLICSNK AIKECLVLST    50
CNRVEVLAYI DDFNYTSDYV IKAISKLSGV DFDELKERAD IYEDDGAIHH 100
LFSVASSLDS LVVGETQIVG QLKDAYNFAK NERKSGVMLD LAINSALKCA 150
AVIRSKTDIS KNPISVASVA VCMAREKIGD LGGTTAVVVG AGEMAELACK 200
HLITHKAKVI IINRNIDHAK KLAESLGENA SIAEFSNLGE FINKYALIFS 250
ATGANKPIIT DLLAKPQNFK RYFFDIAVPR DIDITCDDLS EVYAVDDLEE 300
IVRKNLLLRE EQAQIAYSIV GRETTKFYKD LKTLSSTPII KALRNSAKKV 350
AETELKKAIK RGYLRHSDID EARKLIHQVF KAFLHTPTVN LKNLDENAQN 400
DINAIAEIFG IEEDFDKFCE NSLENKNEI 429
Length:429
Mass (Da):47,896
Last modified:September 11, 2007 - v1
Checksum:i24112E1047B97089
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000776 Genomic DNA. Translation: ABS52226.1.
RefSeqiWP_012108749.1. NC_009714.1.
YP_001406458.1. NC_009714.1.

Genome annotation databases

EnsemblBacteriaiABS52226; ABS52226; CHAB381_0896.
GeneIDi5408761.
KEGGicha:CHAB381_0896.
PATRICi20039928. VBICamHom81367_0860.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000776 Genomic DNA. Translation: ABS52226.1 .
RefSeqi WP_012108749.1. NC_009714.1.
YP_001406458.1. NC_009714.1.

3D structure databases

ProteinModelPortali A7I1R7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 360107.CHAB381_0896.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABS52226 ; ABS52226 ; CHAB381_0896 .
GeneIDi 5408761.
KEGGi cha:CHAB381_0896.
PATRICi 20039928. VBICamHom81367_0860.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CHOM360107:GHCX-900-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. "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a commensal isolated from the human gastrointestinal tract."
    Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Nelson K.E.
    Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A.

Entry informationi

Entry nameiHEM1_CAMHC
AccessioniPrimary (citable) accession number: A7I1R7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 11, 2007
Last modified: September 3, 2014
This is version 57 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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