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B8G817

- HEM1_CHLAD

UniProt

B8G817 - HEM1_CHLAD

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Cagg_1288
Organism
Chloroflexus aggregans (strain MD-66 / DSM 9485)
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 sitei55 – 551Nucleophile By similarity
Sitei103 – 1031Important for activity By similarity
Binding sitei113 – 1131Substrate By similarity
Binding sitei124 – 1241Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi193 – 1986NADP 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

BioCyciCAGG326427:GHS8-1301-MONOMER.
UniPathwayiUPA00251; UER00316.
UPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:Cagg_1288
OrganismiChloroflexus aggregans (strain MD-66 / DSM 9485)
Taxonomic identifieri326427 [NCBI]
Taxonomic lineageiBacteriaChloroflexiChloroflexiaChloroflexalesChloroflexineaeChloroflexaceaeChloroflexus
ProteomesiUP000002508: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453Glutamyl-tRNA reductaseUniRule annotation
PRO_1000190511Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi326427.Cagg_1288.

Structurei

3D structure databases

ProteinModelPortaliB8G817.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 574Substrate binding By similarity
Regioni118 – 1203Substrate 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.
HOGENOMiHOG000109650.
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.
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.

Sequencei

Sequence statusi: Complete.

B8G817-1 [UniParc]FASTAAdd to Basket

« Hide

MNLFLAGLDH TTAPVEIREQ LAFSQTDLPS ALLQLTQADN GSPPLFTEAV    50
ILSTCNRVEI YGVANPGTTA QHVVDFLANF HRRPAGSFVH TLYFYQGEAV 100
ARHLCATAAG LRSLVLGEAQ IQGQVRSAYE AAQRIGSVGS VLHRLFQIAL 150
VAGKRVRHET TIGKGAASVS QAGVELARRR LGDLRGREVL LIGGGEVSEL 200
AAQNLIANGA DRLTIVNRTS SRAAALAERY GAEMLDFGAL PEALARADIV 250
ISSTAAPVPI IYRHHIAEAL SHKQRMRACG DCDPPAMLLI DLAVPRDIAA 300
DVAELPGVYL FTVDDLREVV SHTIELRSAV IDIANQIVEE QVREFSDWLR 350
TQEALPVLTM LRQRAEEVRN EELTRALRRL HDLSPEQRAV IEGLSRSIVN 400
KLLHPPTRCL REAAAHGQGK RYATMLAELF NLEHALEHKA GAMGNTELTD 450
RMR 453
Length:453
Mass (Da):49,496
Last modified:March 3, 2009 - v1
Checksum:i4D3B325E808BA6CE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001337 Genomic DNA. Translation: ACL24196.1.
RefSeqiWP_012616560.1. NC_011831.1.
YP_002462632.1. NC_011831.1.

Genome annotation databases

EnsemblBacteriaiACL24196; ACL24196; Cagg_1288.
GeneIDi7266274.
KEGGicag:Cagg_1288.
PATRICi21405082. VBIChlAgg85409_1336.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001337 Genomic DNA. Translation: ACL24196.1 .
RefSeqi WP_012616560.1. NC_011831.1.
YP_002462632.1. NC_011831.1.

3D structure databases

ProteinModelPortali B8G817.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 326427.Cagg_1288.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACL24196 ; ACL24196 ; Cagg_1288 .
GeneIDi 7266274.
KEGGi cag:Cagg_1288.
PATRICi 21405082. VBIChlAgg85409_1336.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
UPA00668 .
BioCyci CAGG326427:GHS8-1301-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.
TIGRFAMsi TIGR01035. hemA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of Chloroflexus aggregans DSM 9485."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.
    Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MD-66 / DSM 9485.

Entry informationi

Entry nameiHEM1_CHLAD
AccessioniPrimary (citable) accession number: B8G817
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: September 3, 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 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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