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A4XK04

- HEM1_CALS8

UniProt

A4XK04 - HEM1_CALS8

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903)
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).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 sitei46 – 461NucleophileUniRule annotation
Sitei89 – 891Important for activityUniRule annotation
Binding sitei99 – 991SubstrateUniRule annotation
Binding sitei110 – 1101SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi175 – 1806NADPUniRule annotation

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

BioCyciCSAC351627:GJ17-1687-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
Ordered Locus Names:Csac_1649
OrganismiCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903)
Taxonomic identifieri351627 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor
ProteomesiUP000000256: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Glutamyl-tRNA reductasePRO_1000004603Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi351627.Csac_1649.

Structurei

3D structure databases

ProteinModelPortaliA4XK04.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 484Substrate bindingUniRule annotation
Regioni104 – 1063Substrate bindingUniRule annotation

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.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000090159.
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.

A4XK04-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLWVIGINHK VEVDIRQKFS LTKTKLQEKL ISLKKLADEV IILSTCNRTE
60 70 80 90 100
IYFFSEEYVD IEKIFTELDW DRRYMPLFYI YKDKDCIKHL FEVVCGFDSL
110 120 130 140 150
LIGEEQIVAQ VKEAKDIAKQ VGGKNPVLER LFEVALKCSK EFRTKARLNE
160 170 180 190 200
HPITIASVVG KVLKESNIRK IAIIGLGNIG FLFCNYFKNS DVDKVFLIGR
210 220 230 240 250
KNERIDQFVK LYPGKFEYSD KKDAISEAQC LICSTSAPHA VVHKDDIPDG
260 270 280 290 300
KNLLIFDLAV PRDVDVEVYK LPNVKVIDID QVHKMDATSR EIRISKMQEN
310 320 330 340 350
YNIIEKYIDE FIEWLGFRQY RNLIIEVKRH AEQLCKAQVK YLKNVDSRER
360 370 380 390
EEVERLLIRM ANLYIDRAIE VLREAHKEGS GEICSNLIKR IFLK
Length:394
Mass (Da):46,005
Last modified:May 29, 2007 - v1
Checksum:i375F79C2B3BD64E1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000679 Genomic DNA. Translation: ABP67239.1.
RefSeqiYP_001180430.1. NC_009437.1.

Genome annotation databases

EnsemblBacteriaiABP67239; ABP67239; Csac_1649.
GeneIDi5088968.
KEGGicsc:Csac_1649.
PATRICi21253014. VBICalSac56748_1816.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000679 Genomic DNA. Translation: ABP67239.1 .
RefSeqi YP_001180430.1. NC_009437.1.

3D structure databases

ProteinModelPortali A4XK04.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 351627.Csac_1649.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABP67239 ; ABP67239 ; Csac_1649 .
GeneIDi 5088968.
KEGGi csc:Csac_1649.
PATRICi 21253014. VBICalSac56748_1816.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000090159.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CSAC351627:GJ17-1687-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43494 / DSM 8903.

Entry informationi

Entry nameiHEM1_CALS8
AccessioniPrimary (citable) accession number: A4XK04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: October 1, 2014
This is version 55 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.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3