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B1I4J1

- HEM1_DESAP

UniProt

B1I4J1 - HEM1_DESAP

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Desulforudis audaxviator (strain MP104C)
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 sitei50 – 501NucleophileUniRule annotation
Sitei98 – 981Important for activityUniRule annotation
Binding sitei108 – 1081SubstrateUniRule annotation
Binding sitei119 – 1191SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi188 – 1936NADPUniRule 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

BioCyciDAUD477974:GH0B-1377-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:Daud_1348
OrganismiDesulforudis audaxviator (strain MP104C)
Taxonomic identifieri477974 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeCandidatus Desulforudis
ProteomesiUP000008544: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446Glutamyl-tRNA reductasePRO_1000093131Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi477974.Daud_1348.

Structurei

3D structure databases

ProteinModelPortaliB1I4J1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni113 – 1153Substrate 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.
HOGENOMiHOG000109651.
KOiK02492.
OMAiLNKQFET.
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.

B1I4J1-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MLITVVGLNH RTAPLAVREK LSFPEHTLKE VLRGLSDREG VESCVVISTC
60 70 80 90 100
NRTEVYAVLS EEDGLQNIWC FLAERCGSPV EAIKSHTYNY SFGESVRHLF
110 120 130 140 150
RVSSGLDSMV LGETQILGQV KQAYQFAQQV GTVNWLLNCA FQQALAVGKR
160 170 180 190 200
VRTETGIDKN PVSISYAAVE LARQTLGSLE GREVLIVGAG KMSELTVKHL
210 220 230 240 250
LSHGVAGVIV SNRSYPRAVE LAAQFGGRAV RFDELYRWMG HADIVISCTA
260 270 280 290 300
ASHYVIRAEP MTSVLAERGG RAIFFIDIAV PRDVDPAVGH LPGVVLYDID
310 320 330 340 350
SLQSVVDANL AERRRAAVAA ERIIDAEVRE FLLALGSRFV IPTVVALKKR
360 370 380 390 400
GEEIKRNELD RALNRLGGEL SERELKVISS MANSIVSQLL HEPITRLKKL
410 420 430 440
ALTPEGHFYS DALQKLFNLE PENGGVPTLV GRTESCPVSC LKGKGC
Length:446
Mass (Da):48,858
Last modified:April 29, 2008 - v1
Checksum:i63B174393A2941FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000860 Genomic DNA. Translation: ACA59857.1.
RefSeqiYP_001717489.1. NC_010424.1.

Genome annotation databases

EnsemblBacteriaiACA59857; ACA59857; Daud_1348.
GeneIDi6026143.
KEGGidau:Daud_1348.
PATRICi31969510. VBICanDes92303_1392.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000860 Genomic DNA. Translation: ACA59857.1 .
RefSeqi YP_001717489.1. NC_010424.1.

3D structure databases

ProteinModelPortali B1I4J1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 477974.Daud_1348.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACA59857 ; ACA59857 ; Daud_1348 .
GeneIDi 6026143.
KEGGi dau:Daud_1348.
PATRICi 31969510. VBICanDes92303_1392.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci DAUD477974:GH0B-1377-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 sequence of chromosome of Desulforudis audaxviator MP104C."
    Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L., Hauser L., Kyrpides N., Ivanova N.N., Richardson P.
    Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MP104C.

Entry informationi

Entry nameiHEM1_DESAP
AccessioniPrimary (citable) accession number: B1I4J1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: November 26, 2014
This is version 52 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