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B1KDU4

- HEM1_SHEWM

UniProt

B1KDU4 - HEM1_SHEWM

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Protein

Glutamyl-tRNA reductase

Gene
hemA, Swoo_3686
Organism
Shewanella woodyi (strain ATCC 51908 / MS32)
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 sitei50 – 501Nucleophile By similarity
Sitei95 – 951Important for activity By similarity
Binding sitei105 – 1051Substrate By similarity
Binding sitei116 – 1161Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi185 – 1906NADP By similarity

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

BioCyciSWOO392500:GI2C-3803-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:Swoo_3686
OrganismiShewanella woodyi (strain ATCC 51908 / MS32)
Taxonomic identifieri392500 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000002168: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416Glutamyl-tRNA reductaseUniRule annotationPRO_1000093169Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi392500.Swoo_3686.

Structurei

3D structure databases

ProteinModelPortaliB1KDU4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni110 – 1123Substrate 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.
OMAiAETEIQG.
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.

B1KDU4-1 [UniParc]FASTAAdd to Basket

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MSLVAIGINH KTATVDLREK VAFSPDKIHD AMKSLAKCTK TGEAVIISTC    50
NRTELYTNTG DEAEVIRWFE EYHQLSHEEV EPCLYKFEGQ GVVKHLMRVS 100
SGLDSLILGE PQILGQVKQS FAKAREAGSV AITMDRLFQN TFSVAKKVRT 150
ETEIGAAAVS VAFAAVSMAK HIFSSISSTK VLLIGAGETI ELVARHLKDN 200
GVDSMVVANR TLSRAEGMCD EFGATAITLE QIPDFLPKAD IVISSTASPL 250
PILGKGMVEK ALKQRRHQPM LLVDIAVPRD IEAEVADLDD AFLYTVDDLQ 300
SIIEQNMASR REAAEQAEVI AENESHLFME WVRSLESVDS IREYRTQSMA 350
IKDELVERAI NKLAQGGDSE QLLLELANKL TNKLIHAPTQ ALTAASRQGD 400
LNSIGQLRSA LGLDKN 416
Length:416
Mass (Da):45,574
Last modified:April 29, 2008 - v1
Checksum:i9F4ED1426B16FDD3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000961 Genomic DNA. Translation: ACA87946.1.
RefSeqiWP_012326278.1. NC_010506.1.
YP_001762041.1. NC_010506.1.

Genome annotation databases

EnsemblBacteriaiACA87946; ACA87946; Swoo_3686.
GeneIDi6118020.
KEGGiswd:Swoo_3686.
PATRICi23609995. VBISheWoo126588_3798.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000961 Genomic DNA. Translation: ACA87946.1 .
RefSeqi WP_012326278.1. NC_010506.1.
YP_001762041.1. NC_010506.1.

3D structure databases

ProteinModelPortali B1KDU4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 392500.Swoo_3686.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACA87946 ; ACA87946 ; Swoo_3686 .
GeneIDi 6118020.
KEGGi swd:Swoo_3686.
PATRICi 23609995. VBISheWoo126588_3798.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci SWOO392500:GI2C-3803-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 51908 / MS32.

Entry informationi

Entry nameiHEM1_SHEWM
AccessioniPrimary (citable) accession number: B1KDU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: September 3, 2014
This is version 53 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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