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B0VTW7

- HEM1_ACIBS

UniProt

B0VTW7 - HEM1_ACIBS

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Protein
Glutamyl-tRNA reductase
Gene
hemA, ABSDF2623
Organism
Acinetobacter baumannii (strain SDF)
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. 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

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:ABSDF2623
OrganismiAcinetobacter baumannii (strain SDF)
Taxonomic identifieri509170 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex
ProteomesiUP000001741: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427Glutamyl-tRNA reductaseUniRule annotation
PRO_1000093108Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi509170.ABSDF2623.

Structurei

3D structure databases

ProteinModelPortaliB0VTW7.

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.
OMAiLAHKLTN.
OrthoDBiEOG6MWNBM.

Family and domain databases

Gene3Di1.10.1200.70. 1 hit.
3.40.50.720. 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.

B0VTW7-1 [UniParc]FASTAAdd to Basket

« Hide

MSFFALGVNH QTASVELREQ IAFNAERLSN LLAEQRHHES LKDLVVVSTC    50
NRTEVYAMAE DAESLLKWLA DANNIDVKQL IHHVYRYENA QAITHLMRVA 100
SGLDSLMLGE PQILGQVKSA LALSKEAQTV SPELNSVFEY AFYAAKRVRS 150
ETAVGSHAVS MGYAVAQLAL QVFSKPEKLT VMVVAAGEMN SLVAKHLAEM 200
GVAKMIICNR SRERADQLAQ EIAHQVEVEI IDFSDLAENL YRADVVSSCT 250
GSLHQVIAYA DVKTALKKRR YQQMLMVDLA VPRDIDPKVE SLDGVYLYGV 300
DDLQSVIDEN LAQRRQAAVE AEVMVNQLAT QLITHQKVKE AGSTIHAYRQ 350
HSEEISQREL THALEALHHG GNPEQVLQQF AHRLTQKLIH PTSMLLREAA 400
KAESPDYFEW LQQHLQDVFD HERKPKR 427
Length:427
Mass (Da):47,964
Last modified:June 10, 2008 - v1
Checksum:iA42E068563D88393
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU468230 Genomic DNA. Translation: CAP01930.1.
RefSeqiYP_001707836.1. NC_010400.1.

Genome annotation databases

EnsemblBacteriaiCAP01930; CAP01930; ABSDF2623.
GeneIDi5986708.
KEGGiabm:ABSDF2623.
PATRICi20735969. VBIAciBau88365_2489.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU468230 Genomic DNA. Translation: CAP01930.1 .
RefSeqi YP_001707836.1. NC_010400.1.

3D structure databases

ProteinModelPortali B0VTW7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 509170.ABSDF2623.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAP01930 ; CAP01930 ; ABSDF2623 .
GeneIDi 5986708.
KEGGi abm:ABSDF2623.
PATRICi 20735969. VBIAciBau88365_2489.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .

Family and domain databases

Gene3Di 1.10.1200.70. 1 hit.
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: SDF.

Entry informationi

Entry nameiHEM1_ACIBS
AccessioniPrimary (citable) accession number: B0VTW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: September 3, 2014
This is version 50 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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