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B2ULP2

- HEM1_AKKM8

UniProt

B2ULP2 - HEM1_AKKM8

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Amuc_0091
Organism
Akkermansia muciniphila (strain ATCC BAA-835)
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
Sitei98 – 981Important for activity By similarity
Binding sitei108 – 1081Substrate By similarity
Binding sitei119 – 1191Substrate By similarity

Regions

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

BioCyciAMUC349741:GHZ7-99-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:Amuc_0091
OrganismiAkkermansia muciniphila (strain ATCC BAA-835)
Taxonomic identifieri349741 [NCBI]
Taxonomic lineageiBacteriaVerrucomicrobiaVerrucomicrobiaeVerrucomicrobialesVerrucomicrobiaceaeAkkermansia
ProteomesiUP000001031: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 340340Glutamyl-tRNA reductaseUniRule annotation
PRO_1000093112Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi349741.Amuc_0091.

Structurei

3D structure databases

ProteinModelPortaliB2ULP2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni113 – 1153Substrate 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.
HOGENOMiHOG000109651.
KOiK02492.
OMAiLNKQFET.
OrthoDBiEOG6MWNBM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.

Sequencei

Sequence statusi: Complete.

B2ULP2-1 [UniParc]FASTAAdd to Basket

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MRMVCLGLNH RTAPVEIRER FAVPSHKLRE EGQRIRSLPG VDQCVVLSTC    50
NRMEIYYWSN APENAQEHIL SHFLGDGRGE LDMASYFYSH QGEDALGHLC 100
RVLSGLDSMV LGETEIFGQV KTAYQTALDA GVTAACANKT FQKAFTIGKK 150
VRTESQIHAG ATSVGSVAVE LAEQIFGDLS GTRVLILGAG EMSRVTGRAL 200
HARGAEGIYV ANRSFDRAVE LAGMIGGQAI RYDVWGNYLR DIDVVVAATA 250
APHCIITRET LLPLRASRKY RSLFLIDISV PRNISPDVAD IDEVYLYDID 300
TLTQLADEAK RSRKQEVSRC EAIIRDSISR YFPDSALYDQ 340
Length:340
Mass (Da):37,606
Last modified:July 1, 2008 - v1
Checksum:i27D3C2F5FF5D3612
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001071 Genomic DNA. Translation: ACD03936.1.
RefSeqiWP_012419151.1. NC_010655.1.
YP_001876717.1. NC_010655.1.

Genome annotation databases

EnsemblBacteriaiACD03936; ACD03936; Amuc_0091.
GeneIDi6274993.
KEGGiamu:Amuc_0091.
PATRICi20832684. VBIAkkMuc16855_0109.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001071 Genomic DNA. Translation: ACD03936.1 .
RefSeqi WP_012419151.1. NC_010655.1.
YP_001876717.1. NC_010655.1.

3D structure databases

ProteinModelPortali B2ULP2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 349741.Amuc_0091.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACD03936 ; ACD03936 ; Amuc_0091 .
GeneIDi 6274993.
KEGGi amu:Amuc_0091.
PATRICi 20832684. VBIAkkMuc16855_0109.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci AMUC349741:GHZ7-99-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view ]
Pfami PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMi SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of Akkermansia muciniphila ATCC BAA-835."
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N.
    , Smidt H., Derrien M., Plugge C.M., Zoetendal E.G., de Vos W.M., Richardson P.
    Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-835.

Entry informationi

Entry nameiHEM1_AKKM8
AccessioniPrimary (citable) accession number: B2ULP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 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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