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Protein

N-acylglucosamine 2-epimerase

Gene

RENBP

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion of N-acetylglucosamine to N-acetylmannosamine. Binds to renin forming a protein complex called high molecular weight (HMW) renin and inhibits renin activity. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway.

Catalytic activityi

N-acyl-D-glucosamine = N-acyl-D-mannosamine.1 Publication

Kineticsi

  1. KM=7.4 mM for N-acetyl-D-glucosamine1 Publication
  2. KM=6.3 mM for N-acetyl-D-mannosamine1 Publication

    pH dependencei

    Optimum pH is 6.8.1 Publication

    Temperature dependencei

    Optimum temperature is 47 degrees Celsius.1 Publication

    Pathwayi: N-acetylneuraminate degradation

    This protein is involved in the pathway N-acetylneuraminate degradation, which is part of Amino-sugar metabolism.
    View all proteins of this organism that are known to be involved in the pathway N-acetylneuraminate degradation and in Amino-sugar metabolism.

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Enzyme and pathway databases

    BRENDAi5.1.3.8. 6170.
    UniPathwayiUPA00629.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acylglucosamine 2-epimerase (EC:5.1.3.8)
    Short name:
    AGE
    Alternative name(s):
    GlcNAc 2-epimerase
    N-acetyl-D-glucosamine 2-epimerase
    Renin-binding protein
    Short name:
    RnBP
    Gene namesi
    Name:RENBP
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    Proteomesi
    • UP000008227 Componenti: Unplaced

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi185 – 1851L → D: Fails to bind renin or to form a dimer. 1 Publication
    Mutagenesisi192 – 1921L → D: Fails to bind renin or to form a dimer. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 402402N-acylglucosamine 2-epimerasePRO_0000208951Add
    BLAST

    Proteomic databases

    PaxDbiP17560.
    PeptideAtlasiP17560.

    Expressioni

    Tissue specificityi

    Kidney, liver, adrenal, and pituitary glands the amount being much greater in kidney than in the other tissues.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000013601.

    Structurei

    Secondary structure

    1
    402
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 2928Combined sources
    Turni33 – 353Combined sources
    Beta strandi36 – 383Combined sources
    Helixi55 – 7117Combined sources
    Helixi73 – 753Combined sources
    Helixi78 – 9417Combined sources
    Beta strandi96 – 983Combined sources
    Beta strandi106 – 1083Combined sources
    Beta strandi114 – 1163Combined sources
    Beta strandi119 – 1213Combined sources
    Helixi122 – 13817Combined sources
    Helixi141 – 15919Combined sources
    Helixi162 – 1654Combined sources
    Beta strandi176 – 1783Combined sources
    Helixi180 – 19314Combined sources
    Helixi197 – 2026Combined sources
    Helixi204 – 21512Combined sources
    Turni220 – 2234Combined sources
    Beta strandi227 – 2304Combined sources
    Helixi238 – 2425Combined sources
    Helixi246 – 26217Combined sources
    Helixi266 – 27611Combined sources
    Helixi278 – 2847Combined sources
    Turni287 – 2893Combined sources
    Turni306 – 3094Combined sources
    Helixi313 – 33018Combined sources
    Helixi333 – 34917Combined sources
    Turni353 – 3553Combined sources
    Beta strandi356 – 3583Combined sources
    Beta strandi368 – 3703Combined sources
    Helixi382 – 40120Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FP3X-ray2.00A/B1-402[»]
    ProteinModelPortaliP17560.
    SMRiP17560. Positions 1-402.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17560.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni185 – 20622Leucine-zipperAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG410IE08. Eukaryota.
    COG2942. LUCA.
    HOGENOMiHOG000252296.
    HOVERGENiHBG054048.
    InParanoidiP17560.
    KOiK01787.

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    [Graphical view]
    SUPFAMiSSF48208. SSF48208. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P17560-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEKERETLQA WKERVGQELD RVMAFWLEHS HDREHGGFFT CLGRDGRVYD
    60 70 80 90 100
    DLKYVWLQGR QVWMYCRLYR KLERFHRPEL LDAAKAGGEF LLRHARVAPP
    110 120 130 140 150
    EKKCAFVLTR DGRPVKVQRS IFSECFYTMA MNELWRVTAE ARYQSEAVDM
    160 170 180 190 200
    MDQIVHWVRE DPSGLGRPQL PGAVASESMA VPMMLLCLVE QLGEEDEELA
    210 220 230 240 250
    GRYAQLGHWC ARRILQHVQR DGQAVLENVS EDGEELSGCL GRHQNPGHAL
    260 270 280 290 300
    EAGWFLLRHS SRSGDAKLRA HVIDTFLLLP FRSGWDADHG GLFYFQDADG
    310 320 330 340 350
    LCPTQLEWAM KLWWPHSEAM IAFLMGYSES GDPALLRLFY QVAEYTFRQF
    360 370 380 390 400
    RDPEYGEWFG YLNREGKVAL TIKGGPFKGC FHVPRCLAMC EEMLSALLSR

    LA
    Length:402
    Mass (Da):46,402
    Last modified:November 9, 2004 - v2
    Checksum:iB8914E76CA4716A6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti149 – 1491D → E in AAA31116 (PubMed:2182620).Curated
    Sequence conflicti289 – 2891H → Y in AAA31116 (PubMed:2182620).Curated
    Sequence conflicti317 – 3182SE → RQ in AAA31116 (PubMed:2182620).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J05399 mRNA. Translation: AAA31116.1.
    D83766 mRNA. Translation: BAA12103.1.
    AY550054 mRNA. Translation: AAS55912.1.
    PIRiA35741.
    RefSeqiNP_999065.1. NM_213900.1.
    UniGeneiSsc.14533.

    Genome annotation databases

    GeneIDi396934.
    KEGGissc:396934.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J05399 mRNA. Translation: AAA31116.1.
    D83766 mRNA. Translation: BAA12103.1.
    AY550054 mRNA. Translation: AAS55912.1.
    PIRiA35741.
    RefSeqiNP_999065.1. NM_213900.1.
    UniGeneiSsc.14533.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FP3X-ray2.00A/B1-402[»]
    ProteinModelPortaliP17560.
    SMRiP17560. Positions 1-402.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000013601.

    Proteomic databases

    PaxDbiP17560.
    PeptideAtlasiP17560.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi396934.
    KEGGissc:396934.

    Organism-specific databases

    CTDi5973.

    Phylogenomic databases

    eggNOGiENOG410IE08. Eukaryota.
    COG2942. LUCA.
    HOGENOMiHOG000252296.
    HOVERGENiHBG054048.
    InParanoidiP17560.
    KOiK01787.

    Enzyme and pathway databases

    UniPathwayiUPA00629.
    BRENDAi5.1.3.8. 6170.

    Miscellaneous databases

    EvolutionaryTraceiP17560.

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    [Graphical view]
    SUPFAMiSSF48208. SSF48208. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Molecular cloning and sequence analysis of a cDNA encoding a porcine kidney renin-binding protein."
      Inoue H., Fukui K., Takahashi S., Miyake Y.
      J. Biol. Chem. 265:6556-6561(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 4-12 AND 326-357.
      Tissue: Kidney.
    2. "Molecular cloning and identification of N-acyl-D-glucosamine 2-epimerase from porcine kidney as a renin-binding protein."
      Maru I., Ohta Y., Murata K., Tsukada Y.
      J. Biol. Chem. 271:16294-16299(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 4-12 AND 86-102, ENZYME ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Kidney cortex.
    3. "Identification of differentially expressed genes in porcine embryos."
      Lee H.Y., Cui X.S., Jeong Y.J., Shin M.L., Hwang K.C., Kim N.H.
      Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 223-402.
    4. "Leucine zipper motif in porcine renin-binding protein (RnBP) and its relationship to the formation of an RnBP-renin heterodimer and an RnBP homodimer."
      Inoue H., Takahashi S., Fukui K., Miyake Y.
      J. Biol. Chem. 266:11896-11900(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN LEUCINE-ZIPPER, MUTAGENESIS OF LEU-185 AND LEU-192.
    5. "Crystal structure of N-acyl-D-glucosamine 2-epimerase from porcine kidney at 2.0 A resolution."
      Itoh T., Mikami B., Maru I., Ohta Y., Hashimoto W., Murata K.
      J. Mol. Biol. 303:733-744(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiRENBP_PIG
    AccessioniPrimary (citable) accession number: P17560
    Secondary accession number(s): Q6QAR6, Q95331
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: November 9, 2004
    Last modified: July 6, 2016
    This is version 101 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.