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Protein

N-acylglucosamine 2-epimerase

Gene

RENBP

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: -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

    Keywordsi

    Molecular functionIsomerase

    Enzyme and pathway databases

    BRENDAi5.1.3.8 6170
    ReactomeiR-SSC-446210 Synthesis of UDP-N-acetyl-glucosamine
    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: Chromosome X

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi185L → D: Fails to bind renin or to form a dimer. 1 Publication1
    Mutagenesisi192L → D: Fails to bind renin or to form a dimer. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002089511 – 402N-acylglucosamine 2-epimeraseAdd BLAST402

    Proteomic databases

    PaxDbiP17560
    PeptideAtlasiP17560
    PRIDEiP17560

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ExpressionAtlasiP17560 baseline and differential

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000013601

    Structurei

    Secondary structure

    1402
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi2 – 29Combined sources28
    Turni33 – 35Combined sources3
    Beta strandi36 – 38Combined sources3
    Helixi55 – 71Combined sources17
    Helixi73 – 75Combined sources3
    Helixi78 – 94Combined sources17
    Beta strandi96 – 98Combined sources3
    Beta strandi106 – 108Combined sources3
    Beta strandi114 – 116Combined sources3
    Beta strandi119 – 121Combined sources3
    Helixi122 – 138Combined sources17
    Helixi141 – 159Combined sources19
    Helixi162 – 165Combined sources4
    Beta strandi176 – 178Combined sources3
    Helixi180 – 193Combined sources14
    Helixi197 – 202Combined sources6
    Helixi204 – 215Combined sources12
    Turni220 – 223Combined sources4
    Beta strandi227 – 230Combined sources4
    Helixi238 – 242Combined sources5
    Helixi246 – 262Combined sources17
    Helixi266 – 276Combined sources11
    Helixi278 – 284Combined sources7
    Turni287 – 289Combined sources3
    Turni306 – 309Combined sources4
    Helixi313 – 330Combined sources18
    Helixi333 – 349Combined sources17
    Turni353 – 355Combined sources3
    Beta strandi356 – 358Combined sources3
    Beta strandi368 – 370Combined sources3
    Helixi382 – 401Combined sources20

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP17560

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni185 – 206Leucine-zipperAdd BLAST22

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG410IE08 Eukaryota
    COG2942 LUCA
    GeneTreeiENSGT00390000013740
    HOGENOMiHOG000252296
    HOVERGENiHBG054048
    InParanoidiP17560
    KOiK01787

    Family and domain databases

    CDDicd00249 AGE, 1 hit
    Gene3Di1.50.10.10, 1 hit
    InterProiView protein in InterPro
    IPR008928 6-hairpin_glycosidase_sf
    IPR012341 6hp_glycosidase-like_sf
    IPR034116 AGE_dom
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti149D → E in AAA31116 (PubMed:2182620).Curated1
    Sequence conflicti289H → Y in AAA31116 (PubMed:2182620).Curated1
    Sequence conflicti317 – 318SE → RQ in AAA31116 (PubMed:2182620).Curated2

    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

    EnsembliENSSSCT00000035242; ENSSSCP00000029971; ENSSSCG00000012792
    GeneIDi396934
    KEGGissc:396934

    Similar proteinsi

    Entry informationi

    Entry nameiRENBP_PIG
    AccessioniPrimary (citable) accession number: P17560
    Secondary accession number(s): Q6QAR6, Q95331
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: November 9, 2004
    Last modified: May 23, 2018
    This is version 110 of the entry and version 2 of the sequence. See 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

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