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N-acylglucosamine 2-epimerase (AGE) (EC 5.1.3.8) (GlcNAc 2-epimerase) (N-acetyl-D-glucosamine 2-epimerase) (Renin-binding protein) (RnBP)

 RENBP_PIG               Reviewed;         402 AA.
P17560; Q6QAR6; Q95331;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
09-NOV-2004, sequence version 2.
28-MAR-2018, entry version 109.
RecName: Full=N-acylglucosamine 2-epimerase;
Short=AGE;
EC=5.1.3.8;
AltName: Full=GlcNAc 2-epimerase;
AltName: Full=N-acetyl-D-glucosamine 2-epimerase;
AltName: Full=Renin-binding protein;
Short=RnBP;
Name=RENBP;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 4-12 AND 326-357.
TISSUE=Kidney;
PubMed=2182620;
Inoue H., Fukui K., Takahashi S., Miyake Y.;
"Molecular cloning and sequence analysis of a cDNA encoding a porcine
kidney renin-binding protein.";
J. Biol. Chem. 265:6556-6561(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 4-12 AND 86-102,
ENZYME ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Kidney cortex;
PubMed=8663114; DOI=10.1074/jbc.271.27.16294;
Maru I., Ohta Y., Murata K., Tsukada Y.;
"Molecular cloning and identification of N-acyl-D-glucosamine 2-
epimerase from porcine kidney as a renin-binding protein.";
J. Biol. Chem. 271:16294-16299(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 223-402.
Lee H.Y., Cui X.S., Jeong Y.J., Shin M.L., Hwang K.C., Kim N.H.;
"Identification of differentially expressed genes in porcine
embryos.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[4]
DOMAIN LEUCINE-ZIPPER, AND MUTAGENESIS OF LEU-185 AND LEU-192.
PubMed=2050686;
Inoue H., Takahashi S., Fukui K., Miyake Y.;
"Leucine zipper motif in porcine renin-binding protein (RnBP) and its
relationship to the formation of an RnBP-renin heterodimer and an RnBP
homodimer.";
J. Biol. Chem. 266:11896-11900(1991).
[5]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=11061972; DOI=10.1006/jmbi.2000.4188;
Itoh T., Mikami B., Maru I., Ohta Y., Hashimoto W., Murata K.;
"Crystal structure of N-acyl-D-glucosamine 2-epimerase from porcine
kidney at 2.0 A resolution.";
J. Mol. Biol. 303:733-744(2000).
-!- FUNCTION: 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 ACTIVITY: N-acyl-D-glucosamine = N-acyl-D-mannosamine.
{ECO:0000269|PubMed:8663114}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.4 mM for N-acetyl-D-glucosamine
{ECO:0000269|PubMed:8663114};
KM=6.3 mM for N-acetyl-D-mannosamine
{ECO:0000269|PubMed:8663114};
pH dependence:
Optimum pH is 6.8. {ECO:0000269|PubMed:8663114};
Temperature dependence:
Optimum temperature is 47 degrees Celsius.
{ECO:0000269|PubMed:8663114};
-!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8663114}.
-!- TISSUE SPECIFICITY: Kidney, liver, adrenal, and pituitary glands
the amount being much greater in kidney than in the other tissues.
-!- SIMILARITY: Belongs to the N-acylglucosamine 2-epimerase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J05399; AAA31116.1; -; mRNA.
EMBL; D83766; BAA12103.1; -; mRNA.
EMBL; AY550054; AAS55912.1; -; mRNA.
PIR; A35741; A35741.
RefSeq; NP_999065.1; NM_213900.1.
UniGene; Ssc.14533; -.
PDB; 1FP3; X-ray; 2.00 A; A/B=1-402.
PDBsum; 1FP3; -.
ProteinModelPortal; P17560; -.
SMR; P17560; -.
STRING; 9823.ENSSSCP00000013601; -.
PaxDb; P17560; -.
PeptideAtlas; P17560; -.
PRIDE; P17560; -.
Ensembl; ENSSSCT00000035242; ENSSSCP00000029971; ENSSSCG00000012792.
GeneID; 396934; -.
KEGG; ssc:396934; -.
CTD; 5973; -.
eggNOG; ENOG410IE08; Eukaryota.
eggNOG; COG2942; LUCA.
GeneTree; ENSGT00390000013740; -.
HOGENOM; HOG000252296; -.
HOVERGEN; HBG054048; -.
InParanoid; P17560; -.
KO; K01787; -.
BRENDA; 5.1.3.8; 6170.
Reactome; R-SSC-446210; Synthesis of UDP-N-acetyl-glucosamine.
UniPathway; UPA00629; -.
EvolutionaryTrace; P17560; -.
Proteomes; UP000008227; Chromosome X.
ExpressionAtlas; P17560; differential.
GO; GO:0004866; F:endopeptidase inhibitor activity; IBA:GO_Central.
GO; GO:0050121; F:N-acylglucosamine 2-epimerase activity; ISS:UniProtKB.
GO; GO:0006044; P:N-acetylglucosamine metabolic process; IBA:GO_Central.
GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
CDD; cd00249; AGE; 1.
Gene3D; 1.50.10.10; -; 1.
InterPro; IPR008928; 6-hairpin_glycosidase_sf.
InterPro; IPR012341; 6hp_glycosidase-like_sf.
InterPro; IPR034116; AGE_dom.
SUPFAM; SSF48208; SSF48208; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing; Isomerase;
Reference proteome.
CHAIN 1 402 N-acylglucosamine 2-epimerase.
/FTId=PRO_0000208951.
REGION 185 206 Leucine-zipper.
MUTAGEN 185 185 L->D: Fails to bind renin or to form a
dimer. {ECO:0000269|PubMed:2050686}.
MUTAGEN 192 192 L->D: Fails to bind renin or to form a
dimer. {ECO:0000269|PubMed:2050686}.
CONFLICT 149 149 D -> E (in Ref. 1; AAA31116).
{ECO:0000305}.
CONFLICT 289 289 H -> Y (in Ref. 1; AAA31116).
{ECO:0000305}.
CONFLICT 317 318 SE -> RQ (in Ref. 1; AAA31116).
{ECO:0000305}.
HELIX 2 29 {ECO:0000244|PDB:1FP3}.
TURN 33 35 {ECO:0000244|PDB:1FP3}.
STRAND 36 38 {ECO:0000244|PDB:1FP3}.
HELIX 55 71 {ECO:0000244|PDB:1FP3}.
HELIX 73 75 {ECO:0000244|PDB:1FP3}.
HELIX 78 94 {ECO:0000244|PDB:1FP3}.
STRAND 96 98 {ECO:0000244|PDB:1FP3}.
STRAND 106 108 {ECO:0000244|PDB:1FP3}.
STRAND 114 116 {ECO:0000244|PDB:1FP3}.
STRAND 119 121 {ECO:0000244|PDB:1FP3}.
HELIX 122 138 {ECO:0000244|PDB:1FP3}.
HELIX 141 159 {ECO:0000244|PDB:1FP3}.
HELIX 162 165 {ECO:0000244|PDB:1FP3}.
STRAND 176 178 {ECO:0000244|PDB:1FP3}.
HELIX 180 193 {ECO:0000244|PDB:1FP3}.
HELIX 197 202 {ECO:0000244|PDB:1FP3}.
HELIX 204 215 {ECO:0000244|PDB:1FP3}.
TURN 220 223 {ECO:0000244|PDB:1FP3}.
STRAND 227 230 {ECO:0000244|PDB:1FP3}.
HELIX 238 242 {ECO:0000244|PDB:1FP3}.
HELIX 246 262 {ECO:0000244|PDB:1FP3}.
HELIX 266 276 {ECO:0000244|PDB:1FP3}.
HELIX 278 284 {ECO:0000244|PDB:1FP3}.
TURN 287 289 {ECO:0000244|PDB:1FP3}.
TURN 306 309 {ECO:0000244|PDB:1FP3}.
HELIX 313 330 {ECO:0000244|PDB:1FP3}.
HELIX 333 349 {ECO:0000244|PDB:1FP3}.
TURN 353 355 {ECO:0000244|PDB:1FP3}.
STRAND 356 358 {ECO:0000244|PDB:1FP3}.
STRAND 368 370 {ECO:0000244|PDB:1FP3}.
HELIX 382 401 {ECO:0000244|PDB:1FP3}.
SEQUENCE 402 AA; 46402 MW; B8914E76CA4716A6 CRC64;
MEKERETLQA WKERVGQELD RVMAFWLEHS HDREHGGFFT CLGRDGRVYD DLKYVWLQGR
QVWMYCRLYR KLERFHRPEL LDAAKAGGEF LLRHARVAPP EKKCAFVLTR DGRPVKVQRS
IFSECFYTMA MNELWRVTAE ARYQSEAVDM MDQIVHWVRE DPSGLGRPQL PGAVASESMA
VPMMLLCLVE QLGEEDEELA GRYAQLGHWC ARRILQHVQR DGQAVLENVS EDGEELSGCL
GRHQNPGHAL EAGWFLLRHS SRSGDAKLRA HVIDTFLLLP FRSGWDADHG GLFYFQDADG
LCPTQLEWAM KLWWPHSEAM IAFLMGYSES GDPALLRLFY QVAEYTFRQF RDPEYGEWFG
YLNREGKVAL TIKGGPFKGC FHVPRCLAMC EEMLSALLSR LA


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