ID   ASPG_ELIMR              Reviewed;         340 AA.
AC   Q47898;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 68.
DE   RecName: Full=N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase;
DE            EC=3.5.1.26;
DE   AltName: Full=Glycosylasparaginase;
DE   AltName: Full=Aspartylglucosaminidase;
DE            Short=AGA;
DE   AltName: Full=N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase;
DE   Contains:
DE     RecName: Full=Glycosylasparaginase alpha chain;
DE   Contains:
DE     RecName: Full=Glycosylasparaginase beta chain;
DE   Flags: Precursor;
OS   Elizabethkingia miricola (Chryseobacterium miricola).
OC   Bacteria; Bacteroidetes; Flavobacteria; Flavobacteriales;
OC   Flavobacteriaceae; Elizabethkingia.
OX   NCBI_TaxID=172045;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 33958;
RX   MEDLINE=95142655; PubMed=7840643; DOI=10.1006/abbi.1995.1053;
RA   Tarentino A.L., Quinones G., Hauer C.R., Changchien L.-M.,
RA   Plummer T.H. Jr.;
RT   "Molecular cloning and sequence analysis of Flavobacterium
RT   meningosepticum glycosylasparaginase: a single gene encodes the alpha
RT   and beta subunits.";
RL   Arch. Biochem. Biophys. 316:399-406(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 46-59 AND 197-211.
RX   MEDLINE=94071939; PubMed=8250923; DOI=10.1006/bbrc.1993.2457;
RA   Tarentino A.L., Plummer T.H. Jr.;
RT   "The first demonstration of a procaryotic glycosylasparaginase.";
RL   Biochem. Biophys. Res. Commun. 197:179-186(1993).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS).
RX   MEDLINE=98200483; PubMed=9541410;
RA   Xuan J., Tarentino A.L., Grimwood B.G., Plummer T.H. Jr., Cui T.,
RA   Guan C., van Roey P.;
RT   "Crystal structure of glycosylasparaginase from Flavobacterium
RT   meningosepticum.";
RL   Protein Sci. 7:774-781(1998).
CC   -!- FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides
CC       to the peptide of asparagine-linked glycoproteins. Requires that
CC       the glycosylated asparagine moiety is not substituted on its N-
CC       (R1) and C- (R2) terminus.
CC   -!- CATALYTIC ACTIVITY: N(4)-(beta-N-acetyl-D-glucosaminyl)-L-
CC       asparagine + H(2)O = N-acetyl-beta-D-glucosaminylamine + L-
CC       aspartate.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged
CC       as a dimer of alpha/beta heterodimers.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the Ntn-hydrolase family.
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DR   EMBL; U08028; AAA68868.1; -; Genomic_DNA.
DR   PIR; S69194; S69194.
DR   PDB; 1AYY; X-ray; 2.32 A; A/C=46-196, B/D=197-340.
DR   PDB; 1P4K; X-ray; 1.90 A; A/C=46-340.
DR   PDB; 1P4V; X-ray; 1.90 A; A/C=46-340.
DR   PDB; 2GAC; X-ray; 2.10 A; A/C=46-196, B/D=198-340.
DR   PDB; 2GAW; X-ray; 2.20 A; A/C=46-196, B/D=197-340.
DR   PDB; 2GL9; X-ray; 2.00 A; A/C=46-196, B/D=198-340.
DR   PDB; 9GAA; X-ray; 2.10 A; A/C=46-340.
DR   PDB; 9GAC; X-ray; 1.90 A; A/C=46-340.
DR   PDB; 9GAF; X-ray; 1.90 A; A/C=47-340.
DR   PDBsum; 1AYY; -.
DR   PDBsum; 1P4K; -.
DR   PDBsum; 1P4V; -.
DR   PDBsum; 2GAC; -.
DR   PDBsum; 2GAW; -.
DR   PDBsum; 2GL9; -.
DR   PDBsum; 9GAA; -.
DR   PDBsum; 9GAC; -.
DR   PDBsum; 9GAF; -.
DR   MEROPS; T02.007; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0003948; F:N4-(beta-N-acetylglucosaminyl)-L-asparagina...; IEA:EC.
DR   InterPro; IPR000246; Peptidase_T2.
DR   InterPro; IPR006311; Tat.
DR   PANTHER; PTHR10188; Peptidase_T2; 1.
DR   Pfam; PF01112; Asparaginase_2; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Hydrolase; Periplasm; Signal.
FT   SIGNAL        1     45
FT   CHAIN        46    196       Glycosylasparaginase alpha chain.
FT                                /FTId=PRO_0000002347.
FT   CHAIN       197    340       Glycosylasparaginase beta chain.
FT                                /FTId=PRO_0000002348.
FT   ACT_SITE    197    197       Nucleophile.
FT   STRAND       50     56
FT   HELIX        59     70
FT   TURN         71     73
FT   HELIX        76     88
FT   STRAND      110    115
FT   STRAND      121    127
FT   HELIX       133    143
FT   STRAND      147    150
FT   HELIX       151    160
FT   HELIX       171    183
FT   STRAND      190    195
FT   STRAND      198    203
FT   STRAND      209    215
FT   TURN        232    234
FT   STRAND      235    239
FT   TURN        240    242
FT   STRAND      243    249
FT   HELIX       251    257
FT   HELIX       259    269
FT   HELIX       273    290
FT   HELIX       295    297
FT   STRAND      300    306
FT   STRAND      311    317
FT   STRAND      322    326
FT   STRAND      329    333
SQ   SEQUENCE   340 AA;  37263 MW;  4C56E5061B4E53D7 CRC64;
     MRIIYKQQTM NNNRRDFIKK LGIATAAIAI NPLEAKNLLD TSEPKTTNKP IVLSTWNFGL
     HANVEAWKVL SKGGKALDAV EKGVRLVEDD PTERSVGYGG RPDRDGRVTL DACIMDENYN
     IGSVACMEHI KNPISVARAV MEKTPHVMLV GDGALEFALS QGFKKENLLT AESEKEWKEW
     LKTSQYKPIV NIENHDTIGM IALDAQGNLS GACTTSGMAY KMHGRVGDSP IIGAGLFVDN
     EIGAATATGH GEEVIRTVGT HLVVELMNQG RTPQQACKEA VERIVKIVNR RGKNLKDIQV
     GFIALNKKGE YGAYCIQDGF NFAVHDQKGN RLETPGFALK
//