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Database: UniProt
Entry: R5KJS6_9BACT
LinkDB: R5KJS6_9BACT
Original site: R5KJS6_9BACT 
ID   R5KJS6_9BACT            Unreviewed;       693 AA.
AC   R5KJS6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Alpha-glucuronidase {ECO:0000313|EMBL:CCY65324.1};
GN   ORFNames=BN467_02033 {ECO:0000313|EMBL:CCY65324.1};
OS   Prevotella sp. CAG:1124.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262920 {ECO:0000313|EMBL:CCY65324.1, ECO:0000313|Proteomes:UP000017956};
RN   [1] {ECO:0000313|EMBL:CCY65324.1, ECO:0000313|Proteomes:UP000017956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:1124 {ECO:0000313|Proteomes:UP000017956};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCY65324.1}.
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DR   EMBL; CAYO010000197; CCY65324.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5KJS6; -.
DR   Proteomes; UP000017956; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0046559; F:alpha-glucuronidase activity; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1330.10; Alpha-glucuronidase, C-terminal domain; 1.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR037054; A-glucoronidase_C_sf.
DR   InterPro; IPR011099; Glyco_hydro_67_C.
DR   InterPro; IPR011100; Glyco_hydro_67_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   PANTHER; PTHR39207; ALPHA-GLUCURONIDASE A; 1.
DR   PANTHER; PTHR39207:SF1; ALPHA-GLUCURONIDASE A; 1.
DR   Pfam; PF07477; Glyco_hydro_67C; 1.
DR   Pfam; PF07488; Glyco_hydro_67M; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017956};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..693
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004395951"
FT   DOMAIN          145..440
FT                   /note="Glycosyl hydrolase family 67 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF07488"
FT   DOMAIN          442..666
FT                   /note="Glycosyl hydrolase family 67 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07477"
FT   REGION          668..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..687
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   693 AA;  78444 MW;  6528775BEE9BF567 CRC64;
     MNMKRITIAA MTALIFITAK ADDGSRLWLN KQRGACTAKI ETSDKSDIAQ TAVSELAAFW
     NGCDIILSRD KSLPDNDGFK IERSGKNGSL IVKARRSAGL LYGAYELLRM QQTKGEIYSG
     KTGQDTNLSA ADNKFRISPS VCVSSSSPAF PYRILNHWDN PDGSVERGYA DKSIWKWDEI
     NGEKGTMSMD QKERLTIYCR ANASIGINGS VLNNVNASPY ILTTEYLDKI KVIADMMRPY
     GIKTYLAVNF ASPMAAGGLE TADPADAKVK EWWEKKVKEI YKKIPDFGGF LVKANSEGQP
     GPGDYHRTHA EGANMLAKAL APYNGIVMWR SFVYGNHEGE DRVKQAVTEF EELDGKFADN
     VILQSKNGPL DFQPREPYAP IFDRMKHTPM WVELQITQEY LGQSRHLVYL APMWKEFFTF
     VSPQQLQGIA GVANTGDNTN WCGHPFSQSN WYAFGRLAWN PELASDSIAR EWLAQTFTRD
     TAFINPMTAV MEASREACVD YMMPLGLHHI FKADHHYGPE PDGLYPNYPI EWCPVYYHKA
     DSLGIGFDRT RTGTDAVGQY RHPYDSIYND INTCPEEYLL WFHHVSWDYK MKNGKTLWEN
     LSAHYNRGVD EVRRFIGTWQ RMRPYVDTER FMIVSALLDH QLENAEEWRD TCLGYFGKIS
     GKIQETATET SANLPQDDGT QPAILQGQET DRP
//
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