GenomeNet

Database: UniProt
Entry: C5BMS9_TERTT
LinkDB: C5BMS9_TERTT
Original site: C5BMS9_TERTT 
ID   C5BMS9_TERTT            Unreviewed;       726 AA.
AC   C5BMS9;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE            EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN   OrderedLocusNames=TERTU_2843 {ECO:0000313|EMBL:ACR12624.1};
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR12624.1, ECO:0000313|Proteomes:UP000009080};
RN   [1] {ECO:0000313|EMBL:ACR12624.1, ECO:0000313|Proteomes:UP000009080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA   Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA   Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA   Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA   Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT   endosymbiont of marine wood-boring bivalves (shipworms).";
RL   PLoS ONE 4:E6085-E6085(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->2)-alpha-D-(4-O-methyl)glucuronosyl links in
CC         the main chain of hardwood xylans.; EC=3.2.1.131;
CC         Evidence={ECO:0000256|RuleBase:RU361198};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU361198}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family.
CC       {ECO:0000256|ARBA:ARBA00008833, ECO:0000256|PIRNR:PIRNR029900,
CC       ECO:0000256|RuleBase:RU361198}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001614; ACR12624.1; -; Genomic_DNA.
DR   RefSeq; WP_015818736.1; NC_012997.1.
DR   AlphaFoldDB; C5BMS9; -.
DR   STRING; 377629.TERTU_2843; -.
DR   CAZy; GH67; Glycoside Hydrolase Family 67.
DR   KEGG; ttu:TERTU_2843; -.
DR   eggNOG; COG3661; Bacteria.
DR   HOGENOM; CLU_007125_1_0_6; -.
DR   OMA; IWRAFVY; -.
DR   OrthoDB; 339499at2; -.
DR   Proteomes; UP000009080; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0046559; F:alpha-glucuronidase activity; IEA:InterPro.
DR   GO; GO:0033939; F:xylan alpha-1,2-glucuronosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
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; IPR011395; Glyco_hydro_67_aGlcAse.
DR   InterPro; IPR005154; Glyco_hydro_67_aGlcAse_N.
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   Pfam; PF03648; Glyco_hydro_67N; 1.
DR   PIRSF; PIRSF029900; Alpha-glucuronds; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361198};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR029900};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR029900};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361198};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009080};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW   ECO:0000256|PIRNR:PIRNR029900}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..726
FT                   /note="Xylan alpha-1,2-glucuronidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002948987"
FT   DOMAIN          35..154
FT                   /note="Alpha glucuronidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03648"
FT   DOMAIN          158..477
FT                   /note="Glycosyl hydrolase family 67 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF07488"
FT   DOMAIN          478..704
FT                   /note="Glycosyl hydrolase family 67 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07477"
FT   ACT_SITE        315
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT   ACT_SITE        389
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT   ACT_SITE        417
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ   SEQUENCE   726 AA;  82206 MW;  D343C90A42BB5795 CRC64;
     MHKILRTFAF LLLSVLACSP AFGQKIFDGE DGYRLWLKYD LLSDQQSIKT YRKQISSIYV
     AGDSATTTVI RDELSHALSG LLGKQPKFVE AVGKHALVVG TPSSSADIRN ADLSELKGLG
     KEGFVIKSLE LSGKPVTLIA ANTDVGALYG TFHLLRLIQT EQPLRELEIV EKPKIDVRVL
     NHWDDMDRHV ERGFAGESIW DWHKLPDYTY PRYYDYARAN ASIGINGTVL NNVNANAITL
     TPHYLDKVEA LADLFRPYGI KVYLSIKFSS PQLIGGLKTS DPLDPTVKQW WKDKVEEIYA
     RIPDFGGFLV KANSEGQPGP GDFGRTHAEG ANLLADALAP HGGVVMWRAF VYANEKNEER
     SKQAYSEFKP LDGKFHDNVL IQVKNGPIDF QPREPFSPLF GATPKTPMMM EFQITMEYLG
     FSTHLVYLGT MYEEALQSDT YAKGKGSTVA KVVDGSLFNN HISGIAGVSN IGTDRNWTGH
     IILQSNWYVF GRLAWDHELT TADIADEWVR MTLSNDEKVV STVTDMMMRS REITVNYMTP
     LGLHHIMGVG HHYGPGPWVK DLGREDWTSV YYHKAGKDGI GFDRSPTGVN SVEQYFSPLK
     EEYAKAETTP EELLLWFHHL PWDYTVKSTG RDLWDELVHR YYQGAADVTA MHNQWQSLQD
     ELDPLQYHQV DMALTIQEKE ARWWRDACVT YFQTFSQRPL PKGFEKPEKT LKEYMDMRFP
     YAPGQG
//
DBGET integrated database retrieval system