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XYNA_BACOV
ID   XYNA_BACOV              Reviewed;         376 AA.
AC   P49942;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Endo-1,4-beta-xylanase A;
DE            Short=Xylanase A;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase A;
DE   Flags: Precursor;
GN   Name=xylI;
OS   Bacteroides ovatus.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=28116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=V975;
RX   PubMed=7766665; DOI=10.1016/0304-4165(95)00051-c;
RA   Whitehead T.R.;
RT   "Nucleotide sequences of xylan-inducible xylanase and
RT   xylosidase/arabinosidase genes from Bacteroides ovatus V975.";
RL   Biochim. Biophys. Acta 1244:239-241(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- INDUCTION: By xylan.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; U04957; AAB08023.1; -; Genomic_DNA.
DR   PIR; S55892; S55892.
DR   RefSeq; WP_004300839.1; NZ_UAQF01000004.1.
DR   AlphaFoldDB; P49942; -.
DR   SMR; P49942; -.
DR   STRING; 28116.Bovatus_01725; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   GeneID; 29451514; -.
DR   OrthoDB; 654705at2; -.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Signal; Xylan degradation.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..376
FT                   /note="Endo-1,4-beta-xylanase A"
FT                   /id="PRO_0000007966"
FT   DOMAIN          25..371
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        160
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        265
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   376 AA;  42980 MW;  40C3B36E2DAA3499 CRC64;
     MKLKRIILLL LTVMFSFSYG EVFAKDGSSL KKALKNKFLI GVSVNTHQSS GKDVAAVEIV
     KKNFNSIVAE NCMKSSVIHP KENKYNFAQA DEFVSFGESN QMAIIGHCLI WHSQLAPWFC
     VDKDGNNVSP EVLKKRMKDH ITTIVKRYKG RIKGWDVVNE AIEDNGAYRK TKFYEILGEE
     YIPLAFQYAH EADPDAELYY NDYSMAQPGR REAVVKMVND LKKRGIRIDA IGMQGHIGMD
     YPKISEFEKS MLAFAGTGVK IMITELDLTV IPSPNPNVGA EVSASFEYKK EMNPYPDGLP
     EEVSKAWTER MNDFFRLFLK HHNLITRVTL WGVADQNSWR NDWPMRGRTD YPLLFDRNYQ
     PKPVVGLIIK EAEKTK
 
 
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