位置:首页 > 蛋白库 > XYNA_ALKHC
XYNA_ALKHC
ID   XYNA_ALKHC              Reviewed;         396 AA.
AC   P07528; Q9JPV5;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 149.
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=xynA; OrderedLocusNames=BH2120;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF N-TERMINUS.
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RA   Hamamoto T., Honda H., Kudo T., Horikoshi K.;
RT   "Nucleotide sequence of the xylanase A gene of alkalophilic Bacillus sp.
RT   strain C-125.";
RL   Agric. Biol. Chem. 51:953-955(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Active over a very broad pH range.;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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; D00087; BAA00055.1; -; Genomic_DNA.
DR   EMBL; BA000004; BAB05839.1; -; Genomic_DNA.
DR   PIR; H83914; H83914.
DR   PIR; JD0003; JD0003.
DR   RefSeq; WP_010898277.1; NC_002570.2.
DR   PDB; 2UWF; X-ray; 2.10 A; A=48-396.
DR   PDB; 7CPK; X-ray; 1.60 A; A=46-396.
DR   PDB; 7CPL; X-ray; 1.52 A; A=46-396.
DR   PDBsum; 2UWF; -.
DR   PDBsum; 7CPK; -.
DR   PDBsum; 7CPL; -.
DR   AlphaFoldDB; P07528; -.
DR   SMR; P07528; -.
DR   STRING; 272558.10174739; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   EnsemblBacteria; BAB05839; BAB05839; BAB05839.
DR   KEGG; bha:BH2120; -.
DR   eggNOG; COG3693; Bacteria.
DR   HOGENOM; CLU_020161_6_1_9; -.
DR   OMA; GIADNHT; -.
DR   OrthoDB; 654705at2; -.
DR   UniPathway; UPA00114; -.
DR   EvolutionaryTrace; P07528; -.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|Ref.1"
FT   CHAIN           29..396
FT                   /note="Endo-1,4-beta-xylanase A"
FT                   /id="PRO_0000007967"
FT   DOMAIN          51..396
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        195
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        301
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT   HELIX           51..53
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           57..60
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   TURN            61..64
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   STRAND          66..71
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           73..75
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           78..87
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   STRAND          89..95
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           99..102
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           112..123
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   STRAND          127..130
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   STRAND          133..138
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           141..144
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           152..154
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           158..183
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   TURN            184..186
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   STRAND          188..195
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   STRAND          201..203
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           207..212
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           215..228
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   STRAND          234..239
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           244..259
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   STRAND          266..269
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   STRAND          272..276
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           280..291
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   TURN            292..294
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   STRAND          296..307
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           318..320
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           323..342
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           344..346
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   STRAND          347..353
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           361..368
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   TURN            369..372
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   STRAND          379..381
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   STRAND          385..387
FT                   /evidence="ECO:0007829|PDB:7CPL"
FT   HELIX           389..395
FT                   /evidence="ECO:0007829|PDB:7CPL"
SQ   SEQUENCE   396 AA;  45294 MW;  29C1F46BE00E180C CRC64;
     MITLFRKPFV AGLAISLLVG GGIGNVAAAQ GGPPKSGVFG ENEKRNDQPF AWQVASLSER
     YQEQFDIGAA VEPYQLEGRQ AQILKHHYNS LVAENAMKPE SLQPREGEWN WEGADKIVEF
     ARKHNMELRF HTLVWHSQVP EWFFIDEDGN RMVDETDPDK REANKQLLLE RMENHIKTVV
     ERYKDDVTSW DVVNEVIDDG GGLRESEWYQ ITGTDYIKVA FETARKYGGE EAKLYINDYN
     TEVPSKRDDL YNLVKDLLEQ GVPIDGVGHQ SHIQIGWPSI EDTRASFEKF TSLGLDNQVT
     ELDMSLYGWP PTGAYTSYDD IPAELLQAQA DRYDQLFELY EELAADISSV TFWGIADNHT
     WLDGRAREYN NGVGIDAPFV FDHNYRVKPA YWRIID
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024