XYNA_THEMA
ID XYNA_THEMA Reviewed; 1059 AA.
AC Q60037;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
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=TM_0061;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=7783614; DOI=10.1111/j.1365-2958.1995.tb02257.x;
RA Winterhalter C., Heinrich P., Candussio A., Wich G., Liebl W.;
RT "Identification of a novel cellulose-binding domain within the multidomain
RT 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga
RT maritima.";
RL Mol. Microbiol. 15:431-444(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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 Optimum pH is 6.2.;
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius. Thermostable.;
CC -!- DOMAIN: The C-terminal CBM-CenC domains mediate the binding of XynA to
CC microcrystalline cellulose. CBM-CenC 2 alone can also promote cellulose
CC binding.
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; Z46264; CAA86406.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35155.1; -; Genomic_DNA.
DR PIR; S61311; S61311.
DR RefSeq; NP_227877.1; NC_000853.1.
DR RefSeq; WP_004082550.1; NZ_CP011107.1.
DR PDB; 1I82; X-ray; 1.90 A; A=871-1059.
DR PDB; 1I8A; X-ray; 1.90 A; A=871-1059.
DR PDB; 1I8U; X-ray; 1.90 A; A=871-1059.
DR PDBsum; 1I82; -.
DR PDBsum; 1I8A; -.
DR PDBsum; 1I8U; -.
DR AlphaFoldDB; Q60037; -.
DR SMR; Q60037; -.
DR STRING; 243274.THEMA_04500; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR CAZy; CBM9; Carbohydrate-Binding Module Family 9.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR EnsemblBacteria; AAD35155; AAD35155; TM_0061.
DR KEGG; tma:TM0061; -.
DR eggNOG; COG3693; Bacteria.
DR InParanoid; Q60037; -.
DR OMA; TYAFEAW; -.
DR OrthoDB; 654705at2; -.
DR BioCyc; MetaCyc:MON-16897; -.
DR BRENDA; 3.2.1.8; 6331.
DR EvolutionaryTrace; Q60037; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR010502; Carb-bd_dom_fam9.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; PF06452; CBM9_1; 2.
DR Pfam; PF02018; CBM_4_9; 2.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF49785; SSF49785; 2.
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; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Repeat; Signal;
KW Xylan degradation.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1059
FT /note="Endo-1,4-beta-xylanase A"
FT /id="PRO_0000007986"
FT DOMAIN 364..692
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT DOMAIN 700..870
FT /note="CBM-cenC 1"
FT DOMAIN 871..1059
FT /note="CBM-cenC 2"
FT REGION 47..199
FT /note="A-1"
FT REGION 200..354
FT /note="A-2"
FT ACT_SITE 502
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 608
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT STRAND 872..877
FT /evidence="ECO:0007829|PDB:1I82"
FT STRAND 882..885
FT /evidence="ECO:0007829|PDB:1I82"
FT HELIX 888..892
FT /evidence="ECO:0007829|PDB:1I82"
FT STRAND 895..897
FT /evidence="ECO:0007829|PDB:1I82"
FT STRAND 900..904
FT /evidence="ECO:0007829|PDB:1I82"
FT TURN 906..908
FT /evidence="ECO:0007829|PDB:1I82"
FT STRAND 911..918
FT /evidence="ECO:0007829|PDB:1I82"
FT STRAND 920..930
FT /evidence="ECO:0007829|PDB:1I82"
FT STRAND 938..940
FT /evidence="ECO:0007829|PDB:1I82"
FT HELIX 941..943
FT /evidence="ECO:0007829|PDB:1I82"
FT STRAND 944..952
FT /evidence="ECO:0007829|PDB:1I82"
FT STRAND 965..971
FT /evidence="ECO:0007829|PDB:1I82"
FT STRAND 976..978
FT /evidence="ECO:0007829|PDB:1I82"
FT HELIX 984..986
FT /evidence="ECO:0007829|PDB:1I82"
FT STRAND 987..994
FT /evidence="ECO:0007829|PDB:1I82"
FT STRAND 997..1005
FT /evidence="ECO:0007829|PDB:1I82"
FT STRAND 1015..1026
FT /evidence="ECO:0007829|PDB:1I82"
FT STRAND 1032..1039
FT /evidence="ECO:0007829|PDB:1I82"
FT STRAND 1041..1043
FT /evidence="ECO:0007829|PDB:1I82"
FT TURN 1045..1047
FT /evidence="ECO:0007829|PDB:1I82"
FT HELIX 1049..1051
FT /evidence="ECO:0007829|PDB:1I82"
FT STRAND 1052..1058
FT /evidence="ECO:0007829|PDB:1I82"
SQ SEQUENCE 1059 AA; 119643 MW; 045936844A2D72E2 CRC64;
MQVRKRRGLL DVSTAVLVGI LAGFLGVVLA ASGVLSFGKE ASSKGDSSLE TVLALSFEGT
TEGVVPFGKD VVLTASQDVA ADGEYSLKVE NRTSPWDGVE IDLTGKVKSG ADYLLSFQVY
QSSDAPQLFN VVARTEDEKG ERYDVILDKV VVSDHWKEIL VPFSPTFEGT PAKYSLIIVA
SKNTNFNFYL DKVQVLAPKE SGPKVIYETS FENGVGDWQP RGDVNIEASS EVAHSGKSSL
FISNRQKGWQ GAQINLKGIL KTGKTYAFEA WVYQNSGQDQ TIIMTMQRKY SSDASTQYEW
IKSATVPSGQ WVQLSGTYTI PAGVTVEDLT LYFESQNPTL EFYVDDVKIV DTTSAEIKIE
MEPEKEIPAL KEVLKDYFKV GVALPSKVFL NPKDIELITK HFNSITAENE MKPESLLAGI
ENGKLKFRFE TADKYIQFVE ENGMVIRGHT LVWHNQTPDW FFKDENGNLL SKEAMTERLK
EYIHTVVGHF KGKVYAWDVV NEAVDPNQPD GLRRSTWYQI MGPDYIELAF KFAREADPDA
KLFYNDYNTF EPRKRDIIYN LVKDLKEKGL IDGIGMQCHI SLATDIKQIE EAIKKFSTIP
GIEIHITELD MSVYRDSSSN YPEAPRTALI EQAHKMMQLF EIFKKYSNVI TNVTFWGLKD
DYSWRATRRN DWPLIFDKDH QAKLAYWAIV APEVLPPLPK ESRISEGEAV VVGMMDDSYL
MSKPIEILDE EGNVKATIRA VWKDSTIYIY GEVQDKTKKP AEDGVAIFIN PNNERTPYLQ
PDDTYAVLWT NWKTEVNRED VQVKKFVGPG FRRYSFEMSI TIPGVEFKKD SYIGFDAAVI
DDGKWYSWSD TTNSQKTNTM NYGTLKLEGI MVATAKYGTP VIDGEIDEIW NTTEEIETKA
VAMGSLDKNA TAKVRVLWDE NYLYVLAIVK DPVLNKDNSN PWEQDSVEIF IDENNHKTGY
YEDDDAQFRV NYMNEQTFGT GGSPARFKTA VKLIEGGYIV EAAIKWKTIK PTPNTVIGFN
IQVNDANEKG QRVGIISWSD PTNNSWRDPS KFGNLRLIK
