ID A0A494XZ12_9BACL Unreviewed; 2131 AA.
AC A0A494XZ12;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=D7Z26_07130 {ECO:0000313|EMBL:RKP54998.1};
OS Cohnella endophytica.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=2419778 {ECO:0000313|EMBL:RKP54998.1, ECO:0000313|Proteomes:UP000282076};
RN [1] {ECO:0000313|EMBL:RKP54998.1, ECO:0000313|Proteomes:UP000282076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M2MS4P-1 {ECO:0000313|EMBL:RKP54998.1,
RC ECO:0000313|Proteomes:UP000282076};
RA Tuo L.;
RT "Cohnella sp. M2MS4P-1, whole genome shotgun sequence.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000256|ARBA:ARBA00000681,
CC ECO:0000256|RuleBase:RU361174};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000256|ARBA:ARBA00004851}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
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:RKP54998.1}.
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DR EMBL; RBZM01000004; RKP54998.1; -; Genomic_DNA.
DR OrthoDB; 9809277at2; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000282076; Unassembled WGS sequence.
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:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00005; CBM9_like_1; 1.
DR CDD; cd10918; CE4_NodB_like_5s_6s; 1.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.1190; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 4.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR010502; Carb-bd_dom_fam9.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR001119; SLH_dom.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF06452; CBM9_1; 1.
DR Pfam; PF02018; CBM_4_9; 4.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR Pfam; PF00395; SLH; 3.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49344; CBD9-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 4.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS51677; NODB; 1.
DR PROSITE; PS51272; SLH; 3.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361174};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361174};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361174};
KW Reference proteome {ECO:0000313|Proteomes:UP000282076};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..2131
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019851281"
FT DOMAIN 91..312
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT DOMAIN 894..1228
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 1439..1528
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1539..1628
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1639..1728
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1950..2013
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 2015..2074
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 2077..2131
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT ACT_SITE 1152
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 2131 AA; 228504 MW; 2C15AEE566F175D5 CRC64;
MSRRFKRQLL SLLAAVLLVP QFWFAPKANA ASATIPVILY HVITDNPSGD YQYSTANFKK
QMKYLNDNGY TTVSAEQYVD IIVNGATAPS KPILLTFDDA TPDFITNALP VLTQYNMKAV
SFVIQDNIGS WGMTLSQLNT LKNNPNISLQ NHTKTHDQAV WTTSITKATA AAEIQSANTF
LKGITGKDPI LLAYPYGNYN ADVKAAATEN GIIVGFKAWS GDDDALAMGR ILIKKDDTLN
TFAAAIGGPT PPTPEAIGNV VVSNDFENGT QGWFKRGTET VTASTNAAHS GTRSLLVEGR
TDNWNGPGFN LAATGKLNKE SVYEFSAWVK LKEGTTGSET IQFGAQQTGA ANEYLNPGSA
ATVTADAWVQ VKGEYTYDMN ANSLQVYLQS NSSKTVSFYV DDFQVKVVKP AVLVEKFENG
KNGWTGNGAT ATVTNAVYHS GSNALLVTGR TQNYHGPSLV LTDTLEKGAE YEISAYAKLD
TGAASTQLKA SIEQSGLTGN DQFKQVIGLT TVTDGAWVKL SGTYTYNTAA TGIKLYFESE
DAGKNTSFAI DDVVIRQTSA APPPGFIVLS QSFEDGQLGG WTDLGWNGTG TAVVSSDYAS
EGTKSLLYKN RSDRKSAVSL NLTSKLVSGH KYDISYKLRS AQGTDNYHLG AKVKSGGTDS
YPWIIGNQAV TDSAWKTFEL KGYEVPASTT EFLVWIEANI YSPDETATAK ADYYMDEFVI
KDVTPGAEPP RTPAVPFNTI TFEDQSKGGF VGRAGTEMLT VTDEANHTDN GSYALKVEGR
TDSWHGPTIR VEQNVDKGSE YKVTAWVKLI SPTSSQLQLS TQVGNGSTAS YNTIQAKTVR
ATDGWVKLEG TYRYSSVGDE FLTIYVESSS NKTASFYIDD ISFVNTGSIP ISVQKDLTPI
KTQYQNDFLI GNAVSAADFD GTRLELLKLH HNVVTAENAM KPDATQAVKG TFTYADSLVD
KAIAAGMKVH GHVLVWHQQT PAWMTTSNGS PLSREEALAN MRTHIETVLT HYGDKYGNNF
VSWDVVNEAM NDNPSNPSDW SASLRTSPWK TAIGNDYVEQ AFLAAREVLD AHPSWNIKLY
YNDYNDDNQN KATAIYNMVK AINDKYALTH PGKKLIDGVG MQAHYNVNTK PDNVKASLER
FISLGVEVSI TELDITAGNG GTITEKEAIV QGYLYAQLFQ IYKEHASNIA RVTFWGLNDA
TSWRKEQPPL LFDNNLQAKQ AYYGVIDPSK FIAEHPPASA TASQTSAKYG TPVIDGTIDT
IWSDAPEVSI QKFQMAWQGA RGVGKALWDD HNLYVLIQVT DNAELDSTSP NAYEQDSVEV
FVDENNGKTA SYESDDGQYR VNYKNQATFN PSSKAAGFES ATSLSGTNYT VEMKIPLTSI
TPENNMKLGF DLQINDGKNG ARQSVAAWND LTGQGYQDTS VFGVLTLFGK SPPATPPEAP
ANVTASAVNA SSIKLNWDAA SDTNVTFSVY RGTSESGPFT EITSGKTGSE YTDTGLEAST
KYYYNVKAVK GELVSDASAV VNATTNPQVV TPPEEVLAVP TGLTAAAQSQ SSIKLNWDAA
SYTNVTFSVY RGESESGPFT VIASGESGTE YTDTGLEAST KYYYNVKAVK GELVSDASAV
VNATTNPQVV TPPEEVLAVP TGLTAAAQSQ SSIKLTWNTT SDTSVTFSVY RGTSESGPFT
EIASGKTGSE YTDMGLTAST KYYYYVKAVK GELVSDASTV VFATTSAAPP QTGTVTPPPV
TEQPAENGQI TPKVTVNNGK ASSNISAGNL QKAFDQVVTN AAGKKKVTID IPATAGANSY
EVQLPLQSLK DSGSTVLAIK TENGTVELPG NMLAGTNVGS SDSISVRLGK VSTEGLSNDV
RQQIGNHPVI SLEVLAGDSV VAWNNPNASV TVSVPYTPTA EELSNPDHII IWYIDGIGKA
TPVPNARYDA ASGTVKFSTT HFSNYAVAFV VKSFGDLQSV PWAKKAIEAM ASRGIINGTS
ENAYDPNAAI KRADFLSLLV RALELKGNNA SVTMFSDVDS SAYYYDAVKI AAQLGIIQGT
GSNLFDPNSK ISRQDMMVIA ARAAKAAGKA LPTGGTLDAF SDEASVASYA KDSVAALVNA
GIVQGSNGKL APNSSLTRAE AAVILQRIWS K
//
