ID D5BHG0_ZUNPS Unreviewed; 374 AA.
AC D5BHG0;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN OrderedLocusNames=ZPR_3039 {ECO:0000313|EMBL:ADF53358.1};
OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS profunda).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zunongwangia.
OX NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF53358.1, ECO:0000313|Proteomes:UP000001654};
RN [1] {ECO:0000313|EMBL:ADF53358.1, ECO:0000313|Proteomes:UP000001654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC {ECO:0000313|Proteomes:UP000001654};
RX PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA Zhou B.C., Yu J., Zhang Y.Z.;
RT "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT to the deep-sea environment and ecological role in sedimentary organic
RT nitrogen degradation.";
RL BMC Genomics 11:247-247(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000256|RuleBase:RU361174};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|RuleBase:RU361174}.
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DR EMBL; CP001650; ADF53358.1; -; Genomic_DNA.
DR RefSeq; WP_013072455.1; NC_014041.1.
DR AlphaFoldDB; D5BHG0; -.
DR SMR; D5BHG0; -.
DR STRING; 655815.ZPR_3039; -.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR KEGG; zpr:ZPR_3039; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_020161_6_1_10; -.
DR OrthoDB; 1032269at2; -.
DR Proteomes; UP000001654; Chromosome.
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 Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
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 Xylan degradation {ECO:0000313|EMBL:ADF53358.1}.
FT DOMAIN 36..371
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 276
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 374 AA; 43696 MW; 5AFF7135BCEAF4CC CRC64;
MKHKKQLHYL LILLLFGIIS CKDQQKTKDI TAKEDPKKEK GLKDYFAEDF PMGVAVSPAS
LEGKSKELIL AEYNSLTPEN VMKMGVIHPK KDEFNWAPAD KIVAFAQENG LKVRGHALVW
HQQTGDWIFK DDKGNDVSRE VLLDRMKAHI DSVVGRYKGK IYAWDVVNEA IDDNPQNFLR
NSKWLEIIGD DFLTKAFEFA HAADPNAKLF YNDYNIIIPE KRDRVLKLID KLKAEGAPIN
GIGIQGHWSV FNPSEEELQQ ALKMYTETGL DVQITELDVS LYKWEKEQRE RRPGDSDEFT
EERKLAQIEA YQKFFKVFRE YRDKLTGITF WNIADRYSWL DHYPVEGRKN YPLLFDENYQ
RKQVYDSVIK FSKK
//
