ID R9GV45_9SPHI Unreviewed; 361 AA.
AC R9GV45;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=ADIARSV_1197 {ECO:0000313|EMBL:EOR95591.1};
OS Arcticibacter svalbardensis MN12-7.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Arcticibacter.
OX NCBI_TaxID=1150600 {ECO:0000313|EMBL:EOR95591.1, ECO:0000313|Proteomes:UP000014174};
RN [1] {ECO:0000313|EMBL:EOR95591.1, ECO:0000313|Proteomes:UP000014174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MN12-7 {ECO:0000313|EMBL:EOR95591.1,
RC ECO:0000313|Proteomes:UP000014174};
RX PubMed=23846277;
RA Shivaji S., Ara S., Prasad S., Manasa B.P., Begum Z., Singh A.,
RA Kumar Pinnaka A.;
RT "Draft Genome Sequence of Arcticibacter svalbardensis Strain MN12-7T, a
RT Member of the Family Sphingobacteriaceae Isolated from an Arctic Soil
RT Sample.";
RL Genome Announc. 1:E00484-13(2013).
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}.
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:EOR95591.1}.
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DR EMBL; AQPN01000045; EOR95591.1; -; Genomic_DNA.
DR RefSeq; WP_016194438.1; NZ_AQPN01000045.1.
DR AlphaFoldDB; R9GV45; -.
DR STRING; 1150600.ADIARSV_1197; -.
DR eggNOG; COG3693; Bacteria.
DR OrthoDB; 1032269at2; -.
DR Proteomes; UP000014174; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000014174};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:EOR95591.1}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..361
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004481969"
FT DOMAIN 46..359
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 361 AA; 40463 MW; E44FD5AAE019FB59 CRC64;
MNKFKILIAC LVLGSFGCAK DDSENTTMTP ESVSATKSTT LALDEGVTLK DLPFKFGAAV
NVNHMKSRPE YKALIIKEYS SLTAENAMKI GALHPAKDTY NFTDADYLVD FAIANGKRVH
GHTLIWDSSL PAWIKNFQGD YPAWKKMFES HITTIVKHFK GRVASWDVIN EAFDDSGNLQ
NTIWRQHLGP NYIDMAFIFA HRADPAAKLF INDYGHENGN SRREGIIAYV KALRTKKVPI
HGIGMQFHTR YNRGTSSWTK AINETAATGL LVHISELDIS VNPDGVKGYV PTAERLAQQA
DAYKTIFKLY NAIPKAQQWG ITTWNLTDND SHLKSRPDYP LPFDTNYQKK PAYQGILDGV
K
//
