ID A0A1A8TGM1_9GAMM Unreviewed; 494 AA.
AC A0A1A8TGM1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN Name=xynB {ECO:0000313|EMBL:SBS32625.1};
GN ORFNames=MSP8886_02497 {ECO:0000313|EMBL:SBS32625.1};
OS Marinomonas spartinae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=1792290 {ECO:0000313|EMBL:SBS32625.1, ECO:0000313|Proteomes:UP000092544};
RN [1] {ECO:0000313|EMBL:SBS32625.1, ECO:0000313|Proteomes:UP000092544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8886 {ECO:0000313|EMBL:SBS32625.1,
RC ECO:0000313|Proteomes:UP000092544};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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|RuleBase:RU361174};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
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DR EMBL; FLOB01000005; SBS32625.1; -; Genomic_DNA.
DR RefSeq; WP_067016856.1; NZ_FLOE01000002.1.
DR AlphaFoldDB; A0A1A8TGM1; -.
DR STRING; 1792290.MSP8886_02497; -.
DR OrthoDB; 4241492at2; -.
DR Proteomes; UP000092544; 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; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
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:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF02018; CBM_4_9; 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 SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 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:UP000092544};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:SBS32625.1}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..494
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008379023"
FT DOMAIN 220..491
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 426
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 494 AA; 54708 MW; 333A1DB3D5FE8D72 CRC64;
MKGIKQQKWL GFGKSHIYTV KALVAFTAMT MPVMSIAADS SAVVPSGFDA YYASASYTAI
ANNGDVENGL SGWSSIGGNI YRTTQDSYSG MASVHIYNRN ATWNGVTFKP APLVNGKQYN
VSVWVKLAPG VQSANIILTG KRTDDADTST NNEYVRIASA SANTYGWTEL KGSYTQSGTP
FQYFIIESDN SQVSYFVDAM KVEDIGGGSG DPGNNGKKFV GNITTSGQVR GDFSQYWDQI
TPENEGKWGS VERTRDVYNW SGIDAAYNYA KQHNMPFKQH TFVWGSQYPA WIDNLSPSEQ
AGEIEEWIRD FCNRYPDVAM IDVVNEATPG HAPAKYARSA FGNDWIIKSF QLAHKYCPNA
TLILNDYNVL SWNTDEFIRM ARPAVQAGVV DAIGLQSHGL EDFSVSQLQE KLNKIAALGL
PIYISEYDIA RSNDQEQLNI MKQQFPLFYN SDAVAGITLW GYVVGKTWVD GSGLIYENGA
QRPAMQWLMN YLGR
//
