ID A0A1V3N2K1_9SPHI Unreviewed; 633 AA.
AC A0A1V3N2K1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:OOG19265.1};
GN ORFNames=BWD42_04805 {ECO:0000313|EMBL:OOG19265.1};
OS Sphingobacterium sp. CZ-UAM.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1933868 {ECO:0000313|EMBL:OOG19265.1, ECO:0000313|Proteomes:UP000188865};
RN [1] {ECO:0000313|EMBL:OOG19265.1, ECO:0000313|Proteomes:UP000188865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CZ-UAM {ECO:0000313|EMBL:OOG19265.1,
RC ECO:0000313|Proteomes:UP000188865};
RA Steffani-Vallejo J.L., Licona-Cassani C., Cruz-Morales P., Lozano L.,
RA Zuniga C., Morales M., Revah S., Utrilla J.;
RT "Genome sequence of Sphingobacterium sp. CZ-UAM, isolated from a
RT methanotrophic consortium.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:OOG19265.1}.
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DR EMBL; MTCM01000001; OOG19265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3N2K1; -.
DR STRING; 1933868.BWD42_04805; -.
DR OrthoDB; 9803461at2; -.
DR Proteomes; UP000188865; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd08983; GH43_Bt3655-like; 1.
DR CDD; cd18828; GH43_BT3675-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 2.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 2.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OOG19265.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..633
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012573069"
FT SITE 466
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 633 AA; 72123 MW; 252C5F3E3084B59C CRC64;
MRFTVIAFLL MNFAASAYAQ GYRQGPSEKD FAGYLFAYFK GNAVADEAVC FAISTDGYTY
RALNGNRPVL DSKSISKTGG VRDPHILRAE DGKTFYMVLT DMTSSKGWDS NRGMVLLKSQ
DLLHWSHQAI DFQQRFTGQE DLKRVWAPQT IFDAAAGKYM IYWSMQHGNG PDIIYYAYAN
KDFTDFETDP KVLFMPKNGK SCIDGDIIEK NGIFYLFYKT EGHGNGIKLA MTDSLTSGKW
IEQPGYKQQT RDAVEGSSVF RRNQSDQYIL MYDVYGRGKY QFCTSDDLDR FKVIDQEIDM
DFHPRHGTII PLSRAELIRL TAKWGKPKDI PFAFKKNPIL DGYYADPDIL YANKTKRYYI
YPTSDGFDGW GGFYFKTFSS ADLIHWKDEG VILDLKKEVP WGPRHAWAPT ITEKKVKGDY
TYYYYFTAAQ KIGVAVADQP TGPFKDSGRP LIDFKPPGVS GGQEIDPAVF NDPRSGKSYL
YWGNGYLAVA ELNTDMVSIK KNTIKVLTPD KTFREGVYVI FRNGIYYFLW SEDDTRSENY
RVRYGTSTSP DGPIQIPENN LILQKDPAKG IYGTGHNSVL QVPGTDEWYI VYHRFSYPNG
IRMGDAAGFH REVCMDRLYF DANGRILPVI PTH
//
