ID A0A1H5ISL2_9FLAO Unreviewed; 601 AA.
AC A0A1H5ISL2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=F5/8 type C domain-containing protein {ECO:0000313|EMBL:SEE43057.1};
GN ORFNames=SAMN04488034_101512 {ECO:0000313|EMBL:SEE43057.1};
OS Salinimicrobium catena.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Salinimicrobium.
OX NCBI_TaxID=390640 {ECO:0000313|EMBL:SEE43057.1, ECO:0000313|Proteomes:UP000199448};
RN [1] {ECO:0000313|EMBL:SEE43057.1, ECO:0000313|Proteomes:UP000199448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23553 {ECO:0000313|EMBL:SEE43057.1,
RC ECO:0000313|Proteomes:UP000199448};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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DR EMBL; FNUG01000001; SEE43057.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5ISL2; -.
DR STRING; 390640.SAMN04488034_101512; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000199448; 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:InterPro.
DR CDD; cd00063; FN3; 1.
DR CDD; cd08982; GH43-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000199448};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..601
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011541918"
FT DOMAIN 355..509
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 514..601
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT SITE 145
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 601 AA; 68827 MW; 7D65275473C03461 CRC64;
MKIFKNIIAT AAFLTAAMLH SQEVVPETYI NPLDIDYTYM VYNSANNISY RSGADPAVIE
YRGEYYMFVT RSFGYWHSKD LVNWEFIKPK QWFFEGSNAP TAFNYKDSLV YFAGDPAGYG
SILYTDDPKS GEWTPTASIS NNIQDSELFI DDDGKTYLYW GSSNLHPLRV KMLDKDDRFL
ETGVQKELIN LVEEEHGWER FGENNFHPTL KEGYMEGASM TKHDGKYYLQ YAAPGTQFNV
YADAAYIGET PLGPFKYMKN NPYSFKPGGF TNGAGHGITV KQTNGQYWHF ATMALASNSH
WERRLAMFPT YFDDEGLMYT NTSYGDYPLH SPAHPTKAGQ HTGWMLLSYK GRTTVSSSKM
QISKSTSTDG QFDITEMPLK KNSEGEIISE VLTDESPKSF WVAEANDDKQ WVEIEMLAPG
NIYALQINFH DEESGIYTRT EGLKHRFTIE VSENGKDWKT IVDRSNSFED SPNAYLTLNK
PVKAKYVRYN NVKVPGKNFA LSEIRVFGKG LGKKPAKVKG FKIERQDDRR DAAFKWEPVK
GAQGYNIRWG IAPDKLYQSW LIYDKNEHFM RNLDKGTTYY FSIEAFNENG ISERTEVQEV
K
//
