ID A0A150AH58_9BACT Unreviewed; 839 AA.
AC A0A150AH58;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glycosyl hydrolase family 2 {ECO:0000313|EMBL:KXX69254.1};
GN ORFNames=AVL50_16470 {ECO:0000313|EMBL:KXX69254.1};
OS Flammeovirga sp. SJP92.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC Flammeovirga.
OX NCBI_TaxID=1775430 {ECO:0000313|EMBL:KXX69254.1, ECO:0000313|Proteomes:UP000075267};
RN [1] {ECO:0000313|EMBL:KXX69254.1, ECO:0000313|Proteomes:UP000075267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJP92 {ECO:0000313|EMBL:KXX69254.1,
RC ECO:0000313|Proteomes:UP000075267};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:KXX69254.1}.
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DR EMBL; LQAQ01000082; KXX69254.1; -; Genomic_DNA.
DR RefSeq; WP_062617914.1; NZ_LQAQ01000082.1.
DR AlphaFoldDB; A0A150AH58; -.
DR STRING; 1775430.AVL50_16470; -.
DR OrthoDB; 811652at2; -.
DR Proteomes; UP000075267; 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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF18565; Glyco_hydro2_C5; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KXX69254.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075267}.
FT DOMAIN 28..176
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 186..283
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 290..451
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 659..719
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 733..834
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 839 AA; 95636 MW; DDBE08458AEFE3D2 CRC64;
MKPFIVLLIL FFTFSSCSQV RRRTVDDFNF GWKFSKNDIS NAQNITFDDT SWEDIRLPHD
WSILGGYQKD KGASSTGFTE GGIGWYRKTF TVPASDRDRE IWIEFDGVYC NSTVYINGEK
LGFRPSGYAS FSYTLSNHLK YGEENVIAVK VDHSNFVDSR WYTGSGIYRD VRLVKTAKTH
IPQWGVQITT PEVTVKQAFV RVKTTIKGKT DHTSVKITLM DEKNTVVAES EAKAITGDIV
DQKLQVLQPK RWGIETPHLY TAKIQVLNNG KMVDEIVEQF GIRAFNFDAK KGFFLNGRNV
KIKGVNLHHD VGAVGAAAVR DHWLFRLKKL KSVGVNAIRM AHNPHSPLLM DLCDEMGFLV
MNEAFDEWYV PKAKMMNCLG GKKASKDISE GYPEVFREWA ERDLKDLIRR DYNHPSVIMW
SIGNEIEWTF PAYSQTYAKL KKGIREYEDT PTFDTTVIKP VFEEVTGGVD SLSIIAHQLS
KWVKEEDTTR PTVCGSVRPS IAFASGYADA VDILGLNYRE IDYDAAHEAF PNKMMLGSEN
WVAYSEWKAV QERDFIPGIF VWTGFAYLGE AGLWPRKGLN ISLFDFAGFK NPRGHFFECL
WKEDPKVYMV TTPVDASEYS YTKKDGWKFD IQLRKPPVWA ELRLWEWYNV NEHWNYKTGE
DIVVQTYTNC EEAELFLNGK SLGKQSLADF SDSDNIIKWL VPYHKGELKV VGYNNGQKVE
EYVLNTVGEV AKIVLASDQT QMKANQYDVA HITVKMFDEE GYEIKNAEKE VTFHVSEELD
LLGVDNGSEM NVSPHNTNHV KSHKGRALAM VRSMDQKGDA TVYVSVGDVK SNEVVIELK
//
