ID A0A1V2BAS4_9BACT Unreviewed; 1635 AA.
AC A0A1V2BAS4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN ORFNames=BW716_04395 {ECO:0000313|EMBL:OMP80368.1};
OS [Flexibacter] sp. ATCC 35208.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1936242 {ECO:0000313|EMBL:OMP80368.1, ECO:0000313|Proteomes:UP000188534};
RN [1] {ECO:0000313|EMBL:OMP80368.1, ECO:0000313|Proteomes:UP000188534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35208 {ECO:0000313|EMBL:OMP80368.1,
RC ECO:0000313|Proteomes:UP000188534};
RA Webster A.L., Walker C., Li H., Skinnider M., Magarvey N.A.;
RT "Elucidation and Expansion of Monobactam Biosynthesis.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-rhamnose residues
CC in alpha-L-rhamnosides.; EC=3.2.1.40;
CC Evidence={ECO:0000256|ARBA:ARBA00001445};
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:OMP80368.1}.
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DR EMBL; MTKN01000004; OMP80368.1; -; Genomic_DNA.
DR OrthoDB; 9766741at2; -.
DR Proteomes; UP000188534; 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; 1.50.10.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR035396; Bac_rhamnosid6H.
DR InterPro; IPR035398; Bac_rhamnosid_C.
DR InterPro; IPR013737; Bac_rhamnosid_N.
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; IPR023232; Glyco_hydro_2_AS.
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 InterPro; IPR008902; Rhamnosid_concanavalin.
DR PANTHER; PTHR33307:SF11; ALPHA-L-RHAMNOSIDASE; 1.
DR PANTHER; PTHR33307; ALPHA-RHAMNOSIDASE (EUROFUNG); 1.
DR Pfam; PF05592; Bac_rhamnosid; 1.
DR Pfam; PF17389; Bac_rhamnosid6H; 1.
DR Pfam; PF17390; Bac_rhamnosid_C; 1.
DR Pfam; PF08531; Bac_rhamnosid_N; 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 SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000188534};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1635
FT /note="alpha-L-rhamnosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012324234"
FT DOMAIN 23..174
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 244..303
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 315..472
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 624..674
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 688..802
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
FT DOMAIN 872..1040
FT /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08531"
FT DOMAIN 1097..1180
FT /note="Alpha-L-rhamnosidase concanavalin-like"
FT /evidence="ECO:0000259|Pfam:PF05592"
FT DOMAIN 1195..1529
FT /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT /evidence="ECO:0000259|Pfam:PF17389"
FT DOMAIN 1533..1606
FT /note="Alpha-L-rhamnosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17390"
FT REGION 216..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1635 AA; 183067 MW; 081011D1D9D0E576 CRC64;
MIRIILISIC LGFLFPASAQ QLFDDDWLFY RGNAQGAENP SFNDQEWRKI DLPHDWSIED
LPGTNSPFSQ GAISQVSGGF TTGGTGWYRK HFTLQADKKP VILQFDGVYM NATVWLNGKK
LGKHPYGYTT FSFDITDKII PGKENVLAVL VRNEGENSRW YAGSGIYRHV WLKSNQYKIA
ITTSVVNRSL ATVAIHTEKP CTTRIYNQKG TLITTTSPSI MSSSSNPSKS SNPSKSSNPH
NPSNPSSSSN SSSSFNPSNS SSLSTDQQFQ ISKPSLWSVD TPNLYTAITI IDGDTIRTTF
GIRTFTADAV NGARLNGLPI KLKGGCVHHD NGPLGAKAYD RAEERKVALL KASGYNAIRC
AHNPPSPAFL DACDRFGVLV IDEAFDTWED PKNPEDYHVF FNDWWQRDIE SMVNRDRNHP
SVIMWSIGNE IPHREKPAVA VVAHTLRQYL LQLDSTRLIT CGVNGIAPDK DTFLSALDVA
GYNYALDKYE PDHARVPNRV IMATESFPLD AGAYWEGVIK HPWVIGDFVW TAFDYIGEAS
IGWLGYMQHQ GFYPWNLAYC GDIDICGWKR PQSYYRDALW MPDQLSLFVH PPQPTYPTNP
DKVDWSRWEW QDVTDSWNWP GNEGKPFEVV AYSSYDQVEL FLNGKSLGKK AVKDHTASWQ
VPYTAGILTA TAGKKKVSLS TTGKSVRLQL QADTLQLAPN NQDLAYITVN LLDSAGHLNP
DDTVLINFKL EGPATIVGVG NADPRSLESN QSLQSSQALQ NNQIAQRKAF HGRALVIIKA
GKTPGAIRLI ASTPNLQPAE ITFNNQENPL VTSPISQPAN TIVKNKQSSP QWIGYEEMPD
SLRLVPGLPN DKTKAQQRAI TPLFRKSFTT NKPIATAKLT ITGLGHYEFT INGRKPVNSF
LAPGWTNYDK RVFYNTYDIA NYLQKGENVL GVIVGNGFYY INKERYHKLL TAFGYPKMYC
QLHITYTDGT TTTIVSDQSW KTSPSPITFT SIYGGEDYDA RLEQDGWDRP GFDDSNWKNV
LLVKAPTGKL QEEKDYPVTL ADTISVKSIN SIPNLTQDSS NTSVKSINNS QDSPDTSIKS
PTNNFLRTPS NPSLQSPTIY DFGQNASGII ALKIKGHKGQ TIKLTPSELL TPTGLANQRA
TGKPYYYSYT LKSDEVEEWQ PRFTYYGFRY VQIEGATPNQ ILDLKLLHNR NSSPENGTFE
CSNPLFNQIY TLIKWAIKSN LQSVVTDCPH REKLGWLEQD YLMGNSIQYN YDIRLLYQKL
VNDMIDAQTP EGLVPDIAPE YVFFDDKGFG FRDSPEWGSA CVILPWLLYK WYGDSTTMQN
AYPMMQRYIA YLESKANNHI LSYGLGDWFD YGPARPGVAQ LTPKELTATA IYYYDCKLLA
DIATILKKKE AKTYQKQAIN IKQSFNNTFF NKQTNMYATG SQTAMAMPLC VGLVDEVNKT
KVFKNLIDSI TTNNNKLTAG DIGFHFLIQA FHQGNASRII YDMNCRNDVP GYGYQIAKGA
TALTESWPAL AEVSNNHLML GHIMEWFFSG LAGIQQSENS IAYRDIIICP EIVGDVTYAK
GTYNTHNGTI VSQWEKGQLF KLYVNIPPNT NATIKIPATP TQHITQMSEP VKPTHYENGR
AIIRITSGQY LFTVI
//
