ID A0A090W1E1_9FLAO Unreviewed; 1176 AA.
AC A0A090W1E1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN ORFNames=JCM19302_2003 {ECO:0000313|EMBL:GAL70840.1}, JCM19538_3273
GN {ECO:0000313|EMBL:GAL89796.1};
OS Jejuia pallidilutea.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Jejuia.
OX NCBI_TaxID=504487 {ECO:0000313|EMBL:GAL70840.1, ECO:0000313|Proteomes:UP000029646};
RN [1] {ECO:0000313|Proteomes:UP000029646, ECO:0000313|Proteomes:UP000030184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19302 {ECO:0000313|EMBL:GAL70840.1}, JCM 19538
RC {ECO:0000313|EMBL:GAL89796.1, ECO:0000313|Proteomes:UP000030184}, and
RC JCM19302 {ECO:0000313|Proteomes:UP000029646};
RA Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K.,
RA Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., Niwa A.,
RA Sawabe T., Sawabe T.;
RT "Draft Genome Sequence of Marine Flavobacterium Jejuia pallidilutea Strain
RT 11shimoA1 and Pigmentation Mutants.";
RL Genome Announc. 2:e01236-14(2014).
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 -!- 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:GAL70840.1}.
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DR EMBL; BBNS01000008; GAL70840.1; -; Genomic_DNA.
DR EMBL; BBNY01000053; GAL89796.1; -; Genomic_DNA.
DR RefSeq; WP_042248302.1; NZ_BBNY01000053.1.
DR AlphaFoldDB; A0A090W1E1; -.
DR OrthoDB; 9815108at2; -.
DR Proteomes; UP000029646; Unassembled WGS sequence.
DR Proteomes; UP000030184; Unassembled WGS sequence.
DR GO; GO:0047753; F:choline-sulfatase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd16031; G6S_like; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
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; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR035396; Bac_rhamnosid6H.
DR InterPro; IPR035398; Bac_rhamnosid_C.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR43108; N-ACETYLGLUCOSAMINE-6-SULFATASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43108:SF8; SD21168P; 1.
DR Pfam; PF17389; Bac_rhamnosid6H; 1.
DR Pfam; PF17390; Bac_rhamnosid_C; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:GAL70840.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1176
FT /note="alpha-L-rhamnosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010408404"
FT DOMAIN 31..362
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT DOMAIN 731..1069
FT /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT /evidence="ECO:0000259|Pfam:PF17389"
FT DOMAIN 1076..1144
FT /note="Alpha-L-rhamnosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17390"
FT COILED 441..468
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1176 AA; 135188 MW; 26AC15D9A6A7BDF4 CRC64;
MFKNSYLLVL LSVLCSFNIT SAQQKNKLEK PNIIFILTDD QRFDAIGYAG NKFVETPQMD
DLAKTGTYFN TAIVTTPICA ASRASIFTGL HERAHNYNFQ TGNIRSEYMA NSYPTLLKNN
GYYTGFFGKY GVRYNGLDKQ FDEYEDYDRN NRYKDRRGYY YKTIDNDTVH LTRYTGQQAL
NFIDKNASNN KPFCLSLSFS APHAHDGAPE QYFWQNTTDN LLSDTTIPGP ELGDDKYFEA
QPKIVKDGFN RLRWTWRYDT PEKYQHSLKG YYRMIAGIDL EIAKIRKKLE DKGIADNTVI
IVMGDNGYFL GERQFAGKWL MYDNSVRVPL IVFDPRINQH QDIDDMVLNI DVPSTIADLA
GVKAPDTWQG KSLMPIVKKE TKSIDRDTIL IEHLWDFKNI PPSEGVRTKK WKYFRYVNDK
TIEELYDLEK DPKEVKNLIG KKKYKEVADK LRAKLEELIK NNSDAYRAAP TELTVELIRE
PGTEVEIYDL KPEFGWTVPL GSKFQGAYQI LVASSKSNID ANNGDVWDSG RVASAQSTDV
EYAGKNKLEI GKTYYWKVRI WEQENRLVDY SEPQKFTTGK SDSYIISTEN KFVTTRVKPV
KFEKTEDFYF IDFGKAAFAT MEFTYNAKTP HTLTVHVGEM ANDKGYLNRT PPEKSNIRYQ
EIKVDVKPGQ TKYQIKVHED ERNTRANKAV PLPDGFPPLV PFRYAEIEGA QSDLKAENFT
QLAFHTYWDE TASGFESNDN ILNQVWDLCK YSIKATTFNG LYVDGDRERI PYEADAYLNQ
LSHYTTDREF AIARRTIEYF MKNPTWPTEW QQHVPLLIYA DYMYTGNTEL IERYYEPLKY
KSLYELSNED GLITSTKVDA EFMSKLGFPE GYKKPLTDIV DWPGANFNRS KTKGERDGFV
FKDYNTVINS FFYENMKIMA EFAKILGKTQ EALDFEYRAA KAKKAVNEQM FDKERGIYVD
GIGTDHASLH ANMMPLAFGL VPEEHFDSVV NYVKSRGMAC SVYGAQFLMD GLYNAGESDY
ALDLLTDTSD RSWYNMIKIG STITLEAWDN KYKNNLDWNH AWGAVPANII PRGLWGIKPK
TPGFEVATIK PQMSRLKSSE ITVPTVRGQI KAKYTHKGAR LQIYEIEIPG NMVAEFSLND
LDGKDLIHNG EKVPSAFHSI RLSPGKHTIQ LKINSF
//
