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Database: UniProt
Entry: W7QRH9_9ALTE
LinkDB: W7QRH9_9ALTE
Original site: W7QRH9_9ALTE 
ID   W7QRH9_9ALTE            Unreviewed;       926 AA.
AC   W7QRH9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=DS2_07638 {ECO:0000313|EMBL:EWH10488.1};
OS   Catenovulum agarivorans DS-2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Catenovulum.
OX   NCBI_TaxID=1328313 {ECO:0000313|EMBL:EWH10488.1, ECO:0000313|Proteomes:UP000019276};
RN   [1] {ECO:0000313|EMBL:EWH10488.1, ECO:0000313|Proteomes:UP000019276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-2 {ECO:0000313|EMBL:EWH10488.1,
RC   ECO:0000313|Proteomes:UP000019276};
RX   PubMed=24604650;
RA   Shan D., Li X., Gu Z., Wei G., Gao Z., Shao Z.;
RT   "Draft Genome Sequence of the Agar-Degrading Bacterium Catenovulum sp.
RT   Strain DS-2, Isolated from Intestines of Haliotis diversicolor.";
RL   Genome Announc. 2:e00144-14(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:EWH10488.1}.
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DR   EMBL; ARZY01000011; EWH10488.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7QRH9; -.
DR   STRING; 1328313.DS2_07638; -.
DR   PATRIC; fig|1328313.3.peg.1559; -.
DR   eggNOG; COG3408; Bacteria.
DR   OrthoDB; 9761045at2; -.
DR   Proteomes; UP000019276; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030596; F:alpha-L-rhamnosidase activity; IEA:UniProtKB-EC.
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; 2.
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; IPR016007; Alpha_rhamnosid.
DR   InterPro; IPR035396; Bac_rhamnosid6H.
DR   InterPro; IPR035398; Bac_rhamnosid_C.
DR   InterPro; IPR013737; Bac_rhamnosid_N.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008902; Rhamnosid_concanavalin.
DR   PANTHER; PTHR33307; ALPHA-RHAMNOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR33307:SF6; ALPHA-RHAMNOSIDASE (EUROFUNG)-RELATED; 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   PIRSF; PIRSF010631; A-rhamnsds; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019276};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          191..360
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          373..470
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          480..822
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          825..893
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
SQ   SEQUENCE   926 AA;  104819 MW;  AEEAE7C86C218D88 CRC64;
     MDRLRVLSRT YKLYVMLVGF CWLLASCSFS FEQFSNNDAP VELKVGEGFV NPIGYYEAKP
     RFSWKIASSS VQNTQSAYQI QVGSAVEQGE SFKANLWDSG KVASADNAWI RYAGQPLVSR
     QQLLWRVRIW DENKQASNWS ELNRVELGLL SNQDWQAEWI AHPDTLQVNK PSQKTIATAQ
     YFRKRFSAEN SIQQARLYVT AKGLFKAFIN GQMVAPDDAM TPGWTPYAKR IETLTYDVTD
     LLSQGENVLA ANLAGGWYAG RVFKFTDKEH KVTPEFLAQL EIIDENGLRQ VITTDNSWRV
     TQQGPIRFSS IYDGELYDQN KQMSSWAQVQ FDDSAWQTAA ANQLDFKVQL APKRHAPIRN
     VASLEPVSII TNNNKAVIFD FGQNMVGVPK INVPALANQA ITIRFAEALH KGEFYTENYR
     SAKSTDIFIP AADGIAEYQP RFTYHGYRYV EISGFDPNAA PSKSWVTAVV QHSDVEVEQN
     FVTSHAKLNK LAQNIRWGLK SNFYDIPLDC PQRDERLGWT GDAQVFTTPS MYMADVYAFW
     AAWLQSVREE QFEDGGVPLY IPFVEWINWP SSGWGDAATI IPWELYQMTG DTSILADNYT
     MMTRWLDYHK SQSDELISSM KTFGDWLQPY PDPAAKNPNR GDTRFDLIST AYFARSVYLT
     AQTASVLDKS ADATRYLALF ERIKHAFVHH FFDEKLNVKQ GQSTQTTYLL GLAFDLFTGE
     QVAIAQHKLI ELIEQADGHL RTGFLGTPLL AQVLQEAGRS DIVYDLIFKE TYPSWFYSIN
     NGATTTWERW NSYSIKDGFN PEGMNSLNHY AYGSIAQWFY QGILGIRAKV AGFKQVEIKP
     QVLGQLDSAE GFYDTPAGRI KVSWQLNLQQ FTMNVSIPKN TSADVVIPAF RANTLMINQQ
     SGKSADLSNL QPGEYQISAA LTRQAP
//
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