ID   G7MDD5_9CLOT            Unreviewed;       884 AA.
AC   G7MDD5;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=CDLVIII_2628 {ECO:0000313|EMBL:EHI99233.1};
OS   Clostridium sp. DL-VIII.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=641107 {ECO:0000313|EMBL:EHI99233.1, ECO:0000313|Proteomes:UP000005106};
RN   [1] {ECO:0000313|EMBL:EHI99233.1, ECO:0000313|Proteomes:UP000005106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DL-VIII {ECO:0000313|EMBL:EHI99233.1,
RC   ECO:0000313|Proteomes:UP000005106};
RX   PubMed=23929491;
RA   Taghavi S., Izquierdo J.A., van der Lelie D.;
RT   "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT   Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL   Genome Announc. 1:e00605-e00613(2013).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM001240; EHI99233.1; -; Genomic_DNA.
DR   RefSeq; WP_009169905.1; NZ_CM001240.1.
DR   AlphaFoldDB; G7MDD5; -.
DR   STRING; 641107.CDLVIII_2628; -.
DR   eggNOG; COG3408; Bacteria.
DR   HOGENOM; CLU_002926_1_2_9; -.
DR   Proteomes; UP000005106; Chromosome.
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; 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:SF5; CELLULOSE-BINDING SDE182 NUCLEOSIDE HYDROLASE-LIKE DOMAIN-CONTAINING PROTEIN-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   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005106}.
FT   DOMAIN          134..304
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          319..435
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          441..778
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          790..851
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
SQ   SEQUENCE   884 AA;  101857 MW;  E013F64F6A537F23 CRC64;
     MNMNNIKINY QDSCINIDSN SLIISWIVDS KQTNYEITIE NKNIIIYESK KINSSENIVY
     IKDLDLKPET EYIVTIKLWN EFDSCIKSEQ FRTSIFGDFI GKWISNGERL GNEIDYYKDN
     RNCLIRKNFN ITDEIHEAFL YIVGLGYYNV YINGRKVGKA VLNTDWTKYS KEIYYDVYEV
     SQFLNKGDNI ISVELGNGWY NPAPLKLFGK YNLRSVLDIG EPKLIADLKI NINSNKRMII
     STDESWEVSK GSYLFNNIYL GERFDSRLFN ETWNSPNSKN MNWEKAILAT SPGGKLSASF
     IEKIEEIKIV PAKSIIVKEK KKVLIDFGET IEGFIDISLI GECGQEVKLI YAENLNKNGT
     VNVVSTLAGS VGNAPNGNRI DGGPGAPEIA KQMDICILSD AETRYVNKFT YHSFRYVEIH
     GIEKENINDI KAIYVYTNLE ESGSFKCSNE FLNKLYDVGK NTKLNNIHSI FEDCARERLG
     YGGDMVCLAT SQIFMFNTEK LYEKVIKDFR YDIRENGGVT ETAPFIGIKT NGTGDGAGPL
     GWQLVYSYMA NKLYQYYGNV RILESEYKYI KSQVDYLMGI GFKKLSKCCL GDWGSAEAKE
     GPYRKISPAW EFTTSCFYYY HIELLSKFAK IIGNEDDYFK YRRKVDEVKK LIISTYKNED
     GSYSDKSQTS YAFALFFDLD DEPQKLAKEF ADKIANNSYN ITCGIFGMFM TYEVLNKYNH
     QDVIYKYLNK RERSTFYNIL KKGQSTLNEF INGGDDIYTG DGASNHAMYS SYMQWLYEGL
     AGINISKNSY GANEIFIKPY FEKDIDFVQC RYKSIKGDII SDWKRDEDNI LLHIEIPSNL
     KACLLILDKR YKNCLQEYIV EKEDESYVYI DITSWNGEIN LKLT
//