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Database: UniProt
Entry: A0A1U7GIT2_9BACT
LinkDB: A0A1U7GIT2_9BACT
Original site: A0A1U7GIT2_9BACT 
ID   A0A1U7GIT2_9BACT        Unreviewed;      1084 AA.
AC   A0A1U7GIT2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=BGO49_18205 {ECO:0000313|EMBL:OJW18971.1};
OS   Planctomycetales bacterium 71-10.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales.
OX   NCBI_TaxID=1895807 {ECO:0000313|EMBL:OJW18971.1, ECO:0000313|Proteomes:UP000185848};
RN   [1] {ECO:0000313|EMBL:OJW18971.1, ECO:0000313|Proteomes:UP000185848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=71-10 {ECO:0000313|EMBL:OJW18971.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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   -!- 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:OJW18971.1}.
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DR   EMBL; MKTT01000085; OJW18971.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U7GIT2; -.
DR   STRING; 1895807.BGO49_18205; -.
DR   Proteomes; UP000185848; Unassembled WGS sequence.
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; 3.
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; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008902; Rhamnosid_concanavalin.
DR   PANTHER; PTHR33307:SF10; 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   PIRSF; PIRSF010631; A-rhamnsds; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1084
FT                   /note="alpha-L-rhamnosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012617554"
FT   DOMAIN          351..518
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          530..630
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          637..973
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          975..1048
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
SQ   SEQUENCE   1084 AA;  117368 MW;  D9809E4DCD3F6F1A CRC64;
     MLNRRFGRAL LAAALAGAAA SPSRAQQAAA PADGLAFSPA YLRVEAKVDP LGVDATNPRL
     SWLVASSRRG EVQSAYQVVV SSDAAKLAAD EGDLWDSGKV QSDETTGVAY AGAPLKSGQK
     ALWKVRLWDG AGQPSDWSAP ASWTVGLLDP SDWKARWIGY DAARDDKAAA VEADFGAAKW
     IWHADDKGGD KPKAHRLFVT EFDVPADSPI AEATLLAGAD DSHRYTVNGE LIAAGTSHKV
     PLQVDALRAV RPGKNKLRVE VENGAPSPAG LIARLTVKLK DGRVVENVTD ASWKSVADPG
     QNWHSREIDV AGLPAAEVVA NYGDGPWGKL TVTKLVLPKP ALLRTEFQVS KPVKRATVYT
     TALGIHDVHL NGSRVSDDLF NPGWTDYTKR VLYRTYDVTP LVAQGANALG AIVADGWYSG
     YVGFGKVRDH YGKKTRVKAQ LVVEYADGTS DVIATGPDWK AAVGPFLEAD FLMGETYDAR
     LEKSGWDRPG YDASSWAAVD TGSEMDPKVE AHRGPAVTAY QELRAKTYSE VKPGVYVIDY
     GQNFAGVPRI RVRGEAGRAI TLRFAERLNP DGTIYTTNLR EARCIDTYVC KGTGEDEVWS
     PRFTFHGYQY LEVSGLKSPP NSETVVGLAI SSATPVVGRF QTSDPMLNQL YSNIVWTQRM
     NFIDIPTDCP QRDERLGWTG DAQVYIKTAT LNADVQAFFD KWLVDLTDGQ RADGQFPMVA
     PVKVAGDDGG PAWAEAGVVC PWTIYQVYND KDVLARQYPS MAKYVDFLVN RSTPDLLPPE
     KYHAFGDWLS IGADTPKDVI YTAYFALAAR LTSQAAAALG KAEDAKKYAD VYEKIKASFN
     KAYVGDDGVV KGDTQACYVL ALANDLVDGE RAKKAAELLV KRIEDKDWHL STGFIGTKDL
     MLVLSKIGRQ DVAYRLLFND TFPSWGFSIR HGATSIWERW DGWTPDKGFQ DPGMNSFAHY
     SFGAVYGWIV ENVGGIHAAD VAYKKIVIEP QLTDKLTFAT TSYRSVRGEI AVTWTRAGGV
     ATVDVTVPPN TTAKVVLPAA DPAAVAESGV ALAQAQGVTK AAAEAGKTVA EIGSGRYVFT
     FAAP
//
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