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Database: UniProt
Entry: I0H9A3_ACTM4
LinkDB: I0H9A3_ACTM4
Original site: I0H9A3_ACTM4 
ID   I0H9A3_ACTM4            Unreviewed;      1029 AA.
AC   I0H9A3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   OrderedLocusNames=AMIS_43700 {ECO:0000313|EMBL:BAL89590.1};
OS   Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 /
OS   JCM 3121 / NBRC 102363 / NCIMB 12654 / NRRL B-3342 / UNCC 431).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=512565 {ECO:0000313|EMBL:BAL89590.1, ECO:0000313|Proteomes:UP000007882};
RN   [1] {ECO:0000313|EMBL:BAL89590.1, ECO:0000313|Proteomes:UP000007882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 /
RC   NCIMB 12654 / NRRL B-3342 / UNCC 431
RC   {ECO:0000313|Proteomes:UP000007882};
RA   Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H.,
RA   Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.;
RT   "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC
RT   102363).";
RL   Submitted (FEB-2012) 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};
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DR   EMBL; AP012319; BAL89590.1; -; Genomic_DNA.
DR   RefSeq; WP_014444484.1; NC_017093.1.
DR   AlphaFoldDB; I0H9A3; -.
DR   STRING; 512565.AMIS_43700; -.
DR   KEGG; ams:AMIS_43700; -.
DR   PATRIC; fig|512565.3.peg.4356; -.
DR   eggNOG; COG3387; Bacteria.
DR   HOGENOM; CLU_002926_1_1_11; -.
DR   OrthoDB; 9761045at2; -.
DR   Proteomes; UP000007882; 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; IPR016007; Alpha_rhamnosid.
DR   InterPro; IPR035396; Bac_rhamnosid6H.
DR   InterPro; IPR035398; Bac_rhamnosid_C.
DR   InterPro; IPR013737; Bac_rhamnosid_N.
DR   InterPro; IPR000421; FA58C.
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   PIRSF; PIRSF010631; A-rhamnsds; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007882};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1029
FT                   /note="alpha-L-rhamnosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003627870"
FT   DOMAIN          213..314
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
SQ   SEQUENCE   1029 AA;  111732 MW;  E38C59AC622FF982 CRC64;
     MPRTLLSTLT AAALLITLAP SPAQAHTITG APAALRTDGK TDPLGTDLAP PQLSWRDTRT
     GHVAYQIQAA TSPAKLAHPD LWDSGRVRGT DISARYAGRA LTERTRVYWR VRTWTSRTTS
     TAWSAPAWFE TGIKDWKAQW IGNEDWQLST KPVTPVVVSL PKQTARFVRL DVSKLGLPLA
     EQPLDSKNRA VMTGGFPAPT YRLQLAELEV RDSATPGVNL AEGRGKNITV SETQTIRKEW
     EPALLADGTA LGYQSAAHDS PDASIQVTLD LGADKTFDRV VLQPRKDTLT ADGRTANFPV
     DYRIETATTD VWTTAATVRD QPTPEAWLPE ALPVFQKRFA TRSTIKTARL YVSGLGVYET
     KLNGRRVGDA VLEPGDVDYA DQVPYAAYDV TKALGRRNTL DIAVGNGTAN ALDHKGRYRK
     FAKQVSDPQV IAQLEITYTD GRRETIATDP TWKTALGATT VSSWYGGEDY DARRENPATW
     ENAVPAPARG PLTARIGEPV KIVERLPATR LENSVFDVGR NIAGFPEIAL TAPAGTTIRV
     YPAESLNSGH VDQSISNVGA PIWDQFTSKG GTQTWHPRFT YHGFRYLEVA GLPEGATIEV
     AGLRTMGDYD SAGTFDTDND VLDGIHRLTR RAVEGNMQSI LTDCPSREKL GWLEQDHLAF
     DAIARSYDVR PLMDKIVRDM VDAQESSGLV PSTVPDHTSL AGAYRDDPNW GGALVLVPWQ
     TYLTYGDRDI LERYYPAMQR HLAYLQGQTA RWVNGVYDYS LGDWITTEKP AMPKAIPGST
     GVWHIADGLS KIATVLGRET DAATYRTTAD SLANALWAKY YDPATGLFGG GGQGATALAL
     DIKAVPDSER PGQLQHLIDA IEAKDNHLIM GEISFPSVLQ VLSEAGRDDV IYKVATQTTS
     PSLGFQVKQG LTSLGETWDG GSGQSQNHFM LGALDAWMQR RITGIDQKSG SAGFRDLVIA
     PAVSGGPASA SGSFLSPYGR IATAWTRTGD RIRLTVTVPP GATAEIRLPG LTRTVGTGTW
     TFTARSADA
//
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