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Database: UniProt
Entry: U4KQT2_9MOLU
LinkDB: U4KQT2_9MOLU
Original site: U4KQT2_9MOLU 
ID   U4KQT2_9MOLU            Unreviewed;       713 AA.
AC   U4KQT2;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=BN85301020 {ECO:0000313|EMBL:CCV65123.1};
OS   Paracholeplasma brassicae.
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Paracholeplasma.
OX   NCBI_TaxID=61635 {ECO:0000313|EMBL:CCV65123.1, ECO:0000313|Proteomes:UP000032737};
RN   [1] {ECO:0000313|EMBL:CCV65123.1, ECO:0000313|Proteomes:UP000032737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0502 {ECO:0000313|Proteomes:UP000032737};
RX   PubMed=24158107; DOI=10.1159/000354322;
RA   Kube M., Siewert C., Migdoll A.M., Duduk B., Holz S., Rabus R.,
RA   Seemuller E., Mitrovic J., Muller I., Buttner C., Reinhardt R.;
RT   "Analysis of the Complete Genomes of Acholeplasma brassicae , A. palmae and
RT   A. laidlawii and Their Comparison to the Obligate Parasites from '
RT   Candidatus Phytoplasma'.";
RL   J. Mol. Microbiol. Biotechnol. 24:19-36(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};
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DR   EMBL; FO681348; CCV65123.1; -; Genomic_DNA.
DR   RefSeq; WP_030003992.1; NC_022549.1.
DR   AlphaFoldDB; U4KQT2; -.
DR   STRING; 61635.BN85301020; -.
DR   KEGG; abra:BN85301020; -.
DR   HOGENOM; CLU_009782_1_0_14; -.
DR   OrthoDB; 9766741at2; -.
DR   Proteomes; UP000032737; Chromosome Acholeplasma brassicae.
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; 2.60.420.10; 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; 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   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000032737}.
FT   DOMAIN          198..294
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          310..623
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
SQ   SEQUENCE   713 AA;  82336 MW;  A5A5F928840FA08B CRC64;
     MFQNAKWIWH HNIIQKNDYG VFVKSFEVDR FNKAILNISG HNHIKLYIND KLISGYVTPA
     PSGLNPKSYL SYDVSKDLLE GNNTIKVVVL YLGGSGQNYQ NGIPGFILNL EIEEEAGVRH
     ILSDETFSSI KNHPYVTGQP FQQNRRITPV ERFDSSKLDE GPIHEPVLVL EGYHNYRKQT
     IKEGIVHKTY EPRLLSQSNT VYVFDADRIV SGFVGLDILS QTNQVLRVRY SEDLDGDRVK
     HNVANEPSET YYDELILKKG MRVSHAFDFT YKAFRYVEVE GNLDELESFS LKVEVASTDL
     GIVGDLKSKS YPMITDLFTL FKHTQTNNTL GLLVDCPHRE QAQYLGDSAL QAESIVYNVL
     ERKPLLEKVL DDFMDAQYAD GTFPFVSPGS TNDEEFSLKI PEYDLYFIEL LEKRYQIDLD
     QKILHRYYEA SKKVIDHYIS KIDEQGLVRK NEHWHISDWP YPSVDQEGDY LCFENMHFHK
     NLSSFIKLYQ DRIDQDYYRK LKDKLYLRIR EVFLERELFK DHEKAASYHQ GIQAFALNHG
     FVLDSELDAV ITYIKQSGFS SSIILGRDVV HALLKSGYTK EALDYMFNYE KGWGTILRHG
     SKTMWEGFDD IESHSHAWGM YVVRLIQTYL VGINVINPDT YIIKPIMIDE VKDIAATIVT
     ERGLLSFSYE VKESDVIYTY DIPLGIQVSL IHNQLTFNLK SAGILKCKKE SVV
//
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