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Database: UniProt
Entry: A0A087N962_9SPHN
LinkDB: A0A087N962_9SPHN
Original site: A0A087N962_9SPHN 
ID   A0A087N962_9SPHN        Unreviewed;      1025 AA.
AC   A0A087N962;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=IL54_1076 {ECO:0000313|EMBL:KFL45665.1};
OS   Sphingobium sp. ba1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1522072 {ECO:0000313|EMBL:KFL45665.1, ECO:0000313|Proteomes:UP000029094};
RN   [1] {ECO:0000313|EMBL:KFL45665.1, ECO:0000313|Proteomes:UP000029094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ba1 {ECO:0000313|Proteomes:UP000029094};
RA   Manzari C., Chiara M., Costanza A., Leoni C., Picardi E., Trotta M.,
RA   Volpicella M., D'Erchia A.M., Horner D.S., Pesole G., Ceci L.R.;
RT   "Draft genome sequence of a Kanamycin and Nickel resistant bacterium
RT   Sphingobium species.";
RL   Submitted (JUL-2014) 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:KFL45665.1}.
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DR   EMBL; JPPQ01000069; KFL45665.1; -; Genomic_DNA.
DR   RefSeq; WP_037473577.1; NZ_JPPQ01000069.1.
DR   AlphaFoldDB; A0A087N962; -.
DR   PATRIC; fig|1522072.3.peg.2929; -.
DR   eggNOG; COG3408; Bacteria.
DR   OrthoDB; 9761045at2; -.
DR   Proteomes; UP000029094; 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; 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   InterPro; IPR006311; TAT_signal.
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; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          320..488
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          498..595
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          603..945
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          947..1022
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
SQ   SEQUENCE   1025 AA;  111910 MW;  FF016A2571762AE3 CRC64;
     MPNLDRRSFL ATGAIVGLSA QGATAASRAN PMVVGLRTAM REMPIGIDDR QPALSWRIKA
     KTGTMQAAYR ILVSSSLAEL TRGRGDLWDS GRIESAACTG ILYAGQPLRS GQTCHWQVQI
     WDQTGKSMQS HPAFWEMGLL DQDDWYGDWL AVEGATERDD RLAGATWVGG TAPSPTQARS
     FRLPFQSGAQ TALLTIVGDG VMSRLTLDGQ PLTLPERDPN AFGGAPAYRL PLEIGAGEHV
     LTVDVAPTPG FFVKPSVSLA AQIRLVDSTG SAHRITQGWE TRLGDREPWS TAVALDRQPI
     FPWPPTPARL LRRAFDSQGA VVRARLYVAA LGGYRLWLNG GRINDDELQC EPGNYAARIP
     YRTYDVTRLV RDGANVIAAM VGDGYFASYQ APNGRYPFGA APRRFRAMLE ITRQDGRIDH
     VTTDTTWRHA EAPVQMSEIY AGEDQDLRLA QSGWDKLGFD DGQWDRAWRA PSPTAPCAAA
     LAEPVRAVRT LAPVTIRRVG NTRHIIDFGQ NFAGRVRLQV KGAAGQHVIV RHAEIVSDTG
     ELDRRNLRAA RAEDHYRLQG TGKPETLEPV FSYQGFRYAE VEGVATLTSA MIAGIQLSSA
     IPETGSFQIS DPNVQKLWLN TLWNQRSNFM GVPTDCPQRD ERLGWTGDAQ IFWDAASFNM
     DVGAFTRSYS RILRDTQAPN GAYPLWAPSP EGLGWGTNSA TPGWADAGVM LPYTAYLHSG
     DRTVVDENWA AMTAYVGGIL ATNPDGLWSK DRGADLGDWL ALDAKFPMDE TTPKALIGTA
     MLARSVDQLA QMAAWTGRAS EADRWRAQHS RIRDAFAAAF VTSDGLVGNG SQCSYILALR
     LDLVPPALRA KAGALLAADI RSRGTLLSTG FLGTPLALDA LADVGEGTLA WDLLLRSDFP
     SWGYMVRKGA TTIWERWNGD TGDVAMNSFN HYALGAVCGF LYRRIAGIDP IEPGFAKFRV
     APVFDPRIPQ FGGKVDSIRG PIETRWNFRD GHAALDLVVP SNTTAEIIVQ GTRRDVGAGH
     HQFTF
//
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