ID A0A2B4S0Y2_STYPI Unreviewed; 3185 AA.
AC A0A2B4S0Y2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Beta-glucuronidase {ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.31 {ECO:0000256|RuleBase:RU361154};
GN Name=bgaM {ECO:0000313|EMBL:PFX22450.1};
GN ORFNames=AWC38_SpisGene13019 {ECO:0000313|EMBL:PFX22450.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX22450.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
CC -!- FUNCTION: Plays an important role in the degradation of dermatan and
CC keratan sulfates. {ECO:0000256|ARBA:ARBA00003025,
CC ECO:0000256|RuleBase:RU361154}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate;
CC Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31;
CC Evidence={ECO:0000256|RuleBase:RU361154};
CC -!- ACTIVITY REGULATION: Inhibited by L-aspartic acid.
CC {ECO:0000256|RuleBase:RU361154}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361154}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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:PFX22450.1}.
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DR EMBL; LSMT01000239; PFX22450.1; -; Genomic_DNA.
DR STRING; 50429.A0A2B4S0Y2; -.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProt.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004566; F:beta-glucuronidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 1.25.40.390; -; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 1.10.8.400; Enoyl acyl carrier protein reductase; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR Gene3D; 2.40.170.20; TonB-dependent receptor, beta-barrel domain; 1.
DR Gene3D; 2.170.130.10; TonB-dependent receptor, plug domain; 1.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR040794; CE2_N.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR012910; Plug_dom.
DR InterPro; IPR037066; Plug_dom_sf.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR033985; SusD-like_N.
DR InterPro; IPR012944; SusD_RagB_dom.
DR InterPro; IPR023996; TonB-dep_OMP_SusC/RagA.
DR InterPro; IPR023997; TonB-dep_OMP_SusC/RagA_CS.
DR InterPro; IPR036942; TonB_rcpt_b-brl_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR NCBIfam; TIGR04056; OMP_RagA_SusC; 1.
DR NCBIfam; TIGR04057; SusC_RagA_signa; 1.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF13715; CarbopepD_reg_2; 1.
DR Pfam; PF17996; CE2_N; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
DR Pfam; PF07715; Plug; 1.
DR Pfam; PF14322; SusD-like_3; 1.
DR Pfam; PF07980; SusD_RagB; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF56935; Porins; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Lysosome {ECO:0000256|RuleBase:RU361154};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 2698..3013
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 3185 AA; 362476 MW; FDD569A2373A1A0A CRC64;
MKFEQEQKIK GVVTDSSGDP LPGVSVIYSI SEKKSVVITD FDGNFELKAP LGTTLEFSYL
GFQKQTLTIT ESSFGKILSI VMQEASSQLD DVVVIGYGKK RQSTLTGSVA SVKGEKITQA
PVANVTNALA GRVAGLSVSQ GSAEPGADGA RLSIRGTNTF KNNSPMIVID GIPNRGGVDR
LNPEDIETIT VLKDASAAIY GSRAANGVIL VTTKKGREGK LKVNYNSNTS FTQPTLIPEM
MNAAEYLDAM NDLLIYQKVP YAEWSSAKTA FNKSGSYTTK AGTKLSGTHP DVLEKHRSGE
DLWRYPDTNW HNALFKAMSL QQRHTLGLSG GTERLKIHAS IDYLTQDAFY KKSATGYDQF
GTRVNGDLKI NESIKLNFSL MARQENRRYP TRSAQDIFDF TFRGKPNSPA FWPNGKPGPD
IEYGNNPVVI STDLTGYNRT RNYVFQNNLT LHFSPKEIKG FNIDLTVGTD KYFNQNKVFR
KPWYLYTWDG SSVDANNTPL LTRAKRGGLD KPELTKSSSE QTAILLQAMA SYKRRFGGHA
IETTFVINRE TDFFDQMWAY RQGYISDTTD QLFAGSDNQK DNSGSSYRTA RMSYVGRINY
ELNRKYLIEL VARYDGSYLF PKNKRFGFFP SLSAGWIISR ESFMTNISWL DFLKIKGSYG
QMGNDGVDPF QHLSTYEFDT YAIAGKPYTT LRESSFPNKD ITWEVSNKTN VGIETRFLED
RLSLNLDYFY NKRTNILTTP SASLPSSSGI TPSDKNIGSM ENRGFDFEVS WGDSIGKDFY
YNIGLAGQYS KNKLLFWDEA KPNRADFKTD EAYQYRLEVF NRQKAEGYQL WSGGQNYVLY
KYIGVLKDEK AIKDNKVDYS ALTSNLRPGD MMFEDVNKDG KITEDDAIRS DKTPRHPWQM
GLNIELRYKN FDFSMLWTAM IGGATQIQYN NSANTIYQKT MFYKNIKNIK AIFCMLTLAF
LTNCAADLEI AAENKISSDR VWKDFSLAEA AVTQLYKALG NPLGQYGLLS NLSDESYHLF
WGENYDLSGT RTAGNMDFSG WEWYGWAHQY QYIRAANVTI EGLLKGDLKN KEREVLLGQA
YFIRAYCYHR LLSHYGGVPV IDRALDQNEN LKFTRNSFKE TVDFIVKDCD EAIKLLDGKN
VDLGRANQAS VMALKSRVLI RAASDLHHIP TSSTKVSIIA AFKNKELLGY VSGDQTQRYQ
KAKLAAKALI DKGGYGYKLN LSAPAKFDEA KQNYQNIYLH RNGGERDIIL RRTYVNDRNF
TGNDDGVNFA KYNGPNGYNA WGGLNPLQNL VDSYRMKDGA TFSWDNHYPY TDREPRFYAT
ILYNRSKWKK RPANTKVYDA YDELQTGWLQ AYDNENKEVW LEGIDRYGAP VNRQNGTWTG
YYYKKFMDPS PTFNYESDLQ YISFPTFRYT EVIFNYIEAC LKTGEETTAR NWLNKIRFRS
GLPATTASGT KLWEAYVTEK QIEMVLEEQR FYDTRRWLIA PSTLGAKARK IEISVYLKSV
VFLSYGQHHI PADHPLIQYR GRVCFTNPKA PSFSMPSSSI KIKFDGTSLK GDFYGENFDG
DGYSYLMVII DGDGDAKNRK ILKIKKGRRK YQICKGLRDQ PHTVELVKLS EYWSKVTFYG
FTSDTANILA LPKKSKHLIE FYGDSNASAW TAWNDKDKGG DADAEGYFSY PAFTARALGT
ELVNFSAGGH GMTTKLKELN LTKHIDKIHL RTKEADRNIW NFKNNYLKNN PEVVVINLGA
NDYYNGADKK MLMNAWEKMI RKQLRPIYPN ANIVLANSEG WAIGEPSDYL EEMMERLKKL
GETRVSYVKF PWLWGESHAV IAEQAHFANI LIHHIAKITG WEILADADYK KYDLSYAKNH
LLANHSFEKS VMIRPDGWRP EELKIDAYTM SDSEEAFDGD HYLECPSGAM VQQTVKATKG
DRFLISIWIK GEVTTLKITA QELPNDWENP KVVGINKLPA RNTSLSYASA KAALTDEIDS
NSRYKCLDGL WKFSFAPTVD KAVVGFENPN YDVSKWKEIP VPSNWELKGY GRAIYKNVGY
AFAKQDYPKV PKDDNPVGSY RRDFSIDKHW KDKKIILHFG GVTSAFYLWV NGKKVGYSQG
SRLPAEFDIT DYLKPGKNTL AVKVFRFSDG SYLEDQDHWR ISGIHRSVYL EATPKTFIYD
FGTRTILDDK YQDATLQILP KINLAKGAKY EDFDIEAQLF DNSDRPVLKK PLLKNLKDVK
KIAGKYWDGI NFKENFAFLK TTIKNPLKWS AEHPNLYTLV LTLKNKNGEI LEARKTRIGF
RKLEIKDGVF LVNGRAVKLY GVNRHDHSQH EGKVISKEIM KRDITLMKKH NFNAVRTSHY
PNNPYWLDLC DKYGLYVIGE TNIETHGLAG VFSNNNEWSH AFLERAIRMV ERDKNHPSIV
FWSLGNESGQ GPNHAAMSGW IKNYDPTRFI HYEGARYFGI NHNGKSDDTY VDVRSRMYVS
TEEMVQLANL ETDKRPIMWC EYAHAMGNSL GDFGAYWKAI RANKRFIGGF IWDWTDGAVW
VKNKEGKYYW AYGGDFGEER HDGNFNNNGI ISPDQSIKPE ILEAKKIQQP IGIEAIDLKK
GIFEIRNYHH FSDLSGYQMR WEISANGKVI QKDIGKTPDL KAGEKGFANI RYQKIKPIAG
THYYLKISFH LKEKKAWASK GYRVAWQQFK LPYYKAAKKV RYKSRKSPLL QKTKDSWTVT
TTKNRVDFDP TSGLLTGIYQ KNKALLKKAL TPYFWRPQTD NDHGYDMSAS DQKYWKTAFE
NAKATKMNST KKAGYIELKA SYDLPKYEDK EAGTLTLCYK IWNDGQIDID YLLDPIADLP
DIPRVGLQMR LISSLDHFSW LGRGPQENYS DRKESAAFGH YQKSVTKDFF HYVRPQESNN
YTGVEWFGLT NKKQAGLMVV AMEKALSVSA WPYSPEDLDK GKKGIIFGAL DSNSIAWKIA
ERAHEEGAKF VLTNAPVAMR MGAINELAEK TGSEIIPADA TSMEDLNTLV EKSMEILGGK
IDFVLHSIGM SINVRKKKPY TENNHDWTHK GFDISALSFH RVMQVLYKKE AMNEWGSIVA
LTYMAAQRVF PDYNDMADNK AYLESIARSF GYFFGRDHKV RVNTISQSPT RTTAGSGVKG
FDGFMKYAEE MSPLGNATAA DCANYAMTLF SDLTKRITLQ NLYNDGGFSN MGVSDAIMKK
FEEEA
//
