ID A0A0J1FZH2_9FIRM Unreviewed; 1681 AA.
AC A0A0J1FZH2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=RHS_5744 {ECO:0000313|EMBL:KLU68433.1};
OS Robinsoniella sp. RHS.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Robinsoniella.
OX NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU68433.1, ECO:0000313|Proteomes:UP000036477};
RN [1] {ECO:0000313|EMBL:KLU68433.1, ECO:0000313|Proteomes:UP000036477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHS {ECO:0000313|EMBL:KLU68433.1};
RX PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL Cell 159:253-266(2014).
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 -!- 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:KLU68433.1}.
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DR EMBL; JNGB01000173; KLU68433.1; -; Genomic_DNA.
DR Proteomes; UP000036477; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.2700; -; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
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; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF07554; FIVAR; 2.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF13306; LRR_5; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000036477}.
FT DOMAIN 1..186
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT REGION 1272..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1681 AA; 184539 MW; 9F32B35BB5EAA024 CRC64;
MNGKEVKLRG TCRHDVSDDL GRSMTREESY AEIAAYKNAN INHIRTSHYP ASEDLLDACD
EMGIYVEQET AVCFQGPWAD VSSKYEDFLP QFTEMIERDR NRPSILIWSL GNESNYSKVA
SQSGGNAFQD EREYLRDVDT TRPCVFSFPD TGEPAGFADI YSAHYANVTG GMGRADKPVI
HDEYAHISCY NLDELQRDVN VRNFWGESVK KGWENIFTSD GALGGALWGG IDDVFYIPEG
TTERWQSHSD GQTAGYGEWG SVLDAYLREK PEAYLTKKAY SPVRVEEEAC YISDGTMYIP
VKNWFDHTDT NELKLEYTVD GEQNEIMVGE SIAPHSDGVI TINGVSQDAQ AVNLKFYTPD
GIMVDEYNVA ISSKQYNFTP AGDQAPAIEE NEQDIVVKGK DFSVSFSKES GMILSGQFQD
QVLVTGGPYL HVTGMSLGKW NLAEIDGITA ETQEQYAVVT VNGSYANGQG VRFDIKISGN
GIITTDYTLT TAPKVTSGLK EVGISYDIDK DTDSVSWLRD GLYTAYPEDH IGRNKGVALK
VREGSDVTPD QYGVEPQWSW KDDMKNYFVY STDDPNNGLV TNDFKTMREH VWSYDVNYGL
EADAPRISVE APDANVAARV AITFDLGYVD DRDAAIKYTG GWATYDSNSD YAGTETFSSK
LGDSCEFKFT GTGIRYIGSK QKNTGLVKVY VDGEFKEEID TYSNLGNDLK QTVIYSIEGL
ENGEHTIKLE TAGGKANCIV VDAFEVLKPE GSSATEKAQL IINNQWYYPN LGWGNYTGIQ
GKLANGSTGS GTIRLTNENN LTEETITSLV NLKISAVNEE ELKVSYHVQN ESEATEVKLQ
WYRVAAGDPD SKAQVIEGAE NDILNIKGLE ANKVYCKATL LIDGKERQTV KSNGIEIGQD
SYRYYDILDD SDEFVFSGTK GTDYKTDKDK SWTANAYGKS VTYLMDTKNE AGVSFKFAGS
GIRWVGAKEN NQGIAEVTVD GGSPVEIDLF DANSSTGNQV NEVLFEQVWD EPGEHEITIN
RTGRKNPLSL GANVSLDAFI IINDVSENVR ISDVAVNENE DGSLTAGCTI TNGAPEDLEY
QWYAADAYSA QGYDKETYVA IEGAVSQNYM PSDTDAGKLL RCDVWSADVS TPVRSANAVL
AKALMIDDTD ESVQYPEGSI QDTADASYLA GNKPYNNTIT YFKDGEVKLK FNGTGIVWLS
GYDQTLRRAA VKIDDGSAES VEIRAAQGGG WDFNQYKVYG VTGLEPGNHS ITITAGTPGV
YNNADAFMVL NPGEEQPQTG SISEDVQEPK MQSGLESESE ANYGEDQAET DNTVMTQTGT
ARKEIRINGN AVMTQTGTVN RTDSQDNGNS VMTQSGTIDK SVSEDIDNAI VKLTKAISDF
KASRIEKEPV DKSKLSALIN SVNGKYNEKL YTPESWKVFI QALNAAKGVN ANDNAVQADV
SKAISALESA IRGLKPAQAK PVPVDKTALK NLYQSCASLK KADYTASTWS VLEAAMKNAA
AVINNPNATK EMTDQAYNAL NKAKSGLSKI PALPKKGSTY QTRGLRYKVT ASTSRTKTVM
LVKPAKKTYR SITIPSTVKI KGYTYKVTRI DDNAFRKNTR LSKITIGSNV TKIGKESFAG
CKKLRSVTLK SKSITSIGKY AFKNISTKAK IYVPKKKYLS YKKMLSKAKL SSKVKIIKKS
M
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