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Database: UniProt
Entry: W4V9V6_9FIRM
LinkDB: W4V9V6_9FIRM
Original site: W4V9V6_9FIRM 
ID   W4V9V6_9FIRM            Unreviewed;       728 AA.
AC   W4V9V6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:GAE90210.1};
GN   ORFNames=JCM21531_3801 {ECO:0000313|EMBL:GAE90210.1};
OS   Acetivibrio straminisolvens JCM 21531.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=1294263 {ECO:0000313|EMBL:GAE90210.1, ECO:0000313|Proteomes:UP000019109};
RN   [1] {ECO:0000313|EMBL:GAE90210.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 21531 {ECO:0000313|EMBL:GAE90210.1};
RA   Yuki M., Oshima K., Suda W., Sakamoto M., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequence of Clostridium straminisolvens Strain JCM 21531T,
RT   Isolated from a Cellulose-Degrading Bacterial Community.";
RL   Genome Announc. 2:e00110-14(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865}.
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:GAE90210.1}.
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DR   EMBL; BAVR01000059; GAE90210.1; -; Genomic_DNA.
DR   RefSeq; WP_038290784.1; NZ_BAVR01000059.1.
DR   AlphaFoldDB; W4V9V6; -.
DR   STRING; 1294263.JCM21531_3801; -.
DR   OrthoDB; 9801455at2; -.
DR   Proteomes; UP000019109; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   CDD; cd04084; CBM6_xylanase-like; 1.
DR   CDD; cd14256; Dockerin_I; 1.
DR   CDD; cd09001; GH43_FsAxh1-like; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR041542; GH43_C2.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR   PANTHER; PTHR42812:SF13; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00930)-RELATED; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   Pfam; PF17851; GH43_C2; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SMART; SM00606; CBD_IV; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF63446; Type I dockerin domain; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019109}.
FT   DOMAIN          535..658
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   DOMAIN          662..728
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000259|PROSITE:PS51766"
FT   ACT_SITE        56
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        213
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            164
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   728 AA;  80489 MW;  02F6690DB4DD0B10 CRC64;
     MLFAKKPKRS LGLKKAIVIL LVLCMSLLQS IFVYGWQSDN GDGTFNNPPL YADYPDPSII
     RVGNYFYMAS STFVGVPGLV ILKSEDLVNW EIAGHCISSF TGDSKYNLEG GTKYGNGCYA
     PSIAYKNGTF YVAVTPNGER TRIYYAKDVA GPWNYNTLGG SYFDPCLFID DDGSAYLAYG
     GAWENSIKMI QLNSNLSATV GSSRVILSYK SVEGTHLSKV NGRYYLFNAV PAQRLVCSRA
     NNVWGPYGET ITLCTAGKGG HQGGIVDLPD GTYWGYLHQD DGAIGRPTRI CPITWQNGWP
     MFGRPGYIGQ VESKYTKPIQ NKPIKVPAAS DEFNSDSLGL QWMWNHNPDN SKWSLTGTSL
     RLKATTAKDF WTARNSLTQK GQGPISTGTI KIDCSGMQPG DICGLGMLGD PRGYIAVTRD
     PKRIIMTEEE VVKATVNNIT SNILYFRLEM NFMTKQARFF WKDDNRDWQQ LGPAITMGFD
     WQYGTFQGEQ YAILNFNPNG STGYMDVDWF RLNDIPGDNQ TPQPTPTPIP RQAFTKIEAE
     SYNNQLGIQT EKCSEGGENI GFIENGDYAV YKNIDFGNGA ASFEARVASA TNGGKIELRI
     DSINGPLIGT CPVAGTGDWQ TWNTVSCDVS EVKGNHDLYL VFTGGSGYLF NVNWFTFIEA
     NNDEHLGDLN GDGKVNSTDL QVLKKHLLRI TSLTGKELSN ADVTKDGKVD SSDYTLLKRY
     ILKFITDF
//
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