ID A0A1Q3TCP6_9SPHI Unreviewed; 1140 AA.
AC A0A1Q3TCP6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Arabinogalactan endo-beta-1,4-galactanase {ECO:0000256|RuleBase:RU361192};
DE EC=3.2.1.89 {ECO:0000256|RuleBase:RU361192};
GN ORFNames=BGO52_02700 {ECO:0000313|EMBL:OJV99997.1};
OS Sphingobacteriales bacterium 44-61.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895838 {ECO:0000313|EMBL:OJV99997.1, ECO:0000313|Proteomes:UP000186208};
RN [1] {ECO:0000313|EMBL:OJV99997.1, ECO:0000313|Proteomes:UP000186208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=44-61 {ECO:0000313|EMBL:OJV99997.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic
CC linkages in type I arabinogalactans.; EC=3.2.1.89;
CC Evidence={ECO:0000256|RuleBase:RU361192};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 53 family.
CC {ECO:0000256|ARBA:ARBA00010687, ECO:0000256|RuleBase:RU361192}.
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:OJV99997.1}.
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DR EMBL; MKTW01000011; OJV99997.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3TCP6; -.
DR STRING; 1895838.BGO52_02700; -.
DR Proteomes; UP000186208; Unassembled WGS sequence.
DR GO; GO:0031218; F:arabinogalactan endo-1,4-beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0015926; F:glucosidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR048230; GalA-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR011683; Glyco_hydro_53.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR NCBIfam; NF041462; GalA; 1.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF18565; Glyco_hydro2_C5; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 2.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF07745; Glyco_hydro_53; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361192};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361192}.
FT DOMAIN 35..212
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 217..328
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 336..411
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 416..524
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 634..688
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 704..806
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 1140 AA; 128470 MW; 40FAC54576841522 CRC64;
MRVNSQQIIL GIILTQLFFN QPVFSQNGEI RKHISLDEGW RFHFGHAANA EKDFNFGIAN
IFSKSGAGLH TPIDTRFVDT TWRQLNIPHD WAVELPFVNV ANNDVTSHGY KPVGGLFPET
SIGWYRQRFT VEPADSGSRF QLQFDGIFRD AKIWLNGFYL GNNTSGYVGV SYDVTDYVRF
KGENVLVVRV DATQYEGWFY EGAGIYRHVW LNQYNNVHIA DGGLFAYSEV KGNAATVNIE
TTVENQGLAS SGVTVYSYVT SRDGKLLSQS KEQPVSLAVN SRSTVKQRLQ VNNARLWSLG
DPYLYRVVSV VKQDGKIIDQ VQHRYGIRTI AFDGEKGFFL NGKPVKLQGT NNHQDHAGIG
SALPDYMHYY RISLLKDLGA NAYRTSHNAP NTELLDACDS LGMLVVDEQR LLNSSPEYMS
QFERLILRDR NHPSVFIWSI GNEEGWIQTN STGKRIAQTL LARQKELDPS RTSTYAADLP
NVFNGVNEVI PVRGFNYRHF AVADYHKDHP SQPLMGTEMG STVTTRGIYE KDSIRGYLPD
QDITAPWWAS RAEQWWPLAA ENSYWAGGFV WTGFDYRGEP TPFEWPNINS HFGIMDMCGF
PKNIYYYYQS WWTDKDVLHI SPHWNFNKQW GKIKPVDVWV NSNADNVELF LNGKSLGKQD
MPRNGHLQWK VEYEPGTLEA VAYKKGRKLT AKIETTGPPA EVVVTPYKTT MLADGTDVSV
VNITVVDKEG REVPNADNLI RFKLEGPGKI IGVGNGDPSS HEADKCMDGL WQRSLFNGKC
QVIIQGLKKP GMIKFEATAT GLYPGSTDIL TVTPASIAQA SIDPVYILRG EAAKARETTK
MLGADISFLP ELEDRGIKFS DNGVEKDAMQ ILKDHGFNYI RLRIFNDPAQ DSGYSPKRGF
CDLEHTKQMA KRVKAAGLKL LLDFHYSDYW ADPGKQYKPA AWKGLSFPEL KKALYDYTKK
VMQELKDQGT VPDMVQIGNE INHGIVWPDG NVSNFDGLAQ LVSAGTAAVK AVDPTVIMML
HVALGGQNHE SVFFIDNMVA RGVHFDVIGE SYYPKWHGTL DDLRDNLNDL ARRYDKDVIV
VEYSQLKEEV NKIAFDLPNG KGKGTCIWEP LSTWEAIFDR QGKSNELLLK YDTISKQFIK
//
