ID   EABC_CLOPF              Reviewed;         800 AA.
AC   Q6RUF5;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Blood-group-substance endo-1,4-beta-galactosidase;
DE            Short=E-ABase;
DE            EC=3.2.1.102;
DE   AltName: Full=Blood group A-and B-cleaving endo-beta-galactosidase;
DE   Flags: Precursor;
GN   Name=eabC;
OS   Clostridium perfringens.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1502;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-59; 293-304;
RP   544-554 AND 572-589, FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 10543;
RX   PubMed=15618227; DOI=10.1074/jbc.m414099200;
RA   Anderson K.M., Ashida H., Maskos K., Dell A., Li S.C., Li Y.T.;
RT   "A clostridial endo-beta-galactosidase that cleaves both blood group A and
RT   B glycotopes: the first member of a new glycoside hydrolase family, GH98.";
RL   J. Biol. Chem. 280:7720-7728(2005).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA   Shearer A.G., Altman T., Rhee C.D.;
RT   "Finding sequences for over 270 orphan enzymes.";
RL   PLoS ONE 9:E97250-E97250(2014).
CC   -!- FUNCTION: Endo-beta-galactosidase capable of releasing both the blood
CC       group A trisaccharide (A-Tri; GalNAcalpha1-->3(Fucalpha1-->2)Gal) and B
CC       trisaccharide (B-Tri; Galalpha1-->3(Fucalpha1-->2)Gal) glycotopes from
CC       blood group A- and B-containing glycoconjugates, respectively.
CC       {ECO:0000269|PubMed:15618227}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-galactosidic linkages in blood
CC         group A and B substances.; EC=3.2.1.102;
CC         Evidence={ECO:0000269|PubMed:15618227};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 98 family. {ECO:0000305}.
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DR   EMBL; AY492085; AAR84225.1; -; Genomic_DNA.
DR   RefSeq; WP_050738144.1; NZ_SPFQ01000004.1.
DR   AlphaFoldDB; Q6RUF5; -.
DR   SMR; Q6RUF5; -.
DR   CAZy; CBM51; Carbohydrate-Binding Module Family 51.
DR   CAZy; GH98; Glycoside Hydrolase Family 98.
DR   BioCyc; MetaCyc:MON-20296; -.
DR   BRENDA; 3.2.1.102; 1503.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0033929; F:blood-group-substance endo-1,4-beta-galactosidase activity; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR   Gene3D; 2.60.120.1060; -; 1.
DR   Gene3D; 2.60.220.10; -; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013190; GH98_C.
DR   InterPro; IPR013191; GH98_central.
DR   InterPro; IPR013222; Glyco_hyd_98_carb-bd.
DR   InterPro; IPR011071; Lyase_8-like_C.
DR   InterPro; IPR038637; NPCBM_sf.
DR   Pfam; PF08307; Glyco_hydro_98C; 1.
DR   Pfam; PF08306; Glyco_hydro_98M; 1.
DR   Pfam; PF08305; NPCBM; 1.
DR   SMART; SM00776; NPCBM; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Secreted; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000269|PubMed:15618227"
FT   CHAIN           36..800
FT                   /note="Blood-group-substance endo-1,4-beta-galactosidase"
FT                   /id="PRO_0000430456"
SQ   SEQUENCE   800 AA;  90958 MW;  9229DD4C76028AC9 CRC64;
     MGGVTMKNNL KKYIKYILSV ILVFFVGVNG MEVYALEESR DVYLSDLDWL NATHGDDTKS
     KIVQKNHPFT PGNNNQSTKI SLKMEDGSIS EFEKGLGTIA GSPSTITYDI SGAGVTKFFS
     YLGIDRSANP INEQYAKVDK IEVVVDGKVI YSTINQFPNG LTYETPAIKV DLNIPENAKR
     LQLKSYAGEK TWGDEVVYAD AKFTAKGDFV NPNDWTPAEK RREISNEKPL LMIPLYANGS
     KYEKGDYAFW GDDTLVGKWK EVPDDLKPYT VIQLHPDDLP KRDGVAADFY EHMLNEAQSY
     VNPKTNKNEP IPIVLTVYTA GNVPGYTAAH WLTTEWIEDM YSKYSALQGV FSTENYWVWT
     DNVESNAAEY LKLSAKYGGY FIWSEQNNGG SIEKAFGSNG KTVFKEAVEK YWENFIFMYK
     NTPQAEGNDA PTSSYMTGLW LTDYAYQWGG LMDTWKWYET GKWKLFESGN IGKTQGNRQW
     LTEPEALLGI EAMNIYLNGG CVYNFEHPAY TYGVRNEESP LFSNVIKEFF RYVINNPSPS
     KNEMRAKTKS LLYGNFTQNG NGNYFVGLNT EMSQSPAYTT GRYGNIPAVP SSIERNKIES
     RLSGSQIKLI DMNSSELSNI TNRKEYFNKL YKEEYNGNIF AQKLDNRWFI YNYKYNENIN
     QKGSFDIANI KSEVTLEPHT YLIMEDNNQS INIKLNNYRT NKDSLWEGAK NADEAKKLPE
     MSKVDALNWV YDSYIKNTNN GEKRTSVIKL MNIDKAPTIT NVNGIEGSYD IPTVKYNSET
     RSAEITIKNN GNIDFDIVIK