ID   A0A1Y4D1B4_9BACT        Unreviewed;       679 AA.
AC   A0A1Y4D1B4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Pectate lyase superfamily protein domain-containing protein {ECO:0000259|Pfam:PF12708};
GN   ORFNames=B5F77_10255 {ECO:0000313|EMBL:OUO51549.1};
OS   Parabacteroides sp. An277.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=1965619 {ECO:0000313|EMBL:OUO51549.1, ECO:0000313|Proteomes:UP000196154};
RN   [1] {ECO:0000313|Proteomes:UP000196154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An277 {ECO:0000313|Proteomes:UP000196154};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC         residues in alpha-D-galactosides, including galactose
CC         oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC         Evidence={ECO:0000256|ARBA:ARBA00001255};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing branched (1->3)-alpha-D-
CC         galactosidic residues, producing free D-galactose.; EC=3.2.1.n1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001271};
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:OUO51549.1}.
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DR   EMBL; NFJB01000023; OUO51549.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4D1B4; -.
DR   OrthoDB; 1100947at2; -.
DR   Proteomes; UP000196154; Unassembled WGS sequence.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR024535; Pectate_lyase_SF_prot.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF12708; Pectate_lyase_3; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000196154}.
FT   DOMAIN          122..320
FT                   /note="Pectate lyase superfamily protein"
FT                   /evidence="ECO:0000259|Pfam:PF12708"
SQ   SEQUENCE   679 AA;  75664 MW;  025E597139799915 CRC64;
     MILRISNIFI NVLVFIILGT YTLSAHNWPE FTPKETISAG VYVVTQDHAV TTNMTMQEGV
     TLIFDGGKLT GSAKIMGNYT QIIASKTQIF DTSLSFDGIW NIDRAYPEWF GAKASTSTNP
     FDCSAAINKA IELKQVGEVY ISRGNYYIKY PINMKYGIIL CGEKAVMVSE EENAGSTICI
     WPYDKENCLP HFSSTKDFII TVNVKNASSN PMWVKTYPAP LTAIRNIYFY NNDAKNAILK
     GVLFSGGMEI THCRWWNFAQ AVKSVSSVYA DNKIITDCQF DNNVNGAFND SYAFDLSGLG
     DNLTFKRNHI TKAGGSYKFK GLKVDKTNGA EICDNIINAS SLIKDSKAVS FVSNHLEGDD
     TQLTIQRSVV HVSNNFFEKG TEPSLVFDEN ADNYDLSVVS LVDNSFLYYE HEKKDSQNKD
     YIEPISMYDL QIDGRISLEI SNSYRYWVKR NMISKVYPIG LTLCDKSGNS IDSFNKYSYF
     LSTKGSLKTA STGANVCIQC NSALNTGNVS WTIMTNSQVK WKIESDTYTY SAILIWDKDR
     KIVHPKVNMT SVNPTKNGNG VLMWMNGAND IGHQAMVRLI RTGNNTTKYV DLPFTGTHFI
     YDNGLSVCGF PWKNADNSIT EITGITPIGA IEFVGNNVVC RSKTKPASTS GWKNGDIVYN
     LGSGTNAMWI LSDNVWIDK
//