ID R5V0W3_9BACE Unreviewed; 539 AA.
AC R5V0W3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCZ74557.1};
GN ORFNames=BN535_00785 {ECO:0000313|EMBL:CCZ74557.1};
OS Bacteroides caccae CAG:21.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1263037 {ECO:0000313|EMBL:CCZ74557.1, ECO:0000313|Proteomes:UP000017990};
RN [1] {ECO:0000313|EMBL:CCZ74557.1, ECO:0000313|Proteomes:UP000017990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:21 {ECO:0000313|Proteomes:UP000017990};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family.
CC {ECO:0000256|ARBA:ARBA00008834, ECO:0000256|RuleBase:RU361169}.
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:CCZ74557.1}.
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DR EMBL; CBAN010000179; CCZ74557.1; -; Genomic_DNA.
DR AlphaFoldDB; R5V0W3; -.
DR Proteomes; UP000017990; Unassembled WGS sequence.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR31339; PECTIN LYASE-RELATED; 1.
DR PANTHER; PTHR31339:SF9; PLASMIN AND FIBRONECTIN-BINDING PROTEIN A; 1.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SMART; SM00710; PbH1; 7.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS00502; POLYGALACTURONASE; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361169};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361169}.
SQ SEQUENCE 539 AA; 59107 MW; C69452A536A9A873 CRC64;
MNTLTKRLLW IAVCCLPFIS GCKQPNENAV SKNAISDALY QNLPFEMPEV QQPAFPAYEV
NIEKFGAKGD GLFLNTKAIN DAIKDVNQRG GGKVIIPEGI WLTGPIELLS NVNLYTEQNA
LVLFTGDFEA YPIIDTSFEG LETRRCQSPI SARNAENIAV TGYGTFDGNG DCWRPVKKEK
LTASQWKKLV NSGGVLDEKQ EIWYPTAGSL KGAMACKDFN VPEGINTDEE WAEIRPWLRP
VLLSIVKSKK VLLEGVTFKN SPSWCLHPLS CEDFTVNNIM VINPWYSQNG DAIDLESCKN
ALIINSVFDA GDDAICIKSG KDEDGRRRGE PCQNVIVKNN TVLHGHGGFV VGSEMSGGVK
NIYVEDCTFM GTDVGLRFKS TRGRGGVVEN IYINNINMIN IPNEPLLFDL FYGGKGAGEE
SEEDLLNRMK TAIPPVTEET PAFRNIHISN IVCRGSGRAM FFNGLPEMPI SNVTVTNVVM
TEATDGVVIS QVDGVTLENV YVESAKGNNI LNVKNAKNLT VDGKVYEELG AKGQILSLK
//
