ID W4UXU6_9BACE Unreviewed; 319 AA.
AC W4UXU6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN ORFNames=JCM10512_3833 {ECO:0000313|EMBL:GAE85403.1};
OS Bacteroides reticulotermitis JCM 10512.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1445607 {ECO:0000313|EMBL:GAE85403.1, ECO:0000313|Proteomes:UP000019131};
RN [1] {ECO:0000313|EMBL:GAE85403.1, ECO:0000313|Proteomes:UP000019131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10512 {ECO:0000313|EMBL:GAE85403.1,
RC ECO:0000313|Proteomes:UP000019131};
RA Yuki M., Oshima K., Suda W., Sakamoto M., Iida T., Hattori M., Ohkuma M.;
RT "Draft Genome Sequence of Bacteroides reticulotermitis Strain JCM 10512T,
RT Isolated from the Gut of a Termite.";
RL Genome Announc. 2:e00072-14(2014).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O =
CC [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol;
CC Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;
CC Evidence={ECO:0000256|RuleBase:RU000589};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5. {ECO:0000256|RuleBase:RU000589}.
CC -!- SIMILARITY: Belongs to the pectinesterase family.
CC {ECO:0000256|ARBA:ARBA00008891}.
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:GAE85403.1}.
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DR EMBL; BAIV01000026; GAE85403.1; -; Genomic_DNA.
DR AlphaFoldDB; W4UXU6; -.
DR STRING; 1445607.JCM10512_3833; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000019131; Unassembled WGS sequence.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0042545; P:cell wall modification; IEA:UniProtKB-UniRule.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR033131; Pectinesterase_Asp_AS.
DR InterPro; IPR000070; Pectinesterase_cat.
DR PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR PANTHER; PTHR31321:SF141; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085,
KW ECO:0000256|RuleBase:RU000589}; Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Reference proteome {ECO:0000313|Proteomes:UP000019131};
KW Signal {ECO:0000256|RuleBase:RU000589}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT CHAIN 21..319
FT /note="Pectinesterase"
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT /id="PRO_5005150348"
FT DOMAIN 24..292
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT ACT_SITE 178
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 319 AA; 36111 MW; 2289D0164A0544A7 CRC64;
MKLKLLYLSL AIFISLQASA ADFDLVVAKD GTGDFTTVQE AINAVPDFRK VRTRILIKAG
SYKEKVIIPA TKTFLSLIGE DEAIITYDDY ASKKNRYGEE VGTSGSSTLY IFAPDLFAEN
ITFENSSGPV GQAVACFVAA DRVHFKHCRF LGFQDTLYTN YDQSRQYYEA CEIWGSIDFI
FGASTCIFYK CHIHSLADGF ITAPSTNEGE KYGYIFYDCR ITAEKEVKDV YLSRPWRPYG
KAVFIRCELG AHINPLGWDP WDKPNPAHTV FYAEYKNSGK GANTKHRAVF SRQLKNLDDY
EIEKILARED GWNPIQSKQ
//
