ID A0A3G3GTF0_9BACT Unreviewed; 633 AA.
AC A0A3G3GTF0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN ORFNames=DTQ70_21470 {ECO:0000313|EMBL:AYQ34573.1};
OS Runella sp. SP2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae; Runella.
OX NCBI_TaxID=2268026 {ECO:0000313|EMBL:AYQ34573.1, ECO:0000313|Proteomes:UP000270973};
RN [1] {ECO:0000313|EMBL:AYQ34573.1, ECO:0000313|Proteomes:UP000270973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|EMBL:AYQ34573.1,
RC ECO:0000313|Proteomes:UP000270973};
RA Jin H.M.;
RT "Genome sequence of Runella sp. SP1.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP031030; AYQ34573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G3GTF0; -.
DR KEGG; rup:DTQ70_21470; -.
DR OrthoDB; 9777975at2; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000270973; Chromosome.
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; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR049492; BD-FAE-like_dom.
DR InterPro; IPR002168; Lipase_GDXG_HIS_AS.
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 InterPro; IPR018040; Pectinesterase_Tyr_AS.
DR PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR PANTHER; PTHR31321:SF141; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR Pfam; PF20434; BD-FAE; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR PROSITE; PS00800; PECTINESTERASE_1; 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:UP000270973};
KW Signal {ECO:0000256|RuleBase:RU000589}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT CHAIN 20..633
FT /note="Pectinesterase"
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT /id="PRO_5017846645"
FT DOMAIN 26..313
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT DOMAIN 381..571
FT /note="BD-FAE-like"
FT /evidence="ECO:0000259|Pfam:PF20434"
FT ACT_SITE 180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 633 AA; 70384 MW; FBC61A6FEAB341B1 CRC64;
MKQIFFVGLL LAGSLFAQTA PKNLLIVAQD GSGDFTTVQA AFNAIPLNNM KDVLIRIKKG
IYKEKLTLDS TKNHVTIMGE DPENTVLTYD DFSGKINPQG VKLGTTTSTS TRIVANDFTA
INITFANSAG PVGQAVAMLV DGDRARFVNC RFLGCQDTLY PKREGTRQYY QNCYIEGTVD
FIFGWATAYF QQCHIRSKLQ GGYYTAASTP QGQAHGFVFN ECTLDGESPE ASVYLGRPWR
DYAQTVFLNC TMSNVVKPEG WHNWDKTHAE KTTFYAEYGS KGAGATASKR VPWSKQLTEI
EAQRYTIWKV LAGKDNWNPQ GPLLTFGLTN VPDTSFNVPK AFSQLQKQYP KASKVAFPLP
NTVAEERNLT YCALGTRNLQ LDVFYPKSKS KKPRPAVLVI HGGGWRSGDR THHIPLAQKL
AEQGFVAVTV EYRLSTEALY PAAVHDLKAA VRWVRANAKK YNIDPNKIAS LGFSAGGQLA
ALLGTTNDNP AFEGSQGEYM AFSSRVNAIV DLDGTLAFIH PESGEGDDSR GISAATYWFG
YNKTQKPELW HEAGALNHVD KNTPPILFVN SSVERMHAGR DDMRRKLDAL HIYSEVHSFP
DAPHTFVLFH PWFEPVLNHS VRFLNKVFET KER
//
