ID A0A1U9N7A6_9GAMM Unreviewed; 595 AA.
AC A0A1U9N7A6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN ORFNames=B0D95_05110 {ECO:0000313|EMBL:AQT59533.1};
OS Cellvibrio sp. PSBB023.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1945512 {ECO:0000313|EMBL:AQT59533.1, ECO:0000313|Proteomes:UP000189646};
RN [1] {ECO:0000313|EMBL:AQT59533.1, ECO:0000313|Proteomes:UP000189646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB023 {ECO:0000313|EMBL:AQT59533.1,
RC ECO:0000313|Proteomes:UP000189646};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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}.
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DR EMBL; CP019799; AQT59533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9N7A6; -.
DR STRING; 1945512.B0D95_05110; -.
DR KEGG; ceb:B0D95_05110; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000189646; Chromosome.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042545; P:cell wall modification; IEA:UniProtKB-UniRule.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd04082; CBM35_pectate_lyase-like; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; PF00553; CBM_2; 1.
DR Pfam; PF16990; CBM_35; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS51175; CBM6; 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};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Reference proteome {ECO:0000313|Proteomes:UP000189646}.
FT DOMAIN 4..105
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT DOMAIN 149..274
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT ACT_SITE 454
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 595 AA; 62344 MW; 1E0D534FDD01BB2B CRC64;
MTFSPFLWAE CTYQVTNNWG SGFTAEIKVT NNTNQTVNNW SVSWQEANAS VTNAWNATLS
GANPYTATGL SWNATLAPNA SASFGFQANG TAGAPKVNGS LCDNNTQTSS LTATSSSVRS
SSAISSVSSS VTTSANQSAR SSASSVSNWL FEENSLGFCN YSGVVATNHA GYTGTGFVDS
ENVLGAAINW SVSAASANTY AISIRFANGG AATRRAAIVV NNNKLLSVDF PSNNNWAAWQ
TVTVNVPLNA GVNSLKAQAE TNDGLANIDS ISIAGLGITP AACPTTAVTM DCNSITDQPV
LRVAADGSAT YRTLQAALNT LPATNTTPTQ IRIKPGVYRE KLTINKPFVT FCGEAGKQSS
TILTNNDSAS TLKPDGTTLG TSGSASVTLR ANDISMENIT IENTFGVGSQ AVALLAQGQR
LQFRNCRLLG HQDTLYVHSG TQYYRNCHIQ GTVDFIFGAA TAVFENNTIH SVGGGTAITA
PSTEQQVPYG LVFLGGKVTA VSNVAKGSVA LGRNWRPYGA ATYIRTELGQ HISNVGWVKM
SENTLDTARF SEYQTTGAGA TTSGRAPQSR QLTAAQAATY NINSIFGSWV PSYSK
//
