ID   Q8X891_ECO57            Unreviewed;       427 AA.
AC   Q8X891; A0A0H3JGK2; A0A6M0JSJ2; Q7AGH4;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE            EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN   Name=ybhC {ECO:0000313|EMBL:BAB34223.1};
GN   ORFNames=ECs_0800 {ECO:0000313|EMBL:BAB34223.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB34223.1, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB34223.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 /
RC   EHEC {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; BA000007; BAB34223.1; -; Genomic_DNA.
DR   RefSeq; NP_308827.1; NC_002695.1.
DR   RefSeq; WP_001091577.1; NZ_VOAI01000019.1.
DR   AlphaFoldDB; Q8X891; -.
DR   STRING; 155864.Z0943; -.
DR   GeneID; 75170771; -.
DR   GeneID; 917540; -.
DR   KEGG; ecs:ECs_0800; -.
DR   PATRIC; fig|386585.9.peg.921; -.
DR   eggNOG; COG4677; Bacteria.
DR   HOGENOM; CLU_012243_5_0_6; -.
DR   OMA; FNRMWEY; -.
DR   UniPathway; UPA00545; UER00823.
DR   Proteomes; UP000000558; 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; 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:UP000000558};
KW   Signal {ECO:0000256|RuleBase:RU000589}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|RuleBase:RU000589"
FT   CHAIN           24..427
FT                   /note="Pectinesterase"
FT                   /evidence="ECO:0000256|RuleBase:RU000589"
FT                   /id="PRO_5035352308"
FT   DOMAIN          195..338
FT                   /note="Pectinesterase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01095"
SQ   SEQUENCE   427 AA;  45981 MW;  0B33AFA4BF594170 CRC64;
     MNTFSVSRLA LALAFGVTLT ACSSTPPDQR PSDQTAPGTS SRPILSAKEA QNFDAQHYFA
     SLTPGAAAWN PSPITLPAQP DFVVGPAGTQ GVTHTTIQAA VDAAIIKRTN KRQYIAVMPG
     EYQGTVYVPA APGGITLYGT GEKPIDVKIG LSLDGGMSPA DWRHDVNPRG KYMPGKPAWY
     MYDSCQSKRS DSIGVLCSAV FWSQNNGLQL QNLTIENTLG DSVDAGNHPA VALRTDGDQV
     QINNVNILGR QNTFFVTNSG VQNRLETNRQ PRTLVTNSYI EGDVDIVSGR GAVVFDNTEF
     RVVNSRTQQE AYVFAPATLS NIYYGFLAVN SRFNASGDGV AQLGRSLDVD ANTNGQVVIR
     DSAINEGFNT AKPWGDAVIS NRPFAGNTGS VDDSDEIQRN LNDTNYNRMW EYNNRGVGSK
     VVAEAKK
//