ID E5WXV2_9BACE Unreviewed; 588 AA.
AC E5WXV2;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN ORFNames=HMPREF1016_01505 {ECO:0000313|EMBL:EFV30201.1};
OS Bacteroides eggerthii 1_2_48FAA.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=665953 {ECO:0000313|EMBL:EFV30201.1, ECO:0000313|Proteomes:UP000003246};
RN [1] {ECO:0000313|EMBL:EFV30201.1, ECO:0000313|Proteomes:UP000003246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_2_48FAA {ECO:0000313|EMBL:EFV30201.1,
RC ECO:0000313|Proteomes:UP000003246};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA Allen-Vercoe E., Ambrose C., Strauss J., Daigneault M., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides eggerthii strain 1_2_48FAA.";
RL Submitted (OCT-2010) 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 -!- 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:EFV30201.1}.
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DR EMBL; ACWG01000016; EFV30201.1; -; Genomic_DNA.
DR RefSeq; WP_004293786.1; NZ_GL622540.1.
DR AlphaFoldDB; E5WXV2; -.
DR HOGENOM; CLU_463570_0_0_10; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000003246; 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 CDD; cd01821; Rhamnogalacturan_acetylesterase_like; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
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 InterPro; IPR037459; RhgT-like.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR PANTHER; PTHR31321:SF141; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 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 Signal {ECO:0000256|RuleBase:RU000589}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT CHAIN 20..588
FT /note="Pectinesterase"
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT /id="PRO_5005128214"
FT DOMAIN 30..218
FT /note="SGNH hydrolase-type esterase"
FT /evidence="ECO:0000259|Pfam:PF13472"
FT DOMAIN 285..552
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT ACT_SITE 440
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 588 AA; 65595 MW; 01D207345ED666F0 CRC64;
MKNKLILLLA VLFLCSAFKA DKPVITIFMI GDSTMANKSL TGGNPERGWG HVLPGFFSED
IQVDNHAMNG RSSKSFINEG RWDKVLSLIK KGDYVFIQFG HNDEKLSAER HTDPGTTFDA
NLRKFVNETR AKGGIPVLFN SIVRRKFGTS NDKAVAEAIL QDDIRKGINP DAKRDASQDD
EVREGDKLID THGAYLDSPR NVAEELDVPF IDMNRLTHEL VEGLGPKESK KLFMWVPANT
IASMPKGRED NTHLNVYGAR VIAGITVDAI AKAVPELAKY VRHYDFVVAQ DGSGDFFTVQ
EAINAVPDFR KNVRTTILIR KGVYKEKLIV PESKINISLI GQEGAVISYD DYAGKPNIFG
ENKGTSGSSS CYIYAPDFYA ENITFENTSG PVGQAVACFV SADRVYFKNC RFLGFQDTLY
TYGKGVRQYY EDCYIEGTVD FIFGWSTAVF NRCHIHSKRD GYVTAPSTDE GQKYGYVFYD
CKLTADAGVT KVYLSRPWRP FARAVFVHCD LGKHILPAGW HNWDKKEAEK TAFYAEYDSY
GPGANPKARA AFSHQLKDLK GYEMESVLSG SDNWNPVANG NALVSIKR
//
