ID D7IBL8_9BACE Unreviewed; 575 AA.
AC D7IBL8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN ORFNames=HMPREF9007_01665 {ECO:0000313|EMBL:EFI05023.1};
OS Bacteroides sp. 1_1_14.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=469585 {ECO:0000313|EMBL:EFI05023.1, ECO:0000313|Proteomes:UP000003951};
RN [1] {ECO:0000313|EMBL:EFI05023.1, ECO:0000313|Proteomes:UP000003951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_1_14 {ECO:0000313|EMBL:EFI05023.1,
RC ECO:0000313|Proteomes:UP000003951};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Strauss J., Daigneault M., McDonald J., Ambrose C.E.,
RA Allen-Vercoe E., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain 1_1_14.";
RL Submitted (MAR-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}.
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DR EMBL; GG774704; EFI05023.1; -; Genomic_DNA.
DR RefSeq; WP_008760992.1; NZ_GG774704.1.
DR AlphaFoldDB; D7IBL8; -.
DR HOGENOM; CLU_463570_0_0_10; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000003951; 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}.
FT DOMAIN 30..205
FT /note="SGNH hydrolase-type esterase"
FT /evidence="ECO:0000259|Pfam:PF13472"
FT DOMAIN 273..539
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT ACT_SITE 427
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 575 AA; 64714 MW; D881F0ED089089A7 CRC64;
MKNRLLLLLI VFILFSAFRA DKPVLTIFTI GDSTMANKNL YGGNPERGWC MVLPGFFSED
IRVDNHAANG RSSKSFISEG RWAKVISQVK KGDYVFIQFG HNDEKADSAR HTDPGTTFDD
NLRRFVNETR AKGGIPVLFN SIVRRNFVQP EDASIATDAR RAPGEQELPK EGNVLYDTHG
AYLDSPRNVA KEMGVAFIDM NKITHDLVQG LGPAESKKLF MFVEPEKVPA FPKGREDNTH
LNVYGARTIA GLTVDAIAKE IPELAKYVRH YDYVVAQDGT GDFFTVQEAI NAVPDFRKNV
RTTILVRKGT YKEKIIIPES KINISLIGED GAVLTNDDFA NKKNVFGENM GTSGSSSCYI
YAPDFYAENI TFENSAGPVG QAVACFVSAD RAFFKNCRFL GYQDTLYTYG KHSRQYYEDC
YIEGTVDFIF GWSVAVFNRC HIHSKRDGYV TAPSTDQGKK YGYVFYDCRL TADPDVAKVY
LSRPWRPYAQ AVFIRCELGK HILPEGWHNW GKKEAEKTVF YAEYDSRGEG ANPKARAAFS
RQLKNLKGYE METVLAGEDG WNPVKNGNRM VEVKR
//
