ID A0A0K9XZ23_9FLAO Unreviewed; 339 AA.
AC A0A0K9XZ23;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN ORFNames=AC804_10215 {ECO:0000313|EMBL:KNB61681.1};
OS Chryseobacterium sp. Hurlbut01.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1681828 {ECO:0000313|EMBL:KNB61681.1, ECO:0000313|Proteomes:UP000036769};
RN [1] {ECO:0000313|Proteomes:UP000036769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hurlbut01 {ECO:0000313|Proteomes:UP000036769};
RA Couger M.B., Youseff N., Elshahed M., French D., Hoff W.;
RT "Draft Genome Sequence of the Environmental Isolate Chryseobacterium sp.
RT Hurlbut 01.";
RL Submitted (JUL-2015) 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 -!- 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:KNB61681.1}.
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; LGIP01000019; KNB61681.1; -; Genomic_DNA.
DR RefSeq; WP_050379237.1; NZ_LGIP01000019.1.
DR AlphaFoldDB; A0A0K9XZ23; -.
DR PATRIC; fig|1681828.3.peg.1183; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000036769; Unassembled WGS sequence.
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 Signal {ECO:0000256|RuleBase:RU000589}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT CHAIN 18..339
FT /note="Pectinesterase"
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT /id="PRO_5005394048"
FT DOMAIN 33..329
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT ACT_SITE 196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 339 AA; 38068 MW; DF172C10036BCFE2 CRC64;
MKFFTFLKNL KSFSVLSIVL LSLLSFRTKD QLIVVSKDGK GNFTTVQQAI DAVENGSSVR
TKILIKAGTY KEKIIIPENK GAILLEGENP ENTIITYDDF ASKKNSDGKD IGTTNSSTIF
IYSDNFSAKN ISFENSSGRV GQAVAVLTSG DRITFENCRF LGNQDTLYLK GVQDSPDKSR
PSRNYFKNCY IEGTTDYIFG AGTAVFENCV IYSKETASYV TAASTPQQNE FGFVFINSKI
LGNAEENSVY LGRPWRPFAK TVFIDCEINS TIKPEGWHNW SKPDAEKTTF YGEYNSKGNG
ANIFKRVFWS HQLTKEESKK YTAKNILSGK DNWNFRKIK
//
