ID A0A067HGX1_CITSI Unreviewed; 230 AA.
AC A0A067HGX1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
DE Flags: Fragment;
GN ORFNames=CISIN_1g0440421mg {ECO:0000313|EMBL:KDO87166.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO87166.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO87166.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) 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|ARBA:ARBA00005184,
CC ECO:0000256|RuleBase:RU000589}.
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DR EMBL; KK784873; KDO87166.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067HGX1; -.
DR STRING; 2711.A0A067HGX1; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
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; PTHR31707; PECTINESTERASE; 1.
DR PANTHER; PTHR31707:SF188; PECTINESTERASE_PECTINESTERASE INHIBITOR 7-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 4: Predicted;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085,
KW ECO:0000256|RuleBase:RU000589}; Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120}.
FT DOMAIN 2..214
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT ACT_SITE 67
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KDO87166.1"
SQ SEQUENCE 230 AA; 25601 MW; A0B6482758FC42D2 CRC64;
VMAPNFVAVD ISFRNTAGPS KHQAVALRSG ADLSTFYSCS FEGYQDSLYT HSQRQFYREC
DIYGTIDFIF GNAAVVLQNC NIYLRLPMSG QYNVITAQGR TDPNQNTGIS IHNCTFRAAD
ELALSNQTVQ TYLGRPWKEY SRTVIMQSFM DSLINPSGWQ IWTGDFALST LYYAEYDNRG
PGSNSANRVT WPGYHVINAT DAANFTVSNF LLGDVWLPQT GVPYTGGLIS
//
