ID F2RHF9_STRVP Unreviewed; 379 AA.
AC F2RHF9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-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 OrderedLocusNames=SVEN_6617 {ECO:0000313|EMBL:CCA59903.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA59903.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA59903.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA59903.1};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
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; FR845719; CCA59903.1; -; Genomic_DNA.
DR RefSeq; WP_015037798.1; NZ_JABVZO010000329.1.
DR AlphaFoldDB; F2RHF9; -.
DR STRING; 953739.SVEN_6617; -.
DR GeneID; 69868619; -.
DR KEGG; sve:SVEN_6617; -.
DR PATRIC; fig|953739.5.peg.1833; -.
DR eggNOG; COG4677; Bacteria.
DR HOGENOM; CLU_012243_3_1_11; -.
DR OrthoDB; 112037at2; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000006854; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 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:UP000006854};
KW Signal {ECO:0000256|RuleBase:RU000589}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT CHAIN 36..379
FT /note="Pectinesterase"
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT /id="PRO_5005129300"
FT DOMAIN 61..345
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT REGION 335..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 224
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 379 AA; 39996 MW; F8B671508F43737D CRC64;
MPSHPTGAVP GRRSLLLGAA GAALALALPA APASAASPSP ARPFGRFGSP ARRLTERTLY
VHQGGLGDHT TVQAAVTAAG GTGWTLVLAP GTYRETVSVT SARTDMTWIG ASGDPRDVVV
VYANAAGTPR PEGGTHGTTG SATTTVQAAG FTAHAVSFAN DFLRTDLPGN PGTQAVALKV
QGDRSAFFHC RFLGHQDTLY ADSMALSAFA RQYFAHCYVE GDVDFVFGRA TAVFEHCHFR
TLLRPDLAAA PHGFVFAPST ARENPYGFLA VRCRVTSEAP DGFYKLARPW VPGSDLTARP
SLVVRESVLG PGIDAVAPYA NMRDAHPWQA QRFAEHHNSG PGARITVPEN RPQLGPTEAA
STTRSTYLGN WNPVPTRPS
//
