ID A0A368W459_9BACL Unreviewed; 1071 AA.
AC A0A368W459;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=galacturonan 1,4-alpha-galacturonidase {ECO:0000256|ARBA:ARBA00038933};
DE EC=3.2.1.67 {ECO:0000256|ARBA:ARBA00038933};
GN ORFNames=DFP97_108132 {ECO:0000313|EMBL:RCW47517.1};
OS Paenibacillus prosopidis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=630520 {ECO:0000313|EMBL:RCW47517.1, ECO:0000313|Proteomes:UP000252415};
RN [1] {ECO:0000313|EMBL:RCW47517.1, ECO:0000313|Proteomes:UP000252415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7506 {ECO:0000313|EMBL:RCW47517.1,
RC ECO:0000313|Proteomes:UP000252415};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-
CC galacturonosyl](n-1) + alpha-D-galacturonate; Xref=Rhea:RHEA:14117,
CC Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14572, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58658, ChEBI:CHEBI:140523; EC=3.2.1.67;
CC Evidence={ECO:0000256|ARBA:ARBA00036499};
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family.
CC {ECO:0000256|ARBA:ARBA00009646}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family.
CC {ECO:0000256|ARBA:ARBA00008834, ECO:0000256|RuleBase:RU361169}.
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:RCW47517.1}.
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DR EMBL; QPJD01000008; RCW47517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368W459; -.
DR OrthoDB; 833750at2; -.
DR Proteomes; UP000252415; Unassembled WGS sequence.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.20.10; Crystallins; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR001064; Beta/gamma_crystallin.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR011024; G_crystallin-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR31736; -; 1.
DR PANTHER; PTHR31736:SF14; EXOPOLYGALACTURONASE X-1-RELATED; 1.
DR Pfam; PF00030; Crystall; 1.
DR Pfam; PF00754; F5_F8_type_C; 3.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SMART; SM00231; FA58C; 3.
DR SMART; SM00247; XTALbg; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR SUPFAM; SSF49695; gamma-Crystallin-like; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 2.
DR PROSITE; PS50022; FA58C_3; 3.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361169};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361169};
KW Reference proteome {ECO:0000313|Proteomes:UP000252415};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1071
FT /note="galacturonan 1,4-alpha-galacturonidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039368815"
FT DOMAIN 488..610
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 628..763
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 788..895
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 897..941
FT /note="Beta/gamma crystallin 'Greek key'"
FT /evidence="ECO:0000259|PROSITE:PS50915"
FT DOMAIN 983..1027
FT /note="Beta/gamma crystallin 'Greek key'"
FT /evidence="ECO:0000259|PROSITE:PS50915"
FT REGION 508..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 114205 MW; 7DD96C97F31F648A CRC64;
MFVNRGKKRS KALSILIVFS MIVSFFPVAL SNPTTVEAAT TLNVYPAPSG VTMNTTYTVQ
VQAPGGPWQS LDVYQTTVNG YTSSKTSFAY FDTDGPVNVS VTSNIGSIST AVIRPAAHGI
TPAINGNTMT FSMSGPMNIS VEVNGDHNNT LDLFANPVDP NPPSPTDPNV IYVGPGLYTQ
NYVVPSGKTL YIAGGAVIIG GITVNNATNA KVLGRGVILN APFRAIEVDH SNQITIDGII
VNDYGASNNG GYAINIGNST NVSVNNFKAY SFKRWTDGID IFASSYVAIN NYFARTGDDA
IAIYGARNFG GNLYSGNTAH ISVTNSFLQP DVAHPINVGT HGDPTKPGGG ETIEDLNFSN
ITIWQKNGSK YTSLTASDGL LVNKVRFTDI TIEDENQGRF IEVLTFKNNG FGLAFGRGVN
DVHVKNMSYT GSNSGTNNIY GKFVNQLTQN VTFENLKVNG NVVLSASAGN FAIGSYAQNI
NFIASGGTVP APTAIPFTTP VDIARGKTAT ADSTQSGKPA SSGNDGNTTT RWCANDGSTG
HWWTVDLGSP MNITGGTQVM WELNNTAYKY KIETSVDNVN WTLKVDKTNN TDTNQVQNDV
FQGTARYVRI TVTGLQSNVW ASFYDFKVFG DPTNLALGKI VTADSSKSGN PAVNGIDSNP
ATLWSANDGN IGHWLTMDLG NAKKITNGTQ VAWAQSGAAY QYKIETSIDN TNWTLKVDKT
GNADTSQVQN DYFTGTARYV RITVTGLPSG AWASFYDFKV FGEPTNLTLG KTATADSSQS
GNPASNGNDG DTSTSWIAAD TNGGHSWVVD LGSMMNITGG TQVKWPQSGV QYKYTISTSP
DNINWTMRLE KTSNNNITQV QNDYFTGTTR YVKITVTGVP SGYSAGIADF KVFGTINGPT
FYEHYNYEGK AVTLDLGNYT LAQMQAAGIA NDSISSIHVP LEYTVVAYNG DGFSGTSWTI
TSDNPAMGTG NNDMISSIKV MSAGPTFYEH YNYGGKAVTL RPGQYTLAQM QAAGIADNGI
SSIRVPAEYT VVAYSDDGFS GTSWTITSDN PAMGDTGNND MISSVIITSN Q
//