ID A0A2S4YD58_9ACTN Unreviewed; 594 AA.
AC A0A2S4YD58;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=galacturonan 1,4-alpha-galacturonidase {ECO:0000256|ARBA:ARBA00038933};
DE EC=3.2.1.67 {ECO:0000256|ARBA:ARBA00038933};
DE AltName: Full=Galacturan 1,4-alpha-galacturonidase {ECO:0000256|ARBA:ARBA00043142};
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase {ECO:0000256|ARBA:ARBA00041604};
GN ORFNames=C3488_25405 {ECO:0000313|EMBL:POX46802.1};
OS Streptomyces sp. Ru72.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2080747 {ECO:0000313|EMBL:POX46802.1, ECO:0000313|Proteomes:UP000237426};
RN [1] {ECO:0000313|EMBL:POX46802.1, ECO:0000313|Proteomes:UP000237426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru72 {ECO:0000313|EMBL:POX46802.1,
RC ECO:0000313|Proteomes:UP000237426};
RA Suneja G., Sharma R.;
RT "Genome sequencing of cellulose degrading bacteria.";
RL Submitted (FEB-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 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:POX46802.1}.
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DR EMBL; PQSR01000062; POX46802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4YD58; -.
DR OrthoDB; 9795222at2; -.
DR Proteomes; UP000237426; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR31736; -; 1.
DR PANTHER; PTHR31736:SF14; EXOPOLYGALACTURONASE X-1-RELATED; 1.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR Pfam; PF05345; He_PIG; 1.
DR SMART; SM00710; PbH1; 6.
DR SUPFAM; SSF49313; Cadherin-like; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51318; TAT; 1.
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:UP000237426};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..594
FT /note="galacturonan 1,4-alpha-galacturonidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015409915"
SQ SEQUENCE 594 AA; 64038 MW; D6BA8BE90EDDF24B CRC64;
MNDTQGTGMT RRTVLQAAGA AAAAYSLVGA AAATARADDT PASTDKLVVY PIPSGVPTNL
SYSVKARTPG GDWQTVPVYR ARAKQIDANT GSGPVFNSSV AMFDFQGTVE VAVTSAKGTI
GTARIRPLSY GTQFTVDGAT IGFTLTEPRN LSIEVDGDIF NNLQLHANPI ETNVPDPDDE
DVLYFGPGLH KTTNNVLTVP SGKTVYLAGG AVLTSQVAFQ NVENARLRGR GVLYNSPSGV
LVEYSKNIEI DGVTVLNPSS GYAITVGQSQ QVTIHNFHAY SHGQWGDGID IFCSQDVLID
NVWMRNADDC IAIYAHRWNY YGDCRNITVR NSTLWADVAH PINVGTHGNT DNPETLENLV
FSNIDILDHR EPQMNYQGCI ALNPGDSNLV SNVRAQDIRV EDFRWGQLLN MRVMFNTTYN
TSVGRGIDGV YIKNLSYNGT HANPAILVGY DADHAIKNVT FQNLVINGKF IGNGMRKPGW
YTFWDMMPGY ANEHVINTRF LNSTDATSTN APQITSPDQA AGTKNQVFNY LITASELPTS
FSAAGLPKGL DIDTGTGLIS GVMRDNVGSF DVTVSATNSV GTATRTVTLT VQHP
//