ID A0A0A2KI50_PENIT Unreviewed; 633 AA.
AC A0A0A2KI50;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 B {ECO:0000256|ARBA:ARBA00041473};
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase B {ECO:0000256|ARBA:ARBA00042261};
GN ORFNames=PITC_009380 {ECO:0000313|EMBL:KGO67487.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO67487.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO67487.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO67487.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- FUNCTION: Specific in hydrolyzing the terminal glycosidic bond of
CC polygalacturonic acid and oligogalacturonates.
CC {ECO:0000256|ARBA:ARBA00037312}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:KGO67487.1}.
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; JQGA01001283; KGO67487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KI50; -.
DR STRING; 40296.A0A0A2KI50; -.
DR HOGENOM; CLU_016031_1_0_1; -.
DR OrthoDB; 922122at2759; -.
DR PhylomeDB; A0A0A2KI50; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.550; Membrane associated eicosanoid/glutathione metabolism-like domain; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR023352; MAPEG-like_dom_sf.
DR InterPro; IPR001129; Membr-assoc_MAPEG.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR31736; -; 1.
DR PANTHER; PTHR31736:SF6; EXOPOLYGALACTURONASE B-RELATED; 1.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR Pfam; PF01124; MAPEG; 1.
DR SUPFAM; SSF161084; MAPEG domain-like; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361169};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361169};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ SEQUENCE 633 AA; 69267 MW; CF6FA05451C8D4B1 CRC64;
MSALLTTLGL RAAPGQTAGN HASALLMVNW FFAYILTSPR GAKMRLGIDH NVNPRDDLAT
YGEAAVQSGK ITRGTLDKLK RQTSAHANVQ EGFTLFVAAI LMSLYAGLPN ETINTVGIWY
SISRVAYHIL YCNIETRSLS LLRSAAWWSG NISCLYALVQ ASKKLYCHWV RDDSRDTFLV
NDQATAASID FIDLTKMKFL AIGALFLSTV GALATEHIIE GAQIIPASDE AALKKIGAHG
HHKYHDRRTV IIRSSKSDTD DVSDDFLWGI KAANHGGRLL LQKGKTYVIG KKLDLSFLDN
IEVQLEGEVK FTDDIDYWQA NNFYYSFQKS ITFWVWGGQD IKIFGKGTLN GNGQEWYNAF
AGLEVLDPDN TFYRPILFLT DNATRVSVEG ITQLNSPCWT NFFVRTKDIS FDDVFINAFS
TNASALPKNT DGFDSLNVDG LSVTNTRVDI GDDCFSPKPN TTNIFVQNLL CNNTHGVSMG
SIGQYSGIED IIENAWIENL TLLNGQNGVR LKAWAGPDIG FGRINNITYK DVHIENTDAP
IVLDQCYFNL NATTCAKFPS SVNFTNINFE NVHGTSSGKN GKVIGDLTCS PNAVCSGIKL
SDINITSPAG GPPIVICDGI DGDIGVECQS SSA
//
