ID A0A084A302_9GAMM Unreviewed; 691 AA.
AC A0A084A302;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Exo-poly-alpha-D-galacturonosidase {ECO:0000313|EMBL:KEY59681.1};
DE EC=3.2.1.82 {ECO:0000313|EMBL:KEY59681.1};
GN Name=pehX {ECO:0000313|EMBL:KEY59681.1};
GN ORFNames=SRDD_14010 {ECO:0000313|EMBL:KEY59681.1};
OS Serratia sp. DD3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY59681.1, ECO:0000313|Proteomes:UP000017810};
RN [1] {ECO:0000313|EMBL:KEY59681.1, ECO:0000313|Proteomes:UP000017810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD3 {ECO:0000313|EMBL:KEY59681.1,
RC ECO:0000313|Proteomes:UP000017810};
RX PubMed=25212623;
RA Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT of Daphnia magna.";
RL Genome Announc. 2:e00903-14(2014).
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:KEY59681.1}.
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DR EMBL; AYKS02000042; KEY59681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084A302; -.
DR STRING; 1410619.SRDD_14010; -.
DR eggNOG; COG5434; Bacteria.
DR Proteomes; UP000017810; Unassembled WGS sequence.
DR GO; GO:0033917; F:exo-poly-alpha-galacturonosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd00063; FN3; 1.
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; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR31339; PECTIN LYASE-RELATED; 1.
DR PANTHER; PTHR31339:SF9; PLASMIN AND FIBRONECTIN-BINDING PROTEIN A; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR Pfam; PF12708; Pectate_lyase_3; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS50853; FN3; 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:UP000017810};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..691
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001770594"
FT DOMAIN 76..193
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 33..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 75261 MW; C802327B00343DF7 CRC64;
MSGFLFSRRI ACCLPLVFSV LVSGCDNGSS SNMNSNANSN ENSNSNSNSS ENSNENSNSN
SNENSNSDSP VDRSAAPQNV RIPPLAYDEH SVVLVWNKPQ QYNNISDYNV YMNGKLLGGT
KANHDAYSPA KPYIDSFYQN RDPNQWHSKI SLHNFTVQNL TPETTYQFTV RAVYADGTES
VESLPLAFTT PTAPQVVNIQ NYGAVGDGTT LDTAAIQKAI DSCTIELYPQ GCKVLIPPGT
FKTGALFLHS DMTLEITANA TLLGSASPDD YPLEKGYYLY PYQLPAPLPK RPPSLINALK
PNDTGSAHAG TFKNIRIVGQ GTIDGNGWVR GIKAGGPENL TDETGNTLPQ YRASNVNKVN
TDGILAAAQT AQGIADGLPA STAYSNRRSS LITLRGVENL YIGQLTILNP AYHGIMMLEN
ENIAINGIIN KTYDANNADG LEFGNSQNAM VFNSFFDTGD DCVNFAAGFG AGVEEYHQPP
QSGTWIFNNY FRNGHGAVVA GSHTGAWIEN ILAEDNVMYL TDVGLRMKSR PYYGGGARNV
VFRDNAMSSL GKQPFIFTIK YASDVNDAVP ASEPAQFRDV QVQNISIDGG TQNSILVDGM
TVAEMEAAYG FTFPRDAYHQ NLHFENVRFN HAIATNISFL HNSQFDNVTY LDTQKAWSFS
YIQDVLLHDS VNNITLTTQA DEVLTYEAAT N
//
