ID F6A9C2_PSEF1 Unreviewed; 608 AA.
AC F6A9C2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Exo-poly-alpha-galacturonosidase {ECO:0000313|EMBL:AEF23123.1};
DE EC=3.2.1.82 {ECO:0000313|EMBL:AEF23123.1};
GN OrderedLocusNames=Psefu_3160 {ECO:0000313|EMBL:AEF23123.1};
OS Pseudomonas fulva (strain 12-X).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF23123.1, ECO:0000313|Proteomes:UP000000686};
RN [1] {ECO:0000313|EMBL:AEF23123.1, ECO:0000313|Proteomes:UP000000686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA Woyke T.;
RT "Complete sequence of Pseudomonas fulva 12-X.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family.
CC {ECO:0000256|ARBA:ARBA00008834, ECO:0000256|RuleBase:RU361169}.
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DR EMBL; CP002727; AEF23123.1; -; Genomic_DNA.
DR RefSeq; WP_013792250.1; NC_015556.1.
DR AlphaFoldDB; F6A9C2; -.
DR STRING; 743720.Psefu_3160; -.
DR KEGG; pfv:Psefu_3160; -.
DR eggNOG; COG5434; Bacteria.
DR HOGENOM; CLU_016031_8_2_6; -.
DR OrthoDB; 9795222at2; -.
DR Proteomes; UP000000686; Chromosome.
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; 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; PF00295; Glyco_hydro_28; 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:UP000000686};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..608
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003337135"
FT DOMAIN 39..156
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 608 AA; 66511 MW; DA400B48CE52C885 CRC64;
MPLIKRLSTP VSLIKSHQSK CVVIPLALLT SGAALALEAP PNIQVPTLAY DDRQIILVWE
KPQDAAGIVD YHVYMDGKKL GGANANNDQH SPAKPYIDQF YAADEANFHH RIAIHNFTVD
GLKPETEYRF TVRSVDAEGR ESADSPVLVQ RTTAVPEVFN VEAQGAKGDG KTLNTAAIQK
TIDACSLNCK VLIPAGVFKT GALYLKSNMT LEIAEGATLL GSERSEDYPL QGYIQYPYST
MVRPASLINA LPRDPRQRQS FENIRIVGKG TIDGNGWKRN DDSQDELGKP LPFYRASDNT
RYREDGILAR DQVEKAVARG IIVKDAYGQM RSSLMTLRNV RNVFYGGFTV LNPAYHGIMN
LETENVVMAG TVHKTYDANN GDGIEFANSK GAMVFNNFFD TGDDCVNFAS GTGAGAAKQP
PQEDAWIFNN FFRRGHGMVV AGSHTGGWIQ NILAEDNVSD GTDTGLRMKS TNFMGGGARN
VTFRDSAIRN PVKQGVIMTL DYHDPNAILD YERSTVPGQF RDIRVSNVTV EGAAGAAIQV
KGDSAHDAFH ENVAFEQVRF KGGAGAQIDG LRDSSFTDVS FVDTQGEAWN IKGSEGLRFD
RVEPQPKR
//
