RGXC_NEOFI
ID RGXC_NEOFI Reviewed; 423 AA.
AC A1D415;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Putative galacturan 1,4-alpha-galacturonidase C;
DE EC=3.2.1.67;
DE AltName: Full=Exopolygalacturonase C;
DE AltName: Full=Exorhamnogalacturonase C;
DE AltName: Full=Poly(1,4-alpha-D-galacturonide)galacturonohydrolase C;
DE Flags: Precursor;
GN Name=rgxC; ORFNames=NFIA_018590;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: Specific in hydrolyzing the terminal glycosidic bond of
CC polygalacturonic acid and oligogalacturonates. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; DS027688; EAW23158.1; -; Genomic_DNA.
DR RefSeq; XP_001265055.1; XM_001265054.1.
DR AlphaFoldDB; A1D415; -.
DR SMR; A1D415; -.
DR STRING; 36630.CADNFIAP00001969; -.
DR EnsemblFungi; EAW23158; EAW23158; NFIA_018590.
DR GeneID; 4591724; -.
DR KEGG; nfi:NFIA_018590; -.
DR VEuPathDB; FungiDB:NFIA_018590; -.
DR eggNOG; ENOG502QVQ1; Eukaryota.
DR HOGENOM; CLU_016031_1_1_1; -.
DR OMA; YNEDMHN; -.
DR OrthoDB; 1028572at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..423
FT /note="Putative galacturan 1,4-alpha-galacturonidase C"
FT /id="PRO_0000395081"
FT ACT_SITE 229
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT ACT_SITE 252
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 231..248
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 379..385
FT /evidence="ECO:0000250|UniProtKB:O74213"
FT DISULFID 409..423
FT /evidence="ECO:0000250|UniProtKB:O74213"
SQ SEQUENCE 423 AA; 46251 MW; 4AE6D514B77780B8 CRC64;
MRFSIISLVS LPLFLGLTYA GGVEKDERNN VCTVKANGKQ KDDMPNLFKA FKECGNGGTI
IFPEDQSYWI GTRLNPLLND VTVQWRGKWT FSDNLDYRRN NSFPVAFQNH RVGFIISGHN
VTIDGNGNTW YTAEKGVTQS GRPMPFVFWN VSEVNVENFY VKDPPLWSLN IMNGTNMRFN
NIYCNATSVD APYGYNWVQN TDGFGSFSAV NTMDAVNIQL TNFVYQGGDD CITIKPRSYN
IDIQNVTCVG GNGIAVGSLG QYLEDSSVEN VRVDKVKIIR YNEDMHNSAY IKTWVGALVP
QSSYESAGLP CGGGWGNVRN ILFSNFEVQG ANAGPSVNQD SGNNGSYSGS SLMTVSNIVF
ANFTGYTSGG TSVTSKVSCS EVHPCYNIEF DDVLLYPGKN ASNLGTGSCK YTANGGVHGL
EGC
