XGHA_ASPNC
ID XGHA_ASPNC Reviewed; 406 AA.
AC A2QK83; Q27UA4;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Probable endo-xylogalacturonan hydrolase A;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=xghA; ORFNames=An04g09700;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16822232; DOI=10.1042/bj20060703;
RA Martens-Uzunova E.S., Zandleven J.S., Benen J.A., Awad H., Kools H.J.,
RA Beldman G., Voragen A.G., Van den Berg J.A., Schaap P.J.;
RT "A new group of exo-acting family 28 glycoside hydrolases of Aspergillus
RT niger that are involved in pectin degradation.";
RL Biochem. J. 400:43-52(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Pectinolytic enzyme involved in the degradation of
CC xylogalacturonan (xga), a galacturonan backbone heavily substituted
CC with xylose, and which is one important component of the hairy regions
CC of pectin. Activity requires a galacturonic acid backbone substituted
CC with xylose (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; DQ374431; ABD61571.1; -; Genomic_DNA.
DR EMBL; AM270096; CAK47977.1; -; Genomic_DNA.
DR RefSeq; XP_001402326.1; XM_001402289.1.
DR AlphaFoldDB; A2QK83; -.
DR SMR; A2QK83; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR PaxDb; A2QK83; -.
DR EnsemblFungi; CAK47977; CAK47977; An04g09700.
DR GeneID; 4991373; -.
DR KEGG; ang:ANI_1_1444184; -.
DR VEuPathDB; FungiDB:An04g09700; -.
DR HOGENOM; CLU_016031_1_3_1; -.
DR Proteomes; UP000006706; Chromosome 6L.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProt.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SMART; SM00710; PbH1; 5.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..406
FT /note="Probable endo-xylogalacturonan hydrolase A"
FT /id="PRO_5000219960"
FT REPEAT 183..213
FT /note="PbH1 1"
FT REPEAT 214..235
FT /note="PbH1 2"
FT REPEAT 266..289
FT /note="PbH1 3"
FT REPEAT 299..320
FT /note="PbH1 4"
FT REPEAT 333..375
FT /note="PbH1 5"
FT ACT_SITE 228
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 251
FT /evidence="ECO:0000250"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 406 AA; 42123 MW; A01FF5293770589E CRC64;
MTLYRNLLLL ASLGLSYAAP SKVQRAPDSS LHARAVCTPT AGGDSSTDDV PAITEALSSC
GNGGTIVFPE GSTYYLNSVL DLGNCSNCDI QVEGLLKFAS DTDYWSGRTA MISVSDVDGL
KLRSLTGSGV IDGNGQDAWD LFASDSSYSR PTLLYITGGS NLEISGLRQK NPPNVFNSVK
GGATNVVFSN LKMDANSKSD NPPKNTDGFD IGESTYVTIT EVTVVNDDDC VALKPSSNYV
TVDTISCTGS HGISVGSLGK SSDDSVKNIY VTGATMINST KAAGIKTYPS GGDHGTSTVS
NVTFTDFTVD NSDYAFQIQS CYGEDDDYCE ENPGNAKLTD IVVSSFSGTT SDKYDPVVAN
IDCGSDGTCG ISISGFDVKA PSGKSEVLCA NTPSDLGVTC TSGASG
