XGHA_ASPTU
ID XGHA_ASPTU Reviewed; 406 AA.
AC Q9UUZ2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Endo-xylogalacturonan hydrolase A;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=xghA;
OS Aspergillus tubingensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=5068;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10618200; DOI=10.1128/aem.66.1.36-41.2000;
RA van der Vlugt-Bergmans C.J., Meeuwsen P.J., Voragen A.G., van Ooyen A.J.;
RT "Endo-xylogalacturonan hydrolase, a novel pectinolytic enzyme.";
RL Appl. Environ. Microbiol. 66:36-41(2000).
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. {ECO:0000269|PubMed:10618200}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10618200}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
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DR EMBL; AJ249460; CAB65657.1; -; mRNA.
DR PDB; 4C2L; X-ray; 1.75 A; A=19-406.
DR PDBsum; 4C2L; -.
DR AlphaFoldDB; Q9UUZ2; -.
DR SMR; Q9UUZ2; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR CLAE; XGH28A_ASPTU; -.
DR VEuPathDB; FungiDB:ASPTUDRAFT_784660; -.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..406
FT /note="Endo-xylogalacturonan hydrolase A"
FT /id="PRO_0000394700"
FT REPEAT 183..213
FT /note="PbH1 1"
FT REPEAT 214..257
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 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:4C2L"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4C2L"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 183..194
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 213..225
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 237..249
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 264..278
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 297..321
FT /evidence="ECO:0007829|PDB:4C2L"
FT HELIX 326..331
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 337..350
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 357..362
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 367..376
FT /evidence="ECO:0007829|PDB:4C2L"
FT STRAND 386..391
FT /evidence="ECO:0007829|PDB:4C2L"
SQ SEQUENCE 406 AA; 42071 MW; 190707D20C9D995E CRC64;
MALYRNLYLL ASLGLSSAAP SKVQRAPDSS IHARAVCTPT AGGDSSTDDV PAITEALSSC
GNGGTIVFPE GSTYYLNSVL DLGSCSDCDI QVEGLLKFAS DTDYWSGRTA MISVSNVDGL
KLRSLTGSGV IDGNGQDAWD LFASDSSYSR PTLLYITGGS NLEISGLRQK NPPNVFNSVK
GGATNVVFSN LKMDANSKSD NPPKNTDGFD IGESTYVTIT EVTVVNDDDC VAFKPSSNYV
TVDTISCTGS HGISVGSLGK SSDDSVKNIY VTGATMINST KAAGIKTYPS GGDHGTSTVS
NVTFNDFTVD NSDYAFQIQS CYGEDDDYCE ENPGNAKLTD IVVSSFSGTT SDKYDPVVAN
LDCGADGTCG ISISGFDVKA PSGKSEVLCA NTPSDLGVTC TSGASG
