XGHA_EMENI
ID XGHA_EMENI Reviewed; 399 AA.
AC Q5B7U1; C8VHN3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Probable endo-xylogalacturonan hydrolase A;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=xghA; ORFNames=AN3389;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000055; EAA63357.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF82806.1; -; Genomic_DNA.
DR RefSeq; XP_660993.1; XM_655901.1.
DR AlphaFoldDB; Q5B7U1; -.
DR SMR; Q5B7U1; -.
DR STRING; 162425.CADANIAP00009651; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR EnsemblFungi; CBF82806; CBF82806; ANIA_03389.
DR EnsemblFungi; EAA63357; EAA63357; AN3389.2.
DR GeneID; 2874071; -.
DR KEGG; ani:AN3389.2; -.
DR eggNOG; ENOG502QTHU; Eukaryota.
DR HOGENOM; CLU_016031_1_3_1; -.
DR InParanoid; Q5B7U1; -.
DR OMA; FKPGANY; -.
DR OrthoDB; 1028572at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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.
DR PROSITE; PS00502; POLYGALACTURONASE; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..399
FT /note="Probable endo-xylogalacturonan hydrolase A"
FT /id="PRO_0000394701"
FT REPEAT 177..207
FT /note="PbH1 1"
FT REPEAT 208..229
FT /note="PbH1 2"
FT REPEAT 231..251
FT /note="PbH1 3"
FT REPEAT 260..283
FT /note="PbH1 4"
FT REPEAT 293..314
FT /note="PbH1 5"
FT ACT_SITE 222
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT ACT_SITE 245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10052"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 399 AA; 41897 MW; 256D544A03F56CF5 CRC64;
MTFGKAAFLS FSLFGASWAG PSRTLQARAV CTPKAGGSSS IDDVPAIVKS ISACGDGGTI
VFPEDSTYYL NSVLDLAGCS GCELQVEGLL KFASDTDYWN GRTAMINVKN IDGLTIRSLT
GSGVIDGNGQ NAYDRFAEDS SYDRPTPLYI TGGGDIKVSN FRLKNAPNVF VSVKGGTTNA
VFSDMRLDAT SKSENLPKNT DGFDIGESTY VTISGTTVSN NDDCVAFKPG CNYLTVTDIT
CTGSHGLSVG SLGKSSDDIV QNVRVEGATM ISSTKAAGIK TYPSGGDHGL STVTNVTWKD
ITIQNCDYAI QIQSCYGEDE EYCETNPGDA VFSGIAFEGF SGTTSSKYDP VTGNLNCGED
GKCDVSVVDY SVKAPSGGAA ENLTVTTYKN RCLCQARSV
