RHGA_EMENI
ID RHGA_EMENI Reviewed; 507 AA.
AC Q5ARE6; C8VK67; Q1HFQ2;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Rhamnogalacturonase A;
DE Short=RGase A;
DE Short=RHG A;
DE EC=3.2.1.171;
DE Flags: Precursor;
GN Name=rhgA; ORFNames=AN9134;
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 [MRNA], AND FUNCTION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT "Development and application of a suite of polysaccharide-degrading enzymes
RT for analyzing plant cell walls.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
RN [2]
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 [3]
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 enzymes consist of four classes of enzymes:
CC pectine lyase, polygalacturonase, pectin methylesterase and
CC rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl-(1,2)-
CC alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions
CC of pectins. Active against linseed rhamnogalacturonan.
CC {ECO:0000269|PubMed:16844780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of alpha-D-GalA-(1->2)-alpha-L-Rha glycosidic
CC bond in the rhamnogalacturonan I backbone with initial inversion of
CC anomeric configuration releasing oligosaccharides with beta-D-GalA at
CC the reducing end.; EC=3.2.1.171;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF82482.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA61967.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ490522; ABF50898.1; -; mRNA.
DR EMBL; AACD01000169; EAA61967.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001306; CBF82482.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_682403.1; XM_677311.1.
DR AlphaFoldDB; Q5ARE6; -.
DR SMR; Q5ARE6; -.
DR STRING; 227321.Q5ARE6; -.
DR CAZy; GH28; Glycoside Hydrolase Family 28.
DR EnsemblFungi; EAA61967; EAA61967; AN9134.2.
DR GeneID; 2867999; -.
DR KEGG; ani:AN9134.2; -.
DR VEuPathDB; FungiDB:AN9134; -.
DR eggNOG; ENOG502R2FT; Eukaryota.
DR HOGENOM; CLU_016031_7_2_1; -.
DR InParanoid; Q5ARE6; -.
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:0046576; F:rhamnogalacturonan alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronide lyase activity; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR Pfam; PF12708; Pectate_lyase_3; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..507
FT /note="Rhamnogalacturonase A"
FT /id="PRO_0000394385"
FT REGION 462..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..507
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 290
FT /evidence="ECO:0000250"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..64
FT /evidence="ECO:0000250"
FT DISULFID 217..234
FT /evidence="ECO:0000250"
FT DISULFID 340..346
FT /evidence="ECO:0000250"
FT DISULFID 368..377
FT /evidence="ECO:0000250"
SQ SEQUENCE 507 AA; 53449 MW; AE6347D789F560C1 CRC64;
MYVSRLLLFL APLLVKGQLS GSVGPLTSVS SKSQTKTCNV LDYGAVADKS TDIGPALSSA
WDECADGGVV YIPPGDYAIE TWVKLSGGKA CAIQLDGIIY RTGTDGGNMI MIEHTSDFEF
FSSTSKGAFQ GYGYEFHAKG SSDGPRILRL YDVSDFSVHD VALVDSPLFH FSMDTCSNGE
VYNMAIRGGN MGGLDGIDVW STNVWIHDVE VTNKDECVTV KSPSKNILVE NIYCNWSGGC
AMGSLGTDTD ISDIVYRNVY TWKSNQMYMV KSNGGSGTVS NLVLENFIGH GNAYSLDIDS
AWSSMSTIEG DGVELKNVTI RNWKGTEADG SQRGPIKVKC ASGAPCTDVT VEDFAMWTES
GDEQTYVCEN AFGDGFCLAD GDGTSTFTTT LTASAAPSGY SAPSMDADLE TAFGTDSEIP
IPTIPTSFYP GATPYSALAG ASVSSSQVPA ASSSAEAKFV ASPATSSPTA TSTAISSVDP
VSAATTTATS HGHGKSHHKH QCRAHRH
