RHA1_EMENI
ID RHA1_EMENI Reviewed; 245 AA.
AC Q5BAA2; C8VPL0; Q1HFU5;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Rhamnogalacturonan acetylesterase {ECO:0000303|PubMed:16844780};
DE Short=RGAE;
DE EC=3.1.1.86 {ECO:0000269|PubMed:16844780};
DE Flags: Precursor;
GN ORFNames=AN2528;
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).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [4]
RP FUNCTION.
RX PubMed=22589326; DOI=10.1093/aob/mcs103;
RA Fursova O., Pogorelko G., Zabotina O.A.;
RT "An efficient method for transient gene expression in monocots applied to
RT modify the Brachypodium distachyon cell wall.";
RL Ann. Bot. 110:47-56(2012).
CC -!- FUNCTION: Plays a key role in the degradation of rhamnogalacturonan in
CC the cell wall. Involved in degradation of pectin.
CC {ECO:0000269|PubMed:16844780, ECO:0000269|PubMed:22589326}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolytic cleavage of 2-O-acetyl- or 3-O-acetyl groups of
CC alpha-D-galacturonic acid in rhamnogalacturonan I.; EC=3.1.1.86;
CC Evidence={ECO:0000269|PubMed:16844780};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22589326}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; BN001307; CBF87034.1; -; Genomic_DNA.
DR EMBL; AACD01000043; EAA64633.1; -; Genomic_DNA.
DR RefSeq; XP_660132.1; XM_655040.1.
DR AlphaFoldDB; Q5BAA2; -.
DR SMR; Q5BAA2; -.
DR STRING; 162425.CADANIAP00009256; -.
DR CLAE; RAE12A_EMENI; -.
DR EnsemblFungi; CBF87034; CBF87034; ANIA_02528.
DR EnsemblFungi; EAA64633; EAA64633; AN2528.2.
DR GeneID; 2874587; -.
DR KEGG; ani:AN2528.2; -.
DR VEuPathDB; FungiDB:AN2528; -.
DR eggNOG; ENOG502RY37; Eukaryota.
DR HOGENOM; CLU_065859_0_0_1; -.
DR InParanoid; Q5BAA2; -.
DR OMA; QMGHNDA; -.
DR OrthoDB; 1234283at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
DR GO; GO:0046575; F:rhamnogalacturonan acetylesterase activity; IDA:UniProtKB.
DR GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR Pfam; PF00657; Lipase_GDSL; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..245
FT /note="Rhamnogalacturonan acetylesterase"
FT /id="PRO_0000432721"
FT ACT_SITE 26
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q00017"
FT ACT_SITE 204
FT /evidence="ECO:0000250|UniProtKB:Q00017"
FT ACT_SITE 207
FT /evidence="ECO:0000250|UniProtKB:Q00017"
FT DISULFID 100..108
FT /evidence="ECO:0000250|UniProtKB:Q00017"
FT DISULFID 226..244
FT /evidence="ECO:0000250|UniProtKB:Q00017"
SQ SEQUENCE 245 AA; 25870 MW; E0D993BAC02EBACD CRC64;
MKSIALTSLS LLPSALAQTI YLAGDSTMAS STPGWGDYIA DSVSVEISNQ AIGGRSARSY
TREGRFQAIA DVLQAGDYVV IEFGHNDGGS LSNDNGRTDC PGDGDETCET VYNGVAETVL
TFPAYIENAA LLFLEKGANV LISSQTPNNP WESGTFSYTP NRFVGYAELA AQRAGVDYVD
HGAYTASIFE ALGADTVNSF YPNDHTHTNA EGSSVVADAF LKAVVCSGVA LNDVLTRTDF
DGECL
