RGLB_EMENI
ID RGLB_EMENI Reviewed; 660 AA.
AC Q5AZ85; C8V0P1; Q1HFS3;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Rhamnogalacturonate lyase B;
DE EC=4.2.2.23;
DE Flags: Precursor;
GN Name=rglB; ORFNames=AN6395;
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 pectin lyase, polygalacturonase, pectin methylesterase and
CC rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone
CC of pectin. Active against linseed rhamnogalacturonan.
CC {ECO:0000269|PubMed:16844780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-
CC (1->4)-alpha-D-galactopyranosyluronic acid bonds of
CC rhamnogalacturonan I domains in ramified hairy regions of pectin
CC leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-
CC unsaturated D-galactopyranosyluronic acid at the non-reducing end.;
CC EC=4.2.2.23;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF69554.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA58417.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ490501; ABF50877.1; -; mRNA.
DR EMBL; AACD01000108; EAA58417.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001301; CBF69554.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_663999.1; XM_658907.1.
DR AlphaFoldDB; Q5AZ85; -.
DR SMR; Q5AZ85; -.
DR STRING; 227321.Q5AZ85; -.
DR CAZy; PL4; Polysaccharide Lyase Family 4.
DR CLAE; RGL4B_EMENI; -.
DR EnsemblFungi; EAA58417; EAA58417; AN6395.2.
DR GeneID; 2871281; -.
DR KEGG; ani:AN6395.2; -.
DR VEuPathDB; FungiDB:AN6395; -.
DR eggNOG; ENOG502QQM5; Eukaryota.
DR HOGENOM; CLU_016624_0_0_1; -.
DR InParanoid; Q5AZ85; -.
DR OrthoDB; 195455at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IDA:UniProtKB.
DR GO; GO:0102210; F:rhamnogalacturonan endolyase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
DR CDD; cd10316; RGL4_M; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR029413; RG-lyase_II.
DR InterPro; IPR029411; RG-lyase_III.
DR Pfam; PF14683; CBM-like; 1.
DR Pfam; PF14686; fn3_3; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW Lyase; Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..660
FT /note="Rhamnogalacturonate lyase B"
FT /id="PRO_0000394378"
FT REGION 446..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 660 AA; 73509 MW; D2629EAE80E2DAB6 CRC64;
MRLGVCFSLA AAASVARAAL TATENDTSIV LENDRLRATF DKGRGSIIDL YLDGQDFLGP
QSGSTGIGPY LDCYCTPSGF YTAGSTNPVT ELVQGTDSTG TKYAGIILND TYTPTGQEFQ
QYWFLRDGET GFHMFSRLAY YNETTPFLRN LQELRTLFRP NTDLWTHLTS SDLQTAPLPS
DEAIAEQIVV QDATWRLNNT PDDAYYQQFS EYFTKYTFSN HWRDNDVHGL YADGSTSDGT
TYGAWLVMNT KDTYYGGPLH SDLTVDGIIY NYIVSNHHGE GTPNITNGFD RTFGPQFYLF
NGGGSSSLEE LRDEARSLAS PSWNADFYDS IAKHVIGYVP SSQRGSVKGT IKLPKNAKSP
IAVLTVDGHY FQDNSAVPSS HQYWADIDKN GRFSIDRVVA GKYRLTVYAD GIFGDFTRDG
IVVKARKSTS IKETWKPESA GTEIWRLGTP DKSSGEFRHG AARDPTHPRH PPEYLIYWGA
YDWQSDFPGG IDYMIGESDP ATDFNTVHWA VFGPTPDNPV AESNTTHDWR IRFDLSAKQL
HARKTATLTI QLAGAKAASG NTDVYNASEP YANLPLRSYI NEQEEPLTMV IGYDQSSSCI
VRSAVSCYQV REKWEFPASW LKEGSNLLRL SLPTNGTNYE SAVLPTSVYV QYDALRLELK
