GANA_EMENI
ID GANA_EMENI Reviewed; 350 AA.
AC Q5B153; C8VFL3; Q1HFS6;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Arabinogalactan endo-beta-1,4-galactanase A;
DE EC=3.2.1.89;
DE AltName: Full=Endo-1,4-beta-galactanase A;
DE Short=Galactanase A;
DE Flags: Precursor;
GN Name=galA; ORFNames=AN5727;
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], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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: Endogalactanase involved in the degradation of plant cell
CC wall polysaccharides, and more particularly of hairy regions of pectin.
CC {ECO:0000269|PubMed:16844780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic
CC linkages in type I arabinogalactans.; EC=3.2.1.89;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:16844780};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 53 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF81324.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA62820.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ490498; ABF50874.1; -; mRNA.
DR EMBL; AACD01000098; EAA62820.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001305; CBF81324.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_663331.1; XM_658239.1.
DR PDB; 4BF7; X-ray; 2.00 A; A=1-350.
DR PDBsum; 4BF7; -.
DR AlphaFoldDB; Q5B153; -.
DR SMR; Q5B153; -.
DR STRING; 162425.CADANIAP00003335; -.
DR CAZy; GH53; Glycoside Hydrolase Family 53.
DR CLAE; GAN53A_EMENI; -.
DR EnsemblFungi; EAA62820; EAA62820; AN5727.2.
DR GeneID; 2872012; -.
DR KEGG; ani:AN5727.2; -.
DR VEuPathDB; FungiDB:AN5727; -.
DR eggNOG; ENOG502QU6R; Eukaryota.
DR HOGENOM; CLU_011259_0_0_1; -.
DR InParanoid; Q5B153; -.
DR OrthoDB; 828182at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0031218; F:arabinogalactan endo-1,4-beta-galactosidase activity; IDA:UniProtKB.
DR GO; GO:0015926; F:glucosidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045490; P:pectin catabolic process; IDA:UniProtKB.
DR InterPro; IPR011683; Glyco_hydro_53.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR34983; PTHR34983; 1.
DR Pfam; PF07745; Glyco_hydro_53; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..350
FT /note="Arabinogalactan endo-beta-1,4-galactanase A"
FT /id="PRO_0000394951"
FT ACT_SITE 153
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 263
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:4BF7"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:4BF7"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:4BF7"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:4BF7"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:4BF7"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:4BF7"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:4BF7"
FT HELIX 120..140
FT /evidence="ECO:0007829|PDB:4BF7"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:4BF7"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4BF7"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4BF7"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:4BF7"
FT HELIX 168..183
FT /evidence="ECO:0007829|PDB:4BF7"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:4BF7"
FT HELIX 203..215
FT /evidence="ECO:0007829|PDB:4BF7"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:4BF7"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:4BF7"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:4BF7"
FT HELIX 241..255
FT /evidence="ECO:0007829|PDB:4BF7"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:4BF7"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:4BF7"
FT HELIX 288..305
FT /evidence="ECO:0007829|PDB:4BF7"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:4BF7"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:4BF7"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:4BF7"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:4BF7"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:4BF7"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:4BF7"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:4BF7"
SQ SEQUENCE 350 AA; 38572 MW; 5FF6131E86E5CA3F CRC64;
MILSSLLPLS LVTLTSAALT YRGADISSLL IEEDSGVAYK NLNGETQAFE LILANNGVNS
IRQRIWVNPS DGSYNLEYNL ELAKRVQDAG MSVYLDLHLS DTWADPGDQA TPSGWSTTDI
DTLAWQVYNY TLDVCNTFAE NNVAVEIVSI GNEIRNGLLH PLGSTDHYDN IARLLHSGAW
GVKDSSLSTT PKILFHLDNG WDWDAQKYFY DTVLATGTLL STDFDLIGVS YYPFYNADAT
LSSLKTSLTN LKSNYGKNVL VVETDWPVQC SSPEYAFPSD LSSIPFSADG QETFLGRLAD
TLEDVGGVGI YYWEPGWVDN AGLGSSCEDN LMVDWRDRTV RESISVFGDL
