ID   AGALC_EMENI             Reviewed;         750 AA.
AC   Q5AU92; C8V6Q1; Q1HFQ9;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Alpha-galactosidase C;
DE            EC=3.2.1.22;
DE   AltName: Full=Melibiase C;
DE   Flags: Precursor;
GN   Name=aglC; ORFNames=AN8138;
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: Hydrolyzes a variety of simple alpha-D-galactoside as well as
CC       more complex molecules such as oligosaccharides and polysaccharides.
CC       Active on paranitrophenyl-alpha-galactoside, raffinose, locust bean gum
CC       and gum guar. {ECO:0000269|PubMed:16844780}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC         residues in alpha-D-galactosides, including galactose
CC         oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 3.5. {ECO:0000269|PubMed:16844780};
CC       Temperature dependence:
CC         Optimum temperature is 52 degrees Celsius.
CC         {ECO:0000269|PubMed:16844780};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 36 family. {ECO:0000305}.
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DR   EMBL; DQ490515; ABF50891.1; -; mRNA.
DR   EMBL; AACD01000140; EAA58775.1; -; Genomic_DNA.
DR   EMBL; BN001302; CBF73961.1; -; Genomic_DNA.
DR   RefSeq; XP_681407.1; XM_676315.1.
DR   AlphaFoldDB; Q5AU92; -.
DR   SMR; Q5AU92; -.
DR   STRING; 162425.CADANIAP00004173; -.
DR   CAZy; GH36; Glycoside Hydrolase Family 36.
DR   CLAE; MEL36C_EMENI; -.
DR   EnsemblFungi; CBF73961; CBF73961; ANIA_08138.
DR   EnsemblFungi; EAA58775; EAA58775; AN8138.2.
DR   GeneID; 2869187; -.
DR   KEGG; ani:AN8138.2; -.
DR   VEuPathDB; FungiDB:AN8138; -.
DR   eggNOG; ENOG502QWG1; Eukaryota.
DR   HOGENOM; CLU_009640_2_1_1; -.
DR   InParanoid; Q5AU92; -.
DR   OMA; WEGIYFD; -.
DR   OrthoDB; 472260at2759; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IDA:UniProtKB.
DR   GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070085; P:glycosylation; IDA:AspGD.
DR   GO; GO:0046355; P:mannan catabolic process; IDA:UniProtKB.
DR   CDD; cd14791; GH36; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 2.70.98.60; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR038417; Alpga-gal_N_sf.
DR   InterPro; IPR002252; Glyco_hydro_36.
DR   InterPro; IPR031705; Glyco_hydro_36_C.
DR   InterPro; IPR031704; Glyco_hydro_36_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF16874; Glyco_hydro_36C; 1.
DR   Pfam; PF16875; Glyco_hydro_36N; 1.
DR   PIRSF; PIRSF005536; Agal; 1.
DR   PRINTS; PR00743; GLHYDRLASE36.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase; Magnesium;
KW   NAD; Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..750
FT                   /note="Alpha-galactosidase C"
FT                   /id="PRO_0000395067"
FT   ACT_SITE        511
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT   ACT_SITE        573
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        432
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        453
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   750 AA;  82202 MW;  826605C1031BE18A CRC64;
     MFRSTATVAA ATAMGLLTAT GHGSLAIAQG TTGSNAVVVD GTNFALNGAS MSYVFHANST
     TGDLVSDHFG ATISGAIPAP KEPAVNGWVG MPGRIRREFP DQGRGDFRIP AVRIRQTAGY
     TVSDLQYQGH EVVDGKPALP GLPATFGEAG DVTTLVVHLY DNYSAVAADL SYSVFPEFDA
     VVRSVNVTNK GKGNITIENL ASLSVDFPLE DLDLVSLRGD WAREANRERR RVEYGIQGFG
     SSTGYSSHLH NPFFALVHPS TTESQGEAWG FNLVYTGSFS AQVEKGSQGL TRALIGFNPD
     QLSWNLGPGE TLTSPECVSV YSKDGIGGMS RKFHRLYRKH LIRSKFATSD RPPLLNSWEG
     VYFDFNQSSI ETLAEQSAAL GIRLFVMDDG WFGDKYPRTS DNAGLGDWTP NPDRFPNGLE
     PVVEEITNLT VNDTSAEKLR FGIWVEPEMV NPNSSLYREH PDWALHAGAY ARTERRNQLV
     LNLALPEVQE YIIDFMTDLL NSADISYIKW DNNRGIHEAP SPSTDHEYML GVYRVFDTLT
     ARFPDVLWEG CASGGGRFDA GVLHYFPQIW TSDNTDGVDR VTIQFGTSLA YPPSAMGAHL
     SAVPNHQTGR TVPLEFRAHV AMMGGSFGLE LDPATLQDDP DVPELIQMAE KVNPLVLNGD
     LYRLRLPEES QWPAALFVAE DGSQAVLFYF QLSPNVNHAA PWVRLQGLDP EASYTVDGDK
     TYTGATLMNL GLQYTFDTEY GSKVVFLERQ