ATC1_CANAL
ID ATC1_CANAL Reviewed; 1078 AA.
AC Q5AAU5; A0A1D8PDZ0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cell wall acid trehalase ATC1;
DE EC=3.2.1.28;
DE AltName: Full=Alpha,alpha-trehalase;
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase;
DE Flags: Precursor;
GN Name=ATC1; Synonyms=ATH1; OrderedLocusNames=CAALFM_C106940CA;
GN ORFNames=CaO19.13595, CaO19.6214;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1103165;
RA Arnold W.N., McLellan M.N.;
RT "Trehalose and glycogen levels during the initial stages of growth of
RT Candida albicans.";
RL Physiol. Chem. Phys. 7:369-380(1975).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7553268; DOI=10.1006/emyc.1995.1022;
RA Molloy C., Shepherd M.G., Sullivan P.A.;
RT "Differential extraction of N-acetylglucosaminidase and trehalase from the
RT cell envelope of Candida albicans.";
RL Exp. Mycol. 19:178-185(1995).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15252058; DOI=10.1074/jbc.m400216200;
RA Pedreno Y., Maicas S., Arguelles J.C., Sentandreu R., Valentin E.;
RT "The ATC1 gene encodes a cell wall-linked acid trehalase required for
RT growth on trehalose in Candida albicans.";
RL J. Biol. Chem. 279:40852-40860(2004).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17464051; DOI=10.1099/mic.0.2006/003921-0;
RA Pedreno Y., Gonzalez-Parraga P., Martinez-Esparza M., Sentandreu R.,
RA Valentin E., Arguelles J.C.;
RT "Disruption of the Candida albicans ATC1 gene encoding a cell-linked acid
RT trehalase decreases hypha formation and infectivity without affecting
RT resistance to oxidative stress.";
RL Microbiology 153:1372-1381(2007).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=19336219; DOI=10.1016/j.bbrc.2009.03.134;
RA Sanchez-Fresneda R., Gonzalez-Parraga P., Esteban O., Laforet L.,
RA Valentin E., Arguelles J.C.;
RT "On the biochemical classification of yeast trehalases: Candida albicans
RT contains two enzymes with mixed features of neutral and acid trehalase
RT activities.";
RL Biochem. Biophys. Res. Commun. 383:98-102(2009).
RN [9]
RP INDUCTION.
RX PubMed=21592964; DOI=10.1074/jbc.m111.233569;
RA Singh R.P., Prasad H.K., Sinha I., Agarwal N., Natarajan K.;
RT "Cap2-HAP complex is a critical transcriptional regulator that has dual but
RT contrasting roles in regulation of iron homeostasis in Candida albicans.";
RL J. Biol. Chem. 286:25154-25170(2011).
CC -!- FUNCTION: Cell wall acid trehalase that catalyzes hydrolysis of the
CC disaccharide trehalose and required for growth on trehalose as carbon
CC source. Plays a role in dimorphic conversion and virulence.
CC {ECO:0000269|PubMed:1103165, ECO:0000269|PubMed:15252058,
CC ECO:0000269|PubMed:17464051, ECO:0000269|PubMed:19336219,
CC ECO:0000269|PubMed:7553268}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-
CC glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28;
CC Evidence={ECO:0000269|PubMed:15252058, ECO:0000269|PubMed:19336219};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:1103165,
CC ECO:0000269|PubMed:15252058, ECO:0000269|PubMed:7553268}.
CC -!- INDUCTION: Expression is repressed by glucose and by HAP43.
CC {ECO:0000269|PubMed:19336219, ECO:0000269|PubMed:21592964}.
CC -!- DISRUPTION PHENOTYPE: Lacks acid trehalase activity and decreases hypha
CC formation and infectivity. {ECO:0000269|PubMed:15252058,
CC ECO:0000269|PubMed:17464051}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26348.1; -; Genomic_DNA.
DR RefSeq; XP_718804.2; XM_713711.2.
DR AlphaFoldDB; Q5AAU5; -.
DR SMR; Q5AAU5; -.
DR STRING; 237561.Q5AAU5; -.
DR PRIDE; Q5AAU5; -.
DR GeneID; 3639570; -.
DR KEGG; cal:CAALFM_C106940CA; -.
DR CGD; CAL0000186706; ATC1.
DR VEuPathDB; FungiDB:C1_06940C_A; -.
DR eggNOG; KOG4125; Eukaryota.
DR HOGENOM; CLU_006285_4_0_1; -.
DR InParanoid; Q5AAU5; -.
DR OrthoDB; 125022at2759; -.
DR BRENDA; 3.2.1.28; 1096.
DR PRO; PR:Q5AAU5; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0030287; C:cell wall-bounded periplasmic space; IEA:EnsemblFungi.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR GO; GO:0016021; C:integral component of membrane; IEA:EnsemblFungi.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0015976; P:carbon utilization; IEA:EnsemblFungi.
DR GO; GO:0005993; P:trehalose catabolic process; IBA:GO_Central.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW Cell wall; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Secreted; Signal; Virulence.
FT SIGNAL 1..54
FT /evidence="ECO:0000255"
FT CHAIN 55..1078
FT /note="Cell wall acid trehalase ATC1"
FT /id="PRO_0000428633"
FT ACT_SITE 607
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 478..479
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 676..677
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 829
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 837
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 904
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 922
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 946
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1003
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1037
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1078 AA; 120236 MW; 2D08E9D5CD11FC24 CRC64;
MAANSSFFLA DNCAPHNQSF IQFCIHAASK KKGRIALMCL ANLFLLFSFH LLYARFCSGF
PYVVPSTARS TNQIFHTNLE QLVNSPENKQ IFSQLKFSDQ AFYDPHDNVV GTTEFPVFNQ
YQRQPYVANG YIGSRIPNLG QGFTYDQLTN SSTANDDDLL NGWPLFNKRY SGAFVAGFYD
LQKNTTGTNF AELLENGYES VIAAVPQWTA LSLSVEILGK KYTLDPSLEH EAIGDITNYV
QNMSLSDGIV TTQFTWLNTF DVKYEILAHR ENINLGLVNM QVYNPGNESV QVIVSDVLDF
NSSQRCQLNQ ISHDKNGIYV TFHPQGLSYI DGAIYSTLSA NGQITREQTN ETVFQNVELT
IEPHSCVQVA KYVGIATTDL DPDSFKTADD VLKFARKVSQ NKKHGDATQL VNSHRSAWSK
IIQDAPLVTF PSDSLLNLGA RASIFHLLAN TRPNAEGVTG ALGVSGLSSD SYGGMVFWDT
DLWMLNGILP FAPDHIKSFI NYRVHLHQQA IDNVPRGYQG AVYPWTSGRF GNCTGTGPCL
DYEYHINMAV AMASWQLYIS GAADDTFLES VAYPIINDAA SFLAEYVVHY NDTLGKYTTK
NLTDPDEFAN HVDNGAYTNT GIVLVMRWAQ IAGSILGKQV PKIYHDIETA MFLPTAENTQ
NITLEYSGMN SSVGIKQADV IMMTYPLENE LIDQDQAYIN MEFYSMKQVG YGPAMTFPIF
SIVASNLAFT GCASQSYLHK AIQPFLRGPF AQFAEQNNDD YLTNGGTHPA FPFLTAHGGF
LQAILQGLTG MRFDYTFENN KLQRLLKLDP IALPCLGEGV RFDSIKYDNH TLSMAINETH
FTIKNKGKTT PNARNYVTIL LAERNAMHGK YTINDEDEQS FPLFETSESF PDSISECNKA
GFFNITEGAY GDVSISINDG DNTTSWQAKY NDTTGKVLVD LKSFRNISSG TFIWGDKPPK
RVKVSKYSGS SFTAVTDFFA QVDFGNELFN EYKYANPEGK LHNQSDVFEE VYSGDVKISA
PFDPEEYFQV WVPTRHNITE VAVNLQTRFL LIEVDEIHNT EAIDGDYGGA KLAEVVFY
