PGA5_CANAL
ID PGA5_CANAL Reviewed; 641 AA.
AC Q59VW6; A0A1D8PCQ4;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=1,3-beta-glucanosyltransferase PGA5;
DE EC=2.4.1.-;
DE AltName: Full=Predicted GPI-anchored protein 5;
DE Flags: Precursor;
GN Name=PGA5; Synonyms=GAS12; OrderedLocusNames=CAALFM_C102360CA;
GN ORFNames=CaO19.11177, CaO19.3693;
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 PREDICTION OF GPI-ANCHOR.
RX PubMed=12845604; DOI=10.1002/yea.1007;
RA De Groot P.W., Hellingwerf K.J., Klis F.M.;
RT "Genome-wide identification of fungal GPI proteins.";
RL Yeast 20:781-796(2003).
RN [5]
RP INDUCTION.
RX PubMed=17257864; DOI=10.1016/j.fgb.2006.12.006;
RA Eckert S.E., Heinz W.J., Zakikhany K., Thewes S., Haynes K., Hube B.,
RA Muhlschlegel F.A.;
RT "PGA4, a GAS homologue from Candida albicans, is up-regulated early in
RT infection processes.";
RL Fungal Genet. Biol. 44:368-377(2007).
CC -!- FUNCTION: Splits internally a 1,3-beta-glucan molecule and transfers
CC the newly generated reducing end (the donor) to the non-reducing end of
CC another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta
CC linkage, resulting in the elongation of 1,3-beta-glucan chains in the
CC cell wall. Involved in spore wall assembly (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- INDUCTION: Expression is very weak and pH-independent.
CC {ECO:0000269|PubMed:17257864}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000305}.
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DR EMBL; CP017623; AOW25920.1; -; Genomic_DNA.
DR RefSeq; XP_713787.2; XM_708694.2.
DR AlphaFoldDB; Q59VW6; -.
DR SMR; Q59VW6; -.
DR STRING; 237561.Q59VW6; -.
DR GeneID; 3644575; -.
DR KEGG; cal:CAALFM_C102360CA; -.
DR CGD; CAL0000178583; PGA5.
DR VEuPathDB; FungiDB:C1_02360C_A; -.
DR eggNOG; ENOG502QRZZ; Eukaryota.
DR HOGENOM; CLU_021855_2_0_1; -.
DR InParanoid; Q59VW6; -.
DR OrthoDB; 728071at2759; -.
DR PRO; PR:Q59VW6; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; ISA:CGD.
DR GO; GO:0030476; P:ascospore wall assembly; IEA:EnsemblFungi.
DR GO; GO:0034411; P:cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR InterPro; IPR004886; Glucanosyltransferase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR012946; X8.
DR PANTHER; PTHR31468; PTHR31468; 1.
DR Pfam; PF03198; Glyco_hydro_72; 1.
DR Pfam; PF07983; X8; 1.
DR SMART; SM00768; X8; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
KW Signal; Transferase.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..622
FT /note="1,3-beta-glucanosyltransferase PGA5"
FT /id="PRO_0000424642"
FT PROPEP 623..641
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424643"
FT REGION 535..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..595
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 304
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 192
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 193
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="2"
FT /ligand_note="acceptor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 234
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="2"
FT /ligand_note="acceptor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 239
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="2"
FT /ligand_note="acceptor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 336
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT LIPID 622
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..135
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 248..390
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 276..307
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 424..474
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 426..528
FT /evidence="ECO:0000250"
FT DISULFID 433..498
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 451..456
FT /evidence="ECO:0000250|UniProtKB:Q06135"
SQ SEQUENCE 641 AA; 72378 MW; 834A8CDBCC6341F0 CRC64;
MTTLSTIWLF LITITAIFQL GLSSNVTTII DDDNNNNNNN NNNADDFLEP QIETIKVIGN
KFFECESGHQ FFIKGIAYQK TRQEGEIYDT TKEPHYIDPL ANPFTCLRDL DYLKELGINL
VRVYQIHPNA NHDVCMNAFA EAGIYVLADL SEPTISIRRD YPHWDTEIFN RYQQVIDSMS
NYKNLLGFFA GNEVTNCQSN IDASPFVRAA IRDCKKYINQ QGYRKIPIGY ASNDDANIRK
NLANYFVCQL DEDEDKGQEH LNSQADFFAI NVYEWCGYST YTTSGYRDLT TMFKDYSVPV
FFSEFGCNII TPRPFTEVEA IYGSTMKKVW SGGIAYEYFE EVNHYGILLT KKDGSITKLP
DFDTLKMRFH AATPIGITMD EATICEPPIC SNSVIDDKSS SSSSSSSFWD VALTLPPTPN
EAKCECLWQS LSCVVSEDAT FDEEVALREL CFKVDCEDIN ANGRSGKYGR YSDCNPTVRT
SYALNKYYEQ CGKKQEICDF QGRGELLPNR NGGLQDLENK FSSDGQNCLS LLEGKEEEKE
VQEEEPDVPG LPGSNKGKEV ESTPKRKGKG KSKEKEKGKL IEEEEEEEEE EEENNKTPSS
GEKSPKTSKS IAGGNAITFK NDSIWKTFIE ILFTCSAAIL I
