PVG1_SCHPO
ID PVG1_SCHPO Reviewed; 401 AA.
AC Q9UT27; Q9P803;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Pyruvyl transferase 1;
DE EC=2.-.-.-;
DE AltName: Full=Pyruvylated Gal-beta-1,3-epitope synthesis protein 1;
DE Short=PvGal synthesis protein 1;
DE Flags: Precursor;
GN Name=pvg1; ORFNames=SPAC8F11.10c, SPACUNK4.18;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION.
RX PubMed=15173185; DOI=10.1074/jbc.m403574200;
RA Andreishcheva E.N., Kunkel J.P., Gemmill T.R., Trimble R.B.;
RT "Five genes involved in biosynthesis of the pyruvylated Galbeta1,3-epitope
RT in Schizosaccharomyces pombe N-linked glycans.";
RL J. Biol. Chem. 279:35644-35655(2004).
CC -!- FUNCTION: Involved in cell wall biogenesis. Has a role in the addition
CC of Gal-beta1,3 moieties to galactomannans and their subsequent
CC pyruvylation. {ECO:0000269|PubMed:15173185}.
CC -!- SIMILARITY: Belongs to the polysaccharide pyruvyl transferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB52171.1; -; Genomic_DNA.
DR PIR; T39185; T39185.
DR RefSeq; NP_593959.1; NM_001019386.2.
DR PDB; 5AX7; X-ray; 2.46 A; A/B=54-401.
DR PDBsum; 5AX7; -.
DR AlphaFoldDB; Q9UT27; -.
DR SMR; Q9UT27; -.
DR BioGRID; 279926; 5.
DR STRING; 4896.SPAC8F11.10c.1; -.
DR MaxQB; Q9UT27; -.
DR PaxDb; Q9UT27; -.
DR PRIDE; Q9UT27; -.
DR EnsemblFungi; SPAC8F11.10c.1; SPAC8F11.10c.1:pep; SPAC8F11.10c.
DR PomBase; SPAC8F11.10c; pvg1.
DR VEuPathDB; FungiDB:SPAC8F11.10c; -.
DR eggNOG; ENOG502S3FU; Eukaryota.
DR HOGENOM; CLU_045699_0_0_1; -.
DR InParanoid; Q9UT27; -.
DR OMA; GNVTYNK; -.
DR PhylomeDB; Q9UT27; -.
DR BioCyc; MetaCyc:MON-20446; -.
DR PRO; PR:Q9UT27; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
DR GO; GO:0046919; F:pyruvyltransferase activity; IDA:PomBase.
DR GO; GO:0051072; P:4,6-pyruvylated galactose residue biosynthetic process; IDA:PomBase.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IC:PomBase.
DR InterPro; IPR007345; Polysacch_pyruvyl_Trfase.
DR Pfam; PF04230; PS_pyruv_trans; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Reference proteome; Signal;
KW Transferase.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..401
FT /note="Pyruvyl transferase 1"
FT /id="PRO_0000029851"
FT REGION 38..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 62..86
FT /evidence="ECO:0007829|PDB:5AX7"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:5AX7"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:5AX7"
FT HELIX 104..119
FT /evidence="ECO:0007829|PDB:5AX7"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:5AX7"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:5AX7"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:5AX7"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:5AX7"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:5AX7"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:5AX7"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:5AX7"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:5AX7"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:5AX7"
FT HELIX 196..208
FT /evidence="ECO:0007829|PDB:5AX7"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:5AX7"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:5AX7"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:5AX7"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:5AX7"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:5AX7"
FT HELIX 249..254
FT /evidence="ECO:0007829|PDB:5AX7"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:5AX7"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:5AX7"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:5AX7"
FT HELIX 312..328
FT /evidence="ECO:0007829|PDB:5AX7"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:5AX7"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:5AX7"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:5AX7"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:5AX7"
FT HELIX 363..369
FT /evidence="ECO:0007829|PDB:5AX7"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:5AX7"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:5AX7"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:5AX7"
FT HELIX 385..398
FT /evidence="ECO:0007829|PDB:5AX7"
SQ SEQUENCE 401 AA; 44872 MW; C79DD4E9B0DBCD1F CRC64;
MFANINIRKS VWLFLLAAVS CTLFIYGVTR TDLQTLKNPS SLTSPSSSTS VDKKKPLFTK
SPRNSASCES TITLQSNLLF TYYKHYFAGI KKVALIGFPD HPNKGDSAIY VAEKKLLDAL
NIEVVYITAQ EADYSASELK SIISDIPRDE FALAFHGGGN FGDLYPDHQH LRELVVRDFP
SFTTISFPQS VWYNEQQLLE QASILYAENP NITLVTRDRQ SYGFAVDAFG KHNEVLLTPD
IVFFMGPIPE IREATPITHD VLILARLDHE GGQQHGAEDY YRDTLNAANL TYSVEDWLLW
DPPVAQNPDS SFDDRGQARY EAGAEFLASA RVVITDRLHA HILSTLMGIP HIVVENSQMG
KITNYHNTWL HGCTLDGVSV VVDSVDKALS LLLEWNEAGY F
