ID   6PGL_ARTBC              Reviewed;         394 AA.
AC   D4B0N9;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Probable 6-phosphogluconolactonase ARB_02015 {ECO:0000305};
DE            EC=3.1.1.31 {ECO:0000250|UniProtKB:O34499};
DE   Flags: Precursor;
GN   ORFNames=ARB_02015;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
CC   -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-
CC       phosphogluconate. {ECO:0000250|UniProtKB:O34499}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
CC         + H(+); Xref=Rhea:RHEA:12556, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57955, ChEBI:CHEBI:58759; EC=3.1.1.31;
CC         Evidence={ECO:0000250|UniProtKB:O34499};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       2/3. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the cycloisomerase 2 family. {ECO:0000305}.
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DR   EMBL; ABSU01000024; EFE31146.1; -; Genomic_DNA.
DR   RefSeq; XP_003011786.1; XM_003011740.1.
DR   AlphaFoldDB; D4B0N9; -.
DR   SMR; D4B0N9; -.
DR   STRING; 663331.D4B0N9; -.
DR   EnsemblFungi; EFE31146; EFE31146; ARB_02015.
DR   GeneID; 9523559; -.
DR   KEGG; abe:ARB_02015; -.
DR   eggNOG; ENOG502S3WY; Eukaryota.
DR   HOGENOM; CLU_038716_0_1_1; -.
DR   OMA; VMSAMYS; -.
DR   UniPathway; UPA00115; UER00409.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR011048; Haem_d1_sf.
DR   InterPro; IPR019405; Lactonase_7-beta_prop.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   Pfam; PF10282; Lactonase; 1.
DR   SUPFAM; SSF51004; SSF51004; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glucose metabolism; Glycoprotein; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..394
FT                   /note="Probable 6-phosphogluconolactonase ARB_02015"
FT                   /id="PRO_5003054590"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   394 AA;  42509 MW;  89582D918F803717 CRC64;
     MKTVPFLSLL QAGILTSGIV AQNIAFVGSN ANAIATVSFD TKTGTFKVTG NNTDSSTPSW
     QEVSRDGKLL YSIEETSTEH ALTSYSIGQD GKLKKLKSIK GLAGPVSLDM HPTQPIIITA
     NYGSASASAY SSKDNGELTH LGDFMFKMQG KGKVPDRQDA PHPHQALFDP TGKFVLMPDL
     GSDLIRILKV DAGQKFSVAP PNKVKPGTGP RHGVLYPASD KPRFYYVVGE LSNTVTAMSV
     EYTVETIKLT EIQTLSTLPD GQRGAAGELI LSPSGKHLYA SNRLDKVFPG SSSVASYTID
     QMTGKLKLLE IFNGGVENIR HMSIHPSGKW FVTEGQNSND IKVFALDPET GKVTPEAKST
     LEIEKPVCLQ WWHNGAQESE APEAGTETEC EFDD