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Database: UniProt
Entry: A0A178EDW1_9PLEO
LinkDB: A0A178EDW1_9PLEO
Original site: A0A178EDW1_9PLEO 
ID   A0A178EDW1_9PLEO        Unreviewed;       606 AA.
AC   A0A178EDW1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Carbohydrate phosphatase {ECO:0000313|EMBL:OAL53449.1};
GN   ORFNames=IQ07DRAFT_597758 {ECO:0000313|EMBL:OAL53449.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL53449.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL53449.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL53449.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC       {ECO:0000256|ARBA:ARBA00005215}.
CC   -!- SIMILARITY: Belongs to the FBPase class 1 family.
CC       {ECO:0000256|ARBA:ARBA00010941}.
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DR   EMBL; KV441640; OAL53449.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178EDW1; -.
DR   STRING; 765867.A0A178EDW1; -.
DR   InParanoid; A0A178EDW1; -.
DR   OrthoDB; 2358283at2759; -.
DR   Proteomes; UP000077535; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR   InterPro; IPR044015; FBPase_C_dom.
DR   InterPro; IPR000146; FBPase_class-1.
DR   InterPro; IPR033391; FBPase_N.
DR   InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR   InterPro; IPR023079; SBPase.
DR   PANTHER; PTHR11556; FRUCTOSE-1,6-BISPHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR11556:SF35; SEDOHEPTULOSE-1,7-BISPHOSPHATASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00316; FBPase; 1.
DR   Pfam; PF18913; FBPase_C; 1.
DR   PRINTS; PR01958; S17BPHPHTASE.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00124; FBPASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077535}.
FT   DOMAIN          312..450
FT                   /note="Fructose-1-6-bisphosphatase class I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00316"
FT   DOMAIN          481..604
FT                   /note="Fructose-1-6-bisphosphatase class 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18913"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   606 AA;  66094 MW;  CC92E29478DEDB26 CRC64;
     MQAQYPQYST TPPSHGVAGV PANQSQGHTY TSPPPPQDEA SSPFAHLLQL PIFQVYSLNE
     FEILQRTIRE NLKNKQIRQE ILDDLPPPPS TADAMTAKVV MEYLSIMSDG GMTFVANRVN
     INKIMSGTMG MLDAMDKQSM QPAATTVYSR WVSPVDMPGP PIIVDILAWY KISKRSHMSG
     VMVKANTEAK FRINSEKPVS VKEGKYWSKT WFRGREDHLN VVVTNDAGVE VSLEKILAVE
     RNLSTPIYGD FLGRWKEFKV PRCVACGSLT RRKSLSCNCR PIMASTKFTA HLQSIFPDQS
     RKALIHEVIP RLLQTLPSIA QGLQRTSVAD VGSANSFGDN QLNVDVLAED LLRSTIAQCP
     AIVTVSSEED PVEKSTDVGS LNTGAGEQYT VAFDPLDGSS IISANWTVGT IIGIWDGASA
     LSKTDTPRQK QIAAILGVLG PRISAVIALR VPGSPQTCIE VTVVDNEITI VNPSVQLKSE
     SKTRYFAPAN MRAAADNANY LQLINYYIAQ KYTLRYSGGL VPDVYHCLVK GHGVYTSPVT
     SSSPAKLRRL YELAPIALVV ECAGGFAIDS ADGSDILDRP IGDTDERGGL ICGSQEELEI
     VRTCLL
//
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