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
//