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Database: UniProt
Entry: A0A374AQ63_9FIRM
LinkDB: A0A374AQ63_9FIRM
Original site: A0A374AQ63_9FIRM 
ID   A0A374AQ63_9FIRM        Unreviewed;       652 AA.
AC   A0A374AQ63;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   05-FEB-2025, entry version 16.
DE   RecName: Full=Fructose-1,6-bisphosphatase class 3 {ECO:0000256|HAMAP-Rule:MF_01854};
DE            Short=FBPase class 3 {ECO:0000256|HAMAP-Rule:MF_01854};
DE            EC=3.1.3.11 {ECO:0000256|HAMAP-Rule:MF_01854};
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 3 {ECO:0000256|HAMAP-Rule:MF_01854};
GN   Name=fbp {ECO:0000256|HAMAP-Rule:MF_01854};
GN   ORFNames=DWV72_04985 {ECO:0000313|EMBL:RGH24174.1};
OS   Firmicutes bacterium AF12-30.
OC   Bacteria; Bacillati; Bacillota.
OX   NCBI_TaxID=2292884 {ECO:0000313|EMBL:RGH24174.1, ECO:0000313|Proteomes:UP000262638};
RN   [1] {ECO:0000313|EMBL:RGH24174.1, ECO:0000313|Proteomes:UP000262638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF12-30 {ECO:0000313|EMBL:RGH24174.1,
RC   ECO:0000313|Proteomes:UP000262638};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC         phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01854};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01854};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01854}.
CC   -!- SIMILARITY: Belongs to the FBPase class 3 family. {ECO:0000256|HAMAP-
CC       Rule:MF_01854}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RGH24174.1}.
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DR   EMBL; QTXP01000006; RGH24174.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A374AQ63; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000262638; Unassembled WGS sequence.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.60.21.10; -; 1.
DR   HAMAP; MF_01854; FBPase_class3; 1.
DR   InterPro; IPR009164; FBPtase_class3.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   Pfam; PF06874; FBPase_2; 1.
DR   PIRSF; PIRSF000906; FBPtase_Bacill; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_01854}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_01854};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01854};
KW   Reference proteome {ECO:0000313|Proteomes:UP000262638}.
SQ   SEQUENCE   652 AA;  75595 MW;  B7C217E7CB9B9094 CRC64;
     MDQMKYLKEL AVRYPNVAAA STEIINLQAI LHLPKGTEHY LSDVHGEYEK FSHIIRNGSG
     AVRSKIEDEF GNTLTKKQKK NLASVIYYPE QKMDLMEEEL PRNELLEWQH DTMVRLVHVA
     RAVGNKYTRS KVRKAMNPQF AYIMEELMVE HRRADKKKYV EQILETIITT GRVRQFIAAM
     AHLIQDLSID HLHVIGDIYD RGSGPHRIMD CIMKTEKVDI QWGNHDILWM GAASGHRACI
     CNVVRICARY NNLDVLENGY GINLIPLARF ALECYKDDDC ELFHASGEVD ESNIREEELN
     KKMHKAIAII QFKVEGQLIK RRPDFLMDDR LLLDKVDYEK GTITLDGKEY ELRDKNFPTI
     DPEDPYKLTK EEEYVMDHLV TVFKYCAYLQ EHVRFLFAKG NLYKVFNGML LYHGCVPLNE
     DGTFREVEIE GRKYAGKELY DILEHLARQG YYEEKNMKAR KYGQDIMWFI WSNENSPVYG
     KAKMATFERY FLDDADLKKE KKDYYYQWYE NETVINQILE EFGLDPATGK IVNGHMPVAV
     KKGESPIKCG GKLFVIDGGF SKAYQKTTGI AGYTLVSNSY ELKIVAHEPF VSRDTAIREE
     TDIHSDTTII NKVTKRKCVL DTDNGKALQE KVADLEQLLW AYQKGLITER IL
//
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