F16PC_LIGS1
ID F16PC_LIGS1 Reviewed; 641 AA.
AC Q1WQZ0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Fructose-1,6-bisphosphatase class 3 {ECO:0000255|HAMAP-Rule:MF_01854};
DE Short=FBPase class 3 {ECO:0000255|HAMAP-Rule:MF_01854};
DE EC=3.1.3.11 {ECO:0000255|HAMAP-Rule:MF_01854};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 3 {ECO:0000255|HAMAP-Rule:MF_01854};
GN Name=fbp {ECO:0000255|HAMAP-Rule:MF_01854}; OrderedLocusNames=LSL_1903;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OG Plasmid pMP118.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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:0000255|HAMAP-Rule:MF_01854};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01854};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_01854}.
CC -!- SIMILARITY: Belongs to the FBPase class 3 family. {ECO:0000255|HAMAP-
CC Rule:MF_01854}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABE00708.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000234; ABE00708.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_536791.1; NC_007930.1.
DR AlphaFoldDB; Q1WQZ0; -.
DR EnsemblBacteria; ABE00708; ABE00708; LSL_1903.
DR KEGG; lsl:LSL_1903; -.
DR PATRIC; fig|362948.14.peg.2029; -.
DR HOGENOM; CLU_028392_2_0_9; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000006559; Plasmid pMP118.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
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; SSF56300; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Hydrolase; Manganese; Plasmid; Reference proteome.
FT CHAIN 1..641
FT /note="Fructose-1,6-bisphosphatase class 3"
FT /id="PRO_0000363097"
SQ SEQUENCE 641 AA; 74546 MW; 3A27DB5D924F956D CRC64;
MNAYSHNLLK EKYPTKQDVI TEIMNLEAIL HLPKGTEHFV SDLHGEYTAF DHVLRNGSGS
IKQKIQDYFS DRMTEQTMQD FALLIYYPED ELALVKKKLR TENELQQWYL DNISHLLEFL
ELSGSKYTRS KVRKALNPNF VYITEELLYN DPQEFNKRSY INQLLKNILK LDQADKFIIA
TCYTIQRLVV DHLHVLGDVY DRGEEPDKIM DRLMNYHSVD MQWGNHDLLW LGAMAGSKLC
MLNLLRICAR YNNLNIIEDA YGINLRHLSR FAEEQYEDNP QFRPKLTNGD GYRFNGEKLQ
ITQIHQAVAM MQFKLEGQVI ARRPELKMDD RDLLNKIDYK KNVINLNGKE YSLQNTCFNT
VDPKNPNELT DEENAIVDEL LISIQHSTKL KRHLDFMMNK GSMYRTYNGN LLFHGCIPAD
EEGNFCSLKI GSKEYSGKKL FDFSEKMIRK AYSKPNVKDD FATDFMWYLW QGALSPLFGK
KSMTTFERYF IADKACHEEV KNPYYKLREN KDFCIKILQE FGFAGDDTNH IINGHTPVKR
GHNAICAEGY MLVIDGGYSK AYQPTTGIAG YTLLYNSYGL QLVSHQPFTS KQDAIRSGKD
IVSTVRVVKH ELQRKSVADT DIGENIKEKI RVLYNLLRNY D