(data stored in ACNUC7421 zone)

SWISSPROT: F16A1_PSEHT

ID   F16A1_PSEHT             Reviewed;         322 AA.
AC   Q3IFQ5;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 86.
DE   RecName: Full=Fructose-1,6-bisphosphatase class 1 1 {ECO:0000255|HAMAP-Rule:MF_01855};
DE            Short=FBPase class 1 1 {ECO:0000255|HAMAP-Rule:MF_01855};
DE            EC=3.1.3.11 {ECO:0000255|HAMAP-Rule:MF_01855};
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 1 {ECO:0000255|HAMAP-Rule:MF_01855};
GN   Name=fbp1 {ECO:0000255|HAMAP-Rule:MF_01855};
GN   OrderedLocusNames=PSHAa0463;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D-
CC       fructose 6-phosphate + phosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_01855}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01855};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01855};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01855}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01855}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01855}.
CC   -!- SIMILARITY: Belongs to the FBPase class 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01855}.
DR   EMBL; CR954246; CAI85560.1; -; Genomic_DNA.
DR   RefSeq; WP_011327173.1; NC_007481.1.
DR   ProteinModelPortal; Q3IFQ5; -.
DR   SMR; Q3IFQ5; -.
DR   STRING; 326442.PSHAa0463; -.
DR   EnsemblBacteria; CAI85560; CAI85560; PSHAa0463.
DR   GeneID; 32567624; -.
DR   KEGG; pha:PSHAa0463; -.
DR   eggNOG; ENOG4105CZI; Bacteria.
DR   eggNOG; COG0158; LUCA.
DR   HOGENOM; HOG000191264; -.
DR   KO; K03841; -.
DR   OMA; QSGLVCR; -.
DR   OrthoDB; POG091H05DB; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   CDD; cd00354; FBPase; 1.
DR   HAMAP; MF_01855; FBPase_class1; 1.
DR   InterPro; IPR000146; FBPase_class-1.
DR   InterPro; IPR033391; FBPase_N.
DR   InterPro; IPR028343; FBPtase.
DR   PANTHER; PTHR11556; PTHR11556; 1.
DR   Pfam; PF00316; FBPase; 1.
DR   PIRSF; PIRSF500210; FBPtase; 1.
DR   PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR   PRINTS; PR00115; F16BPHPHTASE.
PE   3: Inferred from homology;
DR   PRODOM; Q3IFQ5.
DR   SWISS-2DPAGE; Q3IFQ5.
KW   Carbohydrate metabolism; Complete proteome; Cytoplasm; Hydrolase;
KW   Magnesium; Metal-binding; Reference proteome.
FT   CHAIN         1    322       Fructose-1,6-bisphosphatase class 1 1.
FT                                /FTId=PRO_0000364637.
FT   REGION      106    109       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL        84     84       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL       103    103       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL       103    103       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL       105    105       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01855}.
FT   METAL       106    106       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL       270    270       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   BINDING     198    198       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   BINDING     264    264       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
SQ   SEQUENCE   322 AA;  35147 MW;  9E4689C2E3350C29 CRC64;
     MRRLPPVLLE DGCPRELISL IRTILAACKE ISFRVGQGEL SGVLGSTLDE NIQGETQKKL
     DVLTNQLLKD ILLESGYVKA IASEEEDYTV AGNPDAEYIV AFDPLDGSSN TDINSLVGTI
     FSVMKAPEGA DPADQSIFMQ PGINQVAAGY VLYGPSTILA LTTGKGTRFF TLDKTHGTFL
     LTQDFAKIPA DTNEYAINAS NQRHWQPAMQ NYINDLVAGD TGPRARNFNM RWIAAMVGDV
     HRVLSRGGLF TYPTDTKNPS QPNKLRLLYE ANPMAMLVEQ AGGIASTGTE RIMDIQPNAI
     HQRVAVILGS KNEVETCLGY HK
//

If you have problems or comments...

PBIL Back to PBIL home page