(data stored in SCRATCH zone)

SWISSPROT: A0KFH1_AERHH

ID   A0KFH1_AERHH            Unreviewed;       336 AA.
AC   A0KFH1;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 76.
DE   RecName: Full=Fructose-1,6-bisphosphatase {ECO:0000256|PIRNR:PIRNR004532};
GN   Name=glpX {ECO:0000313|EMBL:ABK38386.1};
GN   OrderedLocusNames=AHA_0464 {ECO:0000313|EMBL:ABK38386.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK38386.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK38386.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR004532-1};
CC   -!- SIMILARITY: Belongs to the FBPase class 2 family.
CC       {ECO:0000256|PIRNR:PIRNR004532}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000462; ABK38386.1; -; Genomic_DNA.
DR   RefSeq; WP_011704437.1; NC_008570.1.
DR   RefSeq; YP_854997.1; NC_008570.1.
DR   STRING; 380703.AHA_0464; -.
DR   EnsemblBacteria; ABK38386; ABK38386; AHA_0464.
DR   GeneID; 4488862; -.
DR   KEGG; aha:AHA_0464; -.
DR   PATRIC; fig|380703.7.peg.456; -.
DR   eggNOG; ENOG4105CBT; Bacteria.
DR   eggNOG; COG1494; LUCA.
DR   HOGENOM; HOG000241252; -.
DR   KO; K02446; -.
DR   OMA; AVFYMDK; -.
DR   BioCyc; AHYD380703:G1G7B-465-MONOMER; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR   CDD; cd01516; FBPase_glpX; 1.
DR   InterPro; IPR004464; FBPase_class-2/SBPase.
DR   PANTHER; PTHR30447; PTHR30447; 1.
DR   Pfam; PF03320; FBPase_glpX; 1.
DR   PIRSF; PIRSF004532; GlpX; 1.
DR   TIGRFAMs; TIGR00330; glpX; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KFH1.
DR   SWISS-2DPAGE; A0KFH1.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR004532};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Hydrolase {ECO:0000313|EMBL:ABK38386.1};
KW   Manganese {ECO:0000256|PIRSR:PIRSR004532-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR004532-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756}.
FT   REGION       88     90       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR004532-2}.
FT   REGION      164    166       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR004532-2}.
FT   REGION      186    188       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR004532-2}.
FT   METAL        33     33       Manganese 1. {ECO:0000256|PIRSR:
FT                                PIRSR004532-1}.
FT   METAL        57     57       Manganese 1. {ECO:0000256|PIRSR:
FT                                PIRSR004532-1}.
FT   METAL        85     85       Manganese 2. {ECO:0000256|PIRSR:
FT                                PIRSR004532-1}.
FT   METAL        88     88       Manganese 2. {ECO:0000256|PIRSR:
FT                                PIRSR004532-1}.
FT   METAL       213    213       Manganese 2. {ECO:0000256|PIRSR:
FT                                PIRSR004532-1}.
FT   BINDING     119    119       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR004532-2}.
FT   BINDING     210    210       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR004532-2}.
SQ   SEQUENCE   336 AA;  35766 MW;  3FCE40C9970557A3 CRC64;
     MRRELAIEFS RVTEAAALAG YKWLGRGDKN IADGAAVAAM RHILNQIQID GEIVIGEGEI
     DEAPMLYIGE KVGTGLGDAV DIAVDPIEGT RMTAMGQANA LAVLAVGDKG SFLKAPDMYM
     EKLIVGPKAK GAIDLDEALE LNLKAVAKAL GKPLSRLTVI TLAKPRHDKA IKEMQGLGVR
     VFAIPDGDVA ASILTCLPDS EVDMLYGIGG APEGVISAAV IRALDGDMQA RLVPRHQVKG
     DSPEVRALGE QEIARCEALG IDVSKVLKLE DLAKNDNVIF SATGITKGDL LDGITSDGVM
     ATTETLLIRG KSRTIRRIKS IHFLDRKDSV VRDIIL
//

If you have problems or comments...

PBIL Back to PBIL home page