(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}.
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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
//
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