ID W2EMD0_9ACTN Unreviewed; 384 AA.
AC W2EMD0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 28-JUN-2023, entry version 28.
DE RecName: Full=Fructose-1,6-bisphosphate aldolase/phosphatase {ECO:0000256|ARBA:ARBA00018635};
DE EC=3.1.3.11 {ECO:0000256|ARBA:ARBA00013093};
GN ORFNames=MPTA5024_27570 {ECO:0000313|EMBL:ETK32850.1};
OS Microbispora sp. ATCC PTA-5024.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=316330 {ECO:0000313|EMBL:ETK32850.1, ECO:0000313|Proteomes:UP000018869};
RN [1] {ECO:0000313|EMBL:ETK32850.1, ECO:0000313|Proteomes:UP000018869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PTA-5024 {ECO:0000313|EMBL:ETK32850.1,
RC ECO:0000313|Proteomes:UP000018869};
RX PubMed=24459268;
RA Sosio M., Gallo G., Pozzi R., Serina S., Monciardini P., Bera A.,
RA Stegmann E., Weber T.;
RT "Draft Genome Sequence of the Microbispora sp. Strain ATCC-PTA-5024,
RT Producing the Lantibiotic NAI-107.";
RL Genome Announc. 2:e01198-13(2014).
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|ARBA:ARBA00001273};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
CC -!- SUBUNIT: Homooctamer; dimer of tetramers.
CC {ECO:0000256|ARBA:ARBA00011820}.
CC -!- SIMILARITY: Belongs to the FBP aldolase/phosphatase family.
CC {ECO:0000256|ARBA:ARBA00010693}.
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:ETK32850.1}.
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DR EMBL; AWEV01000214; ETK32850.1; -; Genomic_DNA.
DR RefSeq; WP_036329692.1; NZ_KI866525.1.
DR AlphaFoldDB; W2EMD0; -.
DR STRING; 316330.MPTA5024_27570; -.
DR PATRIC; fig|316330.3.peg.5324; -.
DR HOGENOM; CLU_041630_0_0_11; -.
DR OrthoDB; 9763541at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000018869; Unassembled WGS sequence.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR InterPro; IPR002803; FBPase_V.
DR InterPro; IPR036076; FBPase_V_sf.
DR PANTHER; PTHR38341; FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE/PHOSPHATASE; 1.
DR PANTHER; PTHR38341:SF1; FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE/PHOSPHATASE; 1.
DR Pfam; PF01950; FBPase_3; 1.
DR SUPFAM; SSF111249; Sulfolobus fructose-1,6-bisphosphatase-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018869};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT REGION 336..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 384 AA; 40939 MW; 353E3D6A292B823F CRC64;
MITMSVVKAC GGGLIGHASV HPDMIAAARQ EVAAAVSADL LVDGYVADLD DDIALILTHT
EGPDSRPVHS CAWTTVQRTV SVAKELGLYA AGGEMLPDAF SENLRGMGPA FVEVEFDERP
VESVVCLLAD RTEPGAWNLP LCRSFADPFT TAGLVADQKM RAGFGFEVYD LWEDRRIVFD
CPADLYDLLA CVSAPARYAV HHVRSKTLGI PAAATGTQRL PLVAGGYGGT EDPLMIVRCE
SGLPSVGEVL EPFAFPYSVA GAVCGSHHAP YVPVAAGQPG PSRFGGAPRV VALGFQIRGG
RLIGPRDLFA DAAFHPARAR AGEVLEYFRR HGPFEPHRLG SQDSSYPTGT PVPRRLAHRW
TPVAAEPPAT RQPTAESEDE HAQP
//