ID A0A0K8QLP1_9GAMM Unreviewed; 336 AA.
AC A0A0K8QLP1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU003994};
DE EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU003994};
GN ORFNames=MBSD_2232 {ECO:0000313|EMBL:GAN45681.1}, MBSD_n0911
GN {ECO:0000313|EMBL:GAP65621.1};
OS Mizugakiibacter sediminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Mizugakiibacter.
OX NCBI_TaxID=1475481 {ECO:0000313|EMBL:GAP65621.1};
RN [1] {ECO:0000313|EMBL:GAN45681.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SkMP5 {ECO:0000313|EMBL:GAN45681.1};
RA Watanabe T., Kojima H., Fukui M.;
RT "Draft genome sequence of Mizugakiibacter sediminis skMP5.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAP65621.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SkMP5 {ECO:0000313|EMBL:GAP65621.1};
RA Rikkerink E.H.A., Fineran P.C.;
RT "Complete DNA Sequence of Pseudomonas syringae pv. actinidiae, the Causal
RT Agent of Kiwifruit Canker Disease.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC Evidence={ECO:0000256|RuleBase:RU003994};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000256|ARBA:ARBA00004714}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000256|ARBA:ARBA00010387, ECO:0000256|RuleBase:RU003994}.
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DR EMBL; DF952382; GAN45681.1; -; Genomic_DNA.
DR EMBL; DF970163; GAP65621.1; -; Genomic_DNA.
DR RefSeq; WP_062535549.1; NZ_DF970163.1.
DR AlphaFoldDB; A0A0K8QLP1; -.
DR HOGENOM; CLU_031243_0_0_6; -.
DR OrthoDB; 9793595at2; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000253740; Unassembled WGS sequence.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00948; FBP_aldolase_I_a; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR NCBIfam; NF033379; FrucBisAld_I; 1.
DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR11627:SF80; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|RuleBase:RU003994};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003994};
KW Reference proteome {ECO:0000313|Proteomes:UP000253740}.
SQ SEQUENCE 336 AA; 36307 MW; F7B90B9B131E2EB3 CRC64;
MSIEQLESIA QAMVAPGKGI IAIDESNNTI KKRFDAVGVE NTEEHRRAYR EMLLTTPGLN
EHISGAILFD ETIRQSTKAG VPFTKVMMDN GILPGIKVDK GPFPLAGFPG EVVTEGLDGL
RDRLNEYARL GAKFAKWRAV ITIGEDMPSS TCIDANCHAL ARYAALCQEA GLVPMVEPEV
LMDGDHDIDV CYDVTEATLR SLFASLYEHN VMLEGTILKA SMVLSGKDCP EQANIDEVAE
ATIRCLKTTV PAALPGIVFL SGGQSDEQAT AHLNAMNQMG PHPWPLSFSY GRAMQQAALK
LWAKDMTGNF AAAQKTVAQR AKENGLAALG QWSKAA
//
