ALF_CORGL
ID ALF_CORGL Reviewed; 344 AA.
AC P19537;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Fructose-bisphosphate aldolase;
DE Short=FBP aldolase;
DE Short=FBPA;
DE EC=4.1.2.13;
DE AltName: Full=Fructose-1,6-bisphosphate aldolase;
GN Name=fba; Synonyms=fda; OrderedLocusNames=Cgl2770, cg3068;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=2615658; DOI=10.1111/j.1365-2958.1989.tb00148.x;
RA von der Osten C.H., Barbas C.F. III, Wong C.-H., Sinskey A.J.;
RT "Molecular cloning, nucleotide sequence and fine-structural analysis of the
RT Corynebacterium glutamicum fda gene: structural comparison of C. glutamicum
RT fructose-1,6-biphosphate aldolase to class I and class II aldolases.";
RL Mol. Microbiol. 3:1625-1637(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone
CC phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate
CC (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and
CC the reverse reaction in glycolysis. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC provides a structural contribution. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; X17313; CAA35190.1; -; Genomic_DNA.
DR EMBL; BA000036; BAC00164.1; -; Genomic_DNA.
DR EMBL; BX927156; CAF20791.1; -; Genomic_DNA.
DR PIR; S09283; S09283.
DR RefSeq; NP_601964.1; NC_003450.3.
DR RefSeq; WP_011015363.1; NC_006958.1.
DR AlphaFoldDB; P19537; -.
DR SMR; P19537; -.
DR STRING; 196627.cg3068; -.
DR World-2DPAGE; 0001:P19537; -.
DR PRIDE; P19537; -.
DR KEGG; cgb:cg3068; -.
DR KEGG; cgl:Cgl2770; -.
DR PATRIC; fig|196627.13.peg.2701; -.
DR eggNOG; COG0191; Bacteria.
DR HOGENOM; CLU_036923_1_0_11; -.
DR OMA; PRTWGKL; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR006411; Fruct_bisP_bact.
DR PANTHER; PTHR30559; PTHR30559; 1.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR TIGRFAMs; TIGR00167; cbbA; 1.
DR TIGRFAMs; TIGR01520; FruBisAldo_II_A; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycolysis; Lyase; Metal-binding;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2615658"
FT CHAIN 2..344
FT /note="Fructose-bisphosphate aldolase"
FT /id="PRO_0000178712"
FT ACT_SITE 95
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 253..255
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 274..277
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT CONFLICT 280
FT /note="Q -> H (in Ref. 1; CAA35190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 37214 MW; 745B189A2AC72BBF CRC64;
MPIATPEVYN EMLDRAKEGG FAFPAINCTS SETINAALKG FAEAESDGII QFSTGGAEFG
SGLAVKNKVK GAVALAAFAH EAAKSYGINV ALHTDHCQKE VLDEYVRPLL AISQERVDRG
ELPLFQSHMW DGSAVPIDEN LEIAQELLAK AKAANIILEV EIGVVGGEED GVEAKAGANL
YTSPEDFEKT IDAIGTGEKG RYLLAATFGN VHGVYKPGNV KLRPEVLLEG QQVARKKLGL
ADDALPFDFV FHGGSGSEKE KIEEALTYGV IKMNVDTDTQ YAFTRPIVSH MFENYNGVLK
IDGEVGNKKA YDPRSYMKKA EQSMSERIIE SCQDLKSVGK TTSK
