ALF_MYCTU
ID ALF_MYCTU Reviewed; 344 AA.
AC P9WQA3; L0T684; O06313; P67475;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
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; OrderedLocusNames=Rv0363c; ORFNames=MTCY13E10.25c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43093.1; -; Genomic_DNA.
DR PIR; D70576; D70576.
DR RefSeq; NP_214877.1; NC_000962.3.
DR RefSeq; WP_003401856.1; NZ_NVQJ01000002.1.
DR PDB; 3EKL; X-ray; 1.51 A; A=1-344.
DR PDB; 3EKZ; X-ray; 2.07 A; A=1-344.
DR PDB; 3ELF; X-ray; 1.31 A; A=1-344.
DR PDB; 4A21; X-ray; 2.35 A; A/B/C/D=1-344.
DR PDB; 4A22; X-ray; 1.90 A; A/B/C/D=1-344.
DR PDB; 4DEF; X-ray; 1.64 A; A=1-344.
DR PDB; 4DEL; X-ray; 1.58 A; A=1-344.
DR PDB; 4LV4; X-ray; 2.08 A; A=1-344.
DR PDBsum; 3EKL; -.
DR PDBsum; 3EKZ; -.
DR PDBsum; 3ELF; -.
DR PDBsum; 4A21; -.
DR PDBsum; 4A22; -.
DR PDBsum; 4DEF; -.
DR PDBsum; 4DEL; -.
DR PDBsum; 4LV4; -.
DR AlphaFoldDB; P9WQA3; -.
DR SMR; P9WQA3; -.
DR STRING; 83332.Rv0363c; -.
DR BindingDB; P9WQA3; -.
DR ChEMBL; CHEMBL1287620; -.
DR PaxDb; P9WQA3; -.
DR DNASU; 886474; -.
DR GeneID; 45424328; -.
DR GeneID; 886474; -.
DR KEGG; mtu:Rv0363c; -.
DR TubercuList; Rv0363c; -.
DR eggNOG; COG0191; Bacteria.
DR OMA; PRTWGKL; -.
DR PhylomeDB; P9WQA3; -.
DR BRENDA; 4.1.2.13; 3445.
DR UniPathway; UPA00109; UER00183.
DR PRO; PR:P9WQA3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:CAFA.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:MTBBASE.
DR GO; GO:0008270; F:zinc ion binding; IDA:MTBBASE.
DR GO; GO:0035375; F:zymogen binding; IPI:CAFA.
DR GO; GO:0006096; P:glycolytic process; IDA:MTBBASE.
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 3D-structure; Glycolysis; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..344
FT /note="Fructose-bisphosphate aldolase"
FT /id="PRO_0000178722"
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 HELIX 6..18
FT /evidence="ECO:0007829|PDB:3ELF"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:3ELF"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:3ELF"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:3ELF"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:3ELF"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:3ELF"
FT HELIX 68..83
FT /evidence="ECO:0007829|PDB:3ELF"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3ELF"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:3ELF"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:3ELF"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:3ELF"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:3ELF"
FT HELIX 137..153
FT /evidence="ECO:0007829|PDB:3ELF"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:3ELF"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:4DEL"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:4DEL"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:4DEL"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:3ELF"
FT TURN 195..199
FT /evidence="ECO:0007829|PDB:4DEL"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3ELF"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:3ELF"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:3ELF"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:3ELF"
FT HELIX 259..267
FT /evidence="ECO:0007829|PDB:3ELF"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:3ELF"
FT HELIX 277..293
FT /evidence="ECO:0007829|PDB:3ELF"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:3ELF"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:3ELF"
FT HELIX 313..334
FT /evidence="ECO:0007829|PDB:3ELF"
SQ SEQUENCE 344 AA; 36544 MW; 04FA3E1123F72FB1 CRC64;
MPIATPEVYA EMLGQAKQNS YAFPAINCTS SETVNAAIKG FADAGSDGII QFSTGGAEFG
SGLGVKDMVT GAVALAEFTH VIAAKYPVNV ALHTDHCPKD KLDSYVRPLL AISAQRVSKG
GNPLFQSHMW DGSAVPIDEN LAIAQELLKA AAAAKIILEI EIGVVGGEED GVANEINEKL
YTSPEDFEKT IEALGAGEHG KYLLAATFGN VHGVYKPGNV KLRPDILAQG QQVAAAKLGL
PADAKPFDFV FHGGSGSLKS EIEEALRYGV VKMNVDTDTQ YAFTRPIAGH MFTNYDGVLK
VDGEVGVKKV YDPRSYLKKA EASMSQRVVQ ACNDLHCAGK SLTH
