ALF1_PORGI
ID ALF1_PORGI Reviewed; 293 AA.
AC P60053;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Fructose-bisphosphate aldolase class 1 {ECO:0000255|HAMAP-Rule:MF_00729};
DE EC=4.1.2.13 {ECO:0000255|HAMAP-Rule:MF_00729};
DE AltName: Full=Fructose-bisphosphate aldolase class I;
DE Short=FBP aldolase {ECO:0000255|HAMAP-Rule:MF_00729};
GN Name=fda {ECO:0000255|HAMAP-Rule:MF_00729}; Synonyms=fbaB;
GN OrderedLocusNames=PG_1755;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
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:0000255|HAMAP-Rule:MF_00729};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000255|HAMAP-Rule:MF_00729}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000255|HAMAP-Rule:MF_00729}.
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DR EMBL; AE015924; AAQ66757.1; -; Genomic_DNA.
DR RefSeq; WP_005875392.1; NC_002950.2.
DR PDB; 2IQT; X-ray; 2.46 A; A=1-293.
DR PDBsum; 2IQT; -.
DR AlphaFoldDB; P60053; -.
DR SMR; P60053; -.
DR STRING; 242619.PG_1755; -.
DR EnsemblBacteria; AAQ66757; AAQ66757; PG_1755.
DR KEGG; pgi:PG_1755; -.
DR PATRIC; fig|242619.8.peg.1622; -.
DR eggNOG; COG3588; Bacteria.
DR HOGENOM; CLU_081560_0_0_10; -.
DR OMA; GVFGTKM; -.
DR OrthoDB; 945470at2; -.
DR BioCyc; PGIN242619:G1G02-1636-MON; -.
DR UniPathway; UPA00109; UER00183.
DR EvolutionaryTrace; P60053; -.
DR Proteomes; UP000000588; Chromosome.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd00949; FBP_aldolase_I_bact; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00729; FBP_aldolase_1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR InterPro; IPR023014; FBA_I_Gram+-type.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycolysis; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..293
FT /note="Fructose-bisphosphate aldolase class 1"
FT /id="PRO_0000216902"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00729"
FT ACT_SITE 211
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00729"
FT HELIX 1..11
FT /evidence="ECO:0007829|PDB:2IQT"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:2IQT"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:2IQT"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:2IQT"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2IQT"
FT HELIX 43..59
FT /evidence="ECO:0007829|PDB:2IQT"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:2IQT"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:2IQT"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:2IQT"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2IQT"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:2IQT"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:2IQT"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:2IQT"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:2IQT"
FT HELIX 149..167
FT /evidence="ECO:0007829|PDB:2IQT"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:2IQT"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:2IQT"
FT HELIX 186..203
FT /evidence="ECO:0007829|PDB:2IQT"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:2IQT"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:2IQT"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:2IQT"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:2IQT"
FT HELIX 242..249
FT /evidence="ECO:0007829|PDB:2IQT"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:2IQT"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:2IQT"
FT HELIX 273..292
FT /evidence="ECO:0007829|PDB:2IQT"
SQ SEQUENCE 293 AA; 32987 MW; 8BF85BFF649DCE93 CRC64;
MNKEQLQQMR QAPGFVGALD QSGGSTPKAL KAYGIQPDAY QSEEEMFDLI HQMRTRMITS
PAFATGKIIG VILFERTMRG KIEGMPTADF LWEKRHIVPF LKVDKGLQDE ANGVQLMKPF
PELGKLCEEA VGYHVFGTKM RSVIKQANEQ GIRDIVEQQF QWGKEILSHG LVPILEPEVD
IHCPEKAKAE EILKRELLAQ LDKMTEPVML KITIPTVDNF YKEIIEHPMM LRVVALSGGY
SREQANELLS RNHGVIASFS RALVEGLSAR QTDAEFNAML EASIEDVYQA SIK
