ID   ALF1_CHLTR              Reviewed;         348 AA.
AC   O84217;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Probable fructose-bisphosphate aldolase class 1;
DE            EC=4.1.2.13;
DE   AltName: Full=Probable fructose-bisphosphate aldolase class I;
DE            Short=FBP aldolase;
GN   Name=fbaB; OrderedLocusNames=CT_215;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. FbaB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE001273; AAC67807.1; -; Genomic_DNA.
DR   PIR; F71542; F71542.
DR   RefSeq; NP_219719.1; NC_000117.1.
DR   RefSeq; WP_009871561.1; NC_000117.1.
DR   AlphaFoldDB; O84217; -.
DR   SMR; O84217; -.
DR   STRING; 272561.CT_215; -.
DR   EnsemblBacteria; AAC67807; AAC67807; CT_215.
DR   GeneID; 884913; -.
DR   KEGG; ctr:CT_215; -.
DR   PATRIC; fig|272561.5.peg.230; -.
DR   HOGENOM; CLU_057069_0_0_0; -.
DR   InParanoid; O84217; -.
DR   OrthoDB; 9769559at2; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd00958; DhnA; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR041720; FbaB-like.
DR   PANTHER; PTHR47916:SF1; 3-HYDROXY-5-PHOSPHONOOXYPENTANE-2,4-DIONE THIOLASE-RELATED; 1.
DR   PANTHER; PTHR47916; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   SMART; SM01133; DeoC; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..348
FT                   /note="Probable fructose-bisphosphate aldolase class 1"
FT                   /id="PRO_0000138943"
FT   ACT_SITE        236
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   348 AA;  37988 MW;  D68CA2CDB498A752 CRC64;
     MTTIFDLLGK DADYLLNHKC VIKKEALTLP SGDLVSRVFA ESDRNNRVLR SLQQMFSCGR
     LGGTGYLSIL PVDQGVEHTA GASFAKNPMY FDPENIVRLA MEAGCSAVAS SYGVLSILAR
     RYAHKIPFLL KLNHNELLSY PTTYHQIFFS QVEDAYNMGA VAVGATIYFG SESSSEEIVA
     VAEAFARARE LGLATVLWCY LRNPHFVVNN VDYHTAADLT GQADHLGATL GADIVKQKLP
     TLQGGFKTIN FSKTDDLVYS ELSSNHPIDL CRYQVLNSYC GKVGLINSGG PSGQDDFAEA
     VKTAVINKRA GGMGLILGRK AFQRPFSEGV RLLNLIQDIY LDPTISIS
//