ID   ALF1_CHLMU              Reviewed;         349 AA.
AC   Q9PKH8;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=TC_0487;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39333.1; -; Genomic_DNA.
DR   PIR; G81697; G81697.
DR   RefSeq; WP_010230582.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PKH8; -.
DR   SMR; Q9PKH8; -.
DR   STRING; 243161.TC_0487; -.
DR   EnsemblBacteria; AAF39333; AAF39333; TC_0487.
DR   GeneID; 1245845; -.
DR   KEGG; cmu:TC_0487; -.
DR   eggNOG; COG1830; Bacteria.
DR   HOGENOM; CLU_057069_0_0_0; -.
DR   OMA; FVKVNYP; -.
DR   OrthoDB; 1560751at2; -.
DR   Proteomes; UP000000800; 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; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR041720; FbaB-like.
DR   Pfam; PF01791; DeoC; 1.
DR   SMART; SM01133; DeoC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; Lyase; Schiff base.
FT   CHAIN           1..349
FT                   /note="Probable fructose-bisphosphate aldolase class 1"
FT                   /id="PRO_0000138941"
FT   ACT_SITE        236
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   349 AA;  38226 MW;  EFFC4F47708E2686 CRC64;
     MTTILDLLGK DADYLLNHQC IIKKEALTLP SGDFVSRVFA ESDRNNRVLR SLQQMFDHGR
     LGGSGYLSIL PVDQGVEHTA GASFAKNPMY FDPENIVRLA IESGCSAVAS SYGVLSILAR
     RYAHKIPFLL KLNHNELLSY PTTYHQIFFS QVEDAYNMGA VAVGATVYFG SESSNEEIVS
     VAKAFSRARE LGLATVLWCY LRNPHFTRNG VDYHTAADLT GQADHLGATL GADIVKQKLP
     TLQEGFKTIN FSKTDDLVYS ELSSNHPIDL CRYQVLNSYC GKVGLINSGG PSSGQNDFTE
     AAKTAVINKR AGGMGLILGR KAFQRPFSEG VQLLNLIQDI YLDPTISIS