ID   ALKH_HAEIN              Reviewed;         212 AA.
AC   P44480;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Putative KHG/KDPG aldolase;
DE   Includes:
DE     RecName: Full=4-hydroxy-2-oxoglutarate aldolase;
DE              EC=4.1.3.16;
DE     AltName: Full=2-keto-4-hydroxyglutarate aldolase;
DE              Short=KHG-aldolase;
DE   Includes:
DE     RecName: Full=2-dehydro-3-deoxy-phosphogluconate aldolase;
DE              EC=4.1.2.14;
DE     AltName: Full=2-keto-3-deoxy-6-phosphogluconate aldolase;
DE              Short=KDPG-aldolase;
DE     AltName: Full=Phospho-2-dehydro-3-deoxygluconate aldolase;
DE     AltName: Full=Phospho-2-keto-3-deoxygluconate aldolase;
GN   Name=eda; OrderedLocusNames=HI_0047;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 2-212.
RX   PubMed=16021622; DOI=10.1002/prot.20541;
RA   Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA   Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA   Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA   Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA   Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA   Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA   Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA   Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA   Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT   "Structural analysis of a set of proteins resulting from a bacterial
RT   genomics project.";
RL   Proteins 60:787-796(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4S)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate;
CC         Xref=Rhea:RHEA:35639, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:71685; EC=4.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4R)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate;
CC         Xref=Rhea:RHEA:30687, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:62213; EC=4.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-dehydro-3-deoxy-6-phospho-D-gluconate = D-glyceraldehyde 3-
CC         phosphate + pyruvate; Xref=Rhea:RHEA:17089, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:57569, ChEBI:CHEBI:59776; EC=4.1.2.14;
CC   -!- PATHWAY: Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate
CC       degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-
CC       3-deoxy-D-gluconate: step 2/2.
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate and dicarboxylate
CC       metabolism.
CC   -!- SUBUNIT: Homotrimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the KHG/KDPG aldolase family. {ECO:0000305}.
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DR   EMBL; L42023; AAC21725.1; -; Genomic_DNA.
DR   PIR; A64045; A64045.
DR   RefSeq; NP_438220.1; NC_000907.1.
DR   PDB; 1VHC; X-ray; 1.89 A; A/B/C/D/E/F=2-212.
DR   PDBsum; 1VHC; -.
DR   AlphaFoldDB; P44480; -.
DR   SMR; P44480; -.
DR   STRING; 71421.HI_0047; -.
DR   EnsemblBacteria; AAC21725; AAC21725; HI_0047.
DR   KEGG; hin:HI_0047; -.
DR   PATRIC; fig|71421.8.peg.47; -.
DR   eggNOG; COG0800; Bacteria.
DR   HOGENOM; CLU_077795_1_1_6; -.
DR   OrthoDB; 9805177at2; -.
DR   PhylomeDB; P44480; -.
DR   BioCyc; HINF71421:G1GJ1-48-MONOMER; -.
DR   UniPathway; UPA00227; -.
DR   UniPathway; UPA00856; UER00829.
DR   EvolutionaryTrace; P44480; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0106009; F:(4S)-4-hydroxy-2-oxoglutarate aldolase activity; IEA:RHEA.
DR   GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008700; F:4-hydroxy-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00452; KDPG_aldolase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR000887; Aldlse_KDPG_KHG.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR031337; KDPG/KHG_AS_1.
DR   InterPro; IPR031338; KDPG/KHG_AS_2.
DR   NCBIfam; TIGR01182; eda; 1.
DR   PANTHER; PTHR30246; 2-KETO-3-DEOXY-6-PHOSPHOGLUCONATE ALDOLASE; 1.
DR   PANTHER; PTHR30246:SF2; KHG_KDPG ALDOLASE; 1.
DR   Pfam; PF01081; Aldolase; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00159; ALDOLASE_KDPG_KHG_1; 1.
DR   PROSITE; PS00160; ALDOLASE_KDPG_KHG_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Lyase; Multifunctional enzyme; Reference proteome;
KW   Schiff base.
FT   CHAIN           1..212
FT                   /note="Putative KHG/KDPG aldolase"
FT                   /id="PRO_0000201041"
FT   ACT_SITE        45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10118"
FT   ACT_SITE        49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10118"
FT   ACT_SITE        133
FT                   /note="Schiff-base intermediate with KHG or pyruvate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10118"
FT   HELIX           5..15
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   STRAND          17..21
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   HELIX           26..28
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   HELIX           29..38
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   STRAND          43..47
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   HELIX           53..63
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   HELIX           77..86
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   STRAND          89..92
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   HELIX           98..106
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   HELIX           118..126
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   STRAND          131..134
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   TURN            135..141
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   HELIX           142..150
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   TURN            151..155
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   STRAND          157..163
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   TURN            166..168
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   HELIX           169..173
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   STRAND          181..183
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   HELIX           185..187
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   HELIX           189..193
FT                   /evidence="ECO:0007829|PDB:1VHC"
FT   HELIX           197..211
FT                   /evidence="ECO:0007829|PDB:1VHC"
SQ   SEQUENCE   212 AA;  22861 MW;  1D920F34AB4C14E3 CRC64;
     MSYTTQQIIE KLRELKIVPV IALDNADDIL PLADTLAKNG LSVAEITFRS EAAADAIRLL
     RANRPDFLIA AGTVLTAEQV VLAKSSGADF VVTPGLNPKI VKLCQDLNFP ITPGVNNPMA
     IEIALEMGIS AVKFFPAEAS GGVKMIKALL GPYAQLQIMP TGGIGLHNIR DYLAIPNIVA
     CGGSWFVEKK LIQSNNWDEI GRLVREVIDI IK
//