ALKH_HAEIN
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 03-AUG-2022, entry version 132.
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; Proteobacteria; 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 RefSeq; WP_005693874.1; 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 OMA; WQEIGRL; -.
DR PhylomeDB; P44480; -.
DR BioCyc; HINF71421:G1GJ1-48-MON; -.
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; -; 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 PANTHER; PTHR30246; PTHR30246; 1.
DR Pfam; PF01081; Aldolase; 1.
DR TIGRFAMs; TIGR01182; eda; 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
