KDSA_HAEIN
ID KDSA_HAEIN Reviewed; 284 AA.
AC P45251;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase;
DE EC=2.5.1.55;
DE AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase;
DE AltName: Full=KDO-8-phosphate synthase;
DE Short=KDO 8-P synthase;
DE Short=KDOPS;
DE AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase;
GN Name=kdsA; OrderedLocusNames=HI_1557;
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-
CC alpha-D-manno-2-octulosonate-8-phosphate + phosphate;
CC Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;
CC -!- PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate
CC biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate:
CC step 2/3.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000305}.
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DR EMBL; L42023; AAC23206.1; -; Genomic_DNA.
DR PIR; G64129; G64129.
DR RefSeq; NP_439706.1; NC_000907.1.
DR RefSeq; WP_005693586.1; NC_000907.1.
DR PDB; 1O60; X-ray; 1.80 A; A/B/C/D=1-284.
DR PDBsum; 1O60; -.
DR AlphaFoldDB; P45251; -.
DR SMR; P45251; -.
DR STRING; 71421.HI_1557; -.
DR EnsemblBacteria; AAC23206; AAC23206; HI_1557.
DR KEGG; hin:HI_1557; -.
DR PATRIC; fig|71421.8.peg.1628; -.
DR eggNOG; COG2877; Bacteria.
DR HOGENOM; CLU_036666_0_0_6; -.
DR OMA; FRGIPTM; -.
DR PhylomeDB; P45251; -.
DR BioCyc; HINF71421:G1GJ1-1577-MON; -.
DR BRENDA; 2.5.1.55; 2529.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR EvolutionaryTrace; P45251; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008676; F:3-deoxy-8-phosphooctulonate synthase activity; IBA:GO_Central.
DR GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0046364; P:monosaccharide biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00056; KDO8P_synth; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006269; KDO8P_synthase.
DR PANTHER; PTHR21057; PTHR21057; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR TIGRFAMs; TIGR01362; KDO8P_synth; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipopolysaccharide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..284
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT /id="PRO_0000187131"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:1O60"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1O60"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:1O60"
FT HELIX 31..48
FT /evidence="ECO:0007829|PDB:1O60"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:1O60"
FT HELIX 74..88
FT /evidence="ECO:0007829|PDB:1O60"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1O60"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1O60"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:1O60"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:1O60"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1O60"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:1O60"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:1O60"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1O60"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:1O60"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:1O60"
FT HELIX 183..190
FT /evidence="ECO:0007829|PDB:1O60"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:1O60"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:1O60"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:1O60"
FT STRAND 234..243
FT /evidence="ECO:0007829|PDB:1O60"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1O60"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:1O60"
FT HELIX 260..276
FT /evidence="ECO:0007829|PDB:1O60"
SQ SEQUENCE 284 AA; 30921 MW; 7A3D2076A9B011B0 CRC64;
MQNKIVKIGN IDVANDKPFV LFGGMNVLES RDMAMQVCEA YVKVTEKLGV PYVFKASFDK
ANRSSIHSYR GPGMEEGLKI FQELKDTFGV KIITDVHEIY QCQPVADVVD IIQLPAFLAR
QTDLVEAMAK TGAVINVKKP QFLSPSQMGN IVEKIEECGN DKIILCDRGT NFGYDNLIVD
MLGFSVMKKA SKGSPVIFDV THSLQCRDPF GAASSGRRAQ VTELARSGLA VGIAGLFLEA
HPNPNQAKCD GPSALPLSAL EGFVSQMKAI DDLVKSFPEL DTSI
