DHOM_PSEAE
ID DHOM_PSEAE Reviewed; 434 AA.
AC P29365;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Homoserine dehydrogenase;
DE Short=HDH;
DE EC=1.1.1.3;
GN Name=hom; OrderedLocusNames=PA3736;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=1333566; DOI=10.1111/j.1365-2958.1992.tb01768.x;
RA Clepet C., Borne F., Krishnapillai V., Baird C., Patte J.-C., Cami B.;
RT "Isolation, organization and expression of the Pseudomonas aeruginosa
RT threonine genes.";
RL Mol. Microbiol. 6:3109-3119(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADH; Xref=Rhea:RHEA:15757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC -!- ACTIVITY REGULATION: Feedback inhibition by threonine.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5.
CC -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA46167.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X65033; CAA46167.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE004091; AAG07123.1; -; Genomic_DNA.
DR PIR; H83179; H83179.
DR PIR; S27979; DEPSHA.
DR RefSeq; NP_252425.1; NC_002516.2.
DR RefSeq; WP_003109642.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; P29365; -.
DR SMR; P29365; -.
DR STRING; 287.DR97_4141; -.
DR PaxDb; P29365; -.
DR PRIDE; P29365; -.
DR DNASU; 880337; -.
DR EnsemblBacteria; AAG07123; AAG07123; PA3736.
DR GeneID; 880337; -.
DR KEGG; pae:PA3736; -.
DR PATRIC; fig|208964.12.peg.3908; -.
DR PseudoCAP; PA3736; -.
DR HOGENOM; CLU_009116_1_0_6; -.
DR InParanoid; P29365; -.
DR OMA; LMFYGPG; -.
DR PhylomeDB; P29365; -.
DR BioCyc; PAER208964:G1FZ6-3807-MON; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IDA:PseudoCAP.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IDA:PseudoCAP.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR016204; HDH.
DR InterPro; IPR001342; HDH_cat.
DR InterPro; IPR019811; HDH_CS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF00742; Homoserine_dh; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR PIRSF; PIRSF000098; Homoser_dehydrog; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Isoleucine biosynthesis; Methionine biosynthesis; NADP; Oxidoreductase;
KW Reference proteome; Threonine biosynthesis.
FT CHAIN 1..434
FT /note="Homoserine dehydrogenase"
FT /id="PRO_0000066703"
FT DOMAIN 353..429
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 9..16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 81..85
FT /note="YTLAH -> PPWPI (in Ref. 1; CAA46167)"
FT /evidence="ECO:0000305"
FT CONFLICT 187..190
FT /note="AEAD -> GRGRS (in Ref. 1; CAA46167)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="H -> T (in Ref. 1; CAA46167)"
FT /evidence="ECO:0000305"
FT CONFLICT 210..214
FT /note="IAFGI -> MLRH (in Ref. 1; CAA46167)"
FT /evidence="ECO:0000305"
FT CONFLICT 276..277
FT /note="NG -> TA (in Ref. 1; CAA46167)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="R -> H (in Ref. 1; CAA46167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 46224 MW; 68770627B8AD9746 CRC64;
MKPVKVGICG LGTVGGGTFN VLERNAEEIA RRAGRGIEVA QIAARRPNPK CDTGATPITA
DIFDVACNPE IDVVVELIGG YTLAHELVLK AIENGKHVVT ANKALIAVHG NEIFAKAREK
GVIVAFEAAV AGGIPVIKAI REGLSANRIN WLAGIINGTG NFILSEMREK GRTFPDVLAE
AQALGYAEAD PTFDVEGIDA AHKLTILASI AFGIPLQFDK AYTEGISKLT SADVNYADAL
GYRIKHLGVA RRTESGFELR VHPTLIPSDR LIANVNGVMN AVMVNGDAVG STLYYGAGAG
MEPTASSVVA DLVDVVRAMT SDPENRVPHL AFQPDALSDH PILPIEACES AYYLRIQAKD
HPGVLAQVAT ILSERGINIE SIMQKEAEEQ DGLVPMILVT HRVIEQRIND AIAALEALEG
VSGPVVRIRV EQLN
