ID D9Q9T8_CORP2 Unreviewed; 449 AA.
AC D9Q9T8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013376, ECO:0000256|RuleBase:RU000579};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|RuleBase:RU000579};
GN ORFNames=CPC231_04190 {ECO:0000313|EMBL:ADL10314.1};
OS Corynebacterium pseudotuberculosis (strain C231).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=681645 {ECO:0000313|EMBL:ADL10314.1, ECO:0000313|Proteomes:UP000000276};
RN [1] {ECO:0000313|EMBL:ADL10314.1, ECO:0000313|Proteomes:UP000000276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C231 {ECO:0000313|EMBL:ADL10314.1,
RC ECO:0000313|Proteomes:UP000000276};
RX PubMed=21037006; DOI=.1128/JB.01211-10;
RG Consortium: Rede Paraense de Genomica e Proteomica (RPGP);
RA Silva A., Schneider M.P., Cerdeira L., Barbosa M.S., Ramos R.T.,
RA Carneiro A.R., Santos R., Lima M., D'Afonseca V., Almeida S.S.,
RA Santos A.R., Soares S.C., Pinto A.C., Ali A., Dorella F.A., Rocha F.,
RA de Abreu V.A., Trost E., Tauch A., Shpigel N., Miyoshi A., Azevedo V.;
RT "Complete genome sequence of Corynebacterium pseudotuberculosis I19, a
RT strain isolated from a cow in Israel with bovine mastitis.";
RL J. Bacteriol. 193:323-324(2011).
RN [2] {ECO:0000313|EMBL:ADL10314.1, ECO:0000313|Proteomes:UP000000276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C231 {ECO:0000313|EMBL:ADL10314.1,
RC ECO:0000313|Proteomes:UP000000276};
RX PubMed=21533164; DOI=10.1371/journal.pone.0018551;
RA Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R.,
RA Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P., Turk M.Z.,
RA Seyffert N., Moraes P.M., Soares S.C., Almeida S.S., Castro T.L.,
RA Abreu V.A., Trost E., Baumbach J., Tauch A., Schneider M.P., McCulloch J.,
RA Cerdeira L.T., Ramos R.T., Zerlotini A., Dominitini A., Resende D.M.,
RA Coser E.M., Oliveira L.M., Pedrosa A.L., Vieira C.U., Guimaraes C.T.,
RA Bartholomeu D.C., Oliveira D.M., Santos F.R., Rabelo E.M., Lobo F.P.,
RA Franco G.R., Costa A.F., Castro I.M., Dias S.R., Ferro J.A., Ortega J.M.,
RA Paiva L.V., Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P.,
RA Falcao P.R., Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C.,
RA Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.;
RT "Evidence for reductive genome evolution and lateral acquisition of
RT virulence functions in two Corynebacterium pseudotuberculosis strains.";
RL PLoS ONE 6:E18551-E18551(2011).
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 Evidence={ECO:0000256|ARBA:ARBA00001406};
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 Evidence={ECO:0000256|ARBA:ARBA00000116,
CC ECO:0000256|RuleBase:RU000579};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00005062, ECO:0000256|RuleBase:RU000579}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5. {ECO:0000256|ARBA:ARBA00005056,
CC ECO:0000256|RuleBase:RU000579}.
CC -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006753, ECO:0000256|RuleBase:RU004171}.
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DR EMBL; CP001829; ADL10314.1; -; Genomic_DNA.
DR RefSeq; WP_013241689.1; NC_017301.2.
DR AlphaFoldDB; D9Q9T8; -.
DR STRING; 681645.CpC231_0833; -.
DR GeneID; 69459955; -.
DR KEGG; cpq:CPC231_04190; -.
DR PATRIC; fig|681645.3.peg.864; -.
DR eggNOG; COG0460; Bacteria.
DR HOGENOM; CLU_009116_1_0_11; -.
DR OrthoDB; 9808167at2; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000000276; Chromosome.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniPathway.
DR CDD; cd04881; ACT_HSDH-Hom; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 PANTHER; PTHR43331; HOMOSERINE DEHYDROGENASE; 1.
DR PANTHER; PTHR43331:SF1; HOMOSERINE DEHYDROGENASE; 1.
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; SSF55021; ACT-like; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU000579};
KW Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU000579};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624,
KW ECO:0000256|RuleBase:RU000579};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167,
KW ECO:0000256|RuleBase:RU000579};
KW NADP {ECO:0000256|PIRSR:PIRSR000098-2, ECO:0000256|RuleBase:RU000579};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000579};
KW Reference proteome {ECO:0000313|Proteomes:UP000000276};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697,
KW ECO:0000256|RuleBase:RU000579}.
FT DOMAIN 372..445
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 223
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT BINDING 26..33
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 123
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ SEQUENCE 449 AA; 47001 MW; C85CDCDB488559A3 CRC64;
MSTEQHISAT FNPGKGEGAP VGIAILGYGT VGSQVLRLLT ENASDFKSRS GGPLEIKGVA
ASSKEKHKGS LADTLGVLTD DARSLIERED VDIVVEVIGG IDYPRELILK ALRSGKSVVT
ANKALVAAHS AELAQAADEA GVDLYFEAAV AAAIPVVGPL RRSLAGDQVQ SVAGIVNGTT
NFILDAMDST GASYDDMLAE ATRLGYAEAD PTADVEGHDA ASKAAILASL AFHTRVTSDD
VHCEGISKIT AKDIEAAKQA GYTIKLLAIC ERLQRENGEE KVSARVHPTL VPRSHPLASV
SKSFNAVFVE AEAAGRLMLY GNGAGGNPTA SAVLGDIVGA ARNKVFGGRA PGESTYANLP
IASFGEVLTR FHIDMEVEDR VGVLADLAQI FAKNGISLST IRQEEKDGHA RLIVVTHTAL
EADLEKTVEN IKDSDAVKQI SSVIRLVGE
//
