DHOM_BACSU
ID DHOM_BACSU Reviewed; 433 AA.
AC P19582; O32122; P70991;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Homoserine dehydrogenase;
DE Short=HDH;
DE EC=1.1.1.3;
GN Name=hom; Synonyms=tdm; OrderedLocusNames=BSU32260;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP AND PATHWAY.
RC STRAIN=168;
RX PubMed=3139660; DOI=10.1016/s0021-9258(18)68087-1;
RA Parsot C., Cohen G.N.;
RT "Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding
RT for homoserine dehydrogenase. Structural and evolutionary relationships
RT with Escherichia coli aspartokinases-homoserine dehydrogenases I and II.";
RL J. Biol. Chem. 263:14654-14660(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 353-433.
RC STRAIN=168;
RX PubMed=3098560; DOI=10.1002/j.1460-2075.1986.tb04600.x;
RA Parsot C.;
RT "Evolution of biosynthetic pathways: a common ancestor for threonine
RT synthase, threonine dehydratase and D-serine dehydratase.";
RL EMBO J. 5:3013-3019(1986).
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:0000269|PubMed:3139660};
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:0000269|PubMed:3139660};
CC -!- ACTIVITY REGULATION: Feedback inhibition by threonine.
CC {ECO:0000269|PubMed:3139660}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC {ECO:0000269|PubMed:3139660}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5. {ECO:0000269|PubMed:3139660}.
CC -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M23217; AAA50609.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15216.1; -; Genomic_DNA.
DR EMBL; X04603; CAA28269.1; -; Genomic_DNA.
DR PIR; A31973; DEECHS.
DR RefSeq; NP_391106.1; NC_000964.3.
DR RefSeq; WP_003228694.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P19582; -.
DR SMR; P19582; -.
DR IntAct; P19582; 4.
DR STRING; 224308.BSU32260; -.
DR PaxDb; P19582; -.
DR PRIDE; P19582; -.
DR EnsemblBacteria; CAB15216; CAB15216; BSU_32260.
DR GeneID; 936654; -.
DR KEGG; bsu:BSU32260; -.
DR PATRIC; fig|224308.179.peg.3492; -.
DR eggNOG; COG0460; Bacteria.
DR InParanoid; P19582; -.
DR OMA; LMFYGPG; -.
DR PhylomeDB; P19582; -.
DR BioCyc; BSUB:BSU32260-MON; -.
DR BRENDA; 1.1.1.3; 658.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR PRO; PR:P19582; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Isoleucine biosynthesis; Methionine biosynthesis; NADP; Oxidoreductase;
KW Reference proteome; Threonine biosynthesis.
FT CHAIN 1..433
FT /note="Homoserine dehydrogenase"
FT /id="PRO_0000066692"
FT DOMAIN 350..426
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT ACT_SITE 205
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 105
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 375
FT /note="S -> T (in Ref. 3; CAA28269)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="E -> Q (in Ref. 1; AAA50609)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 47494 MW; 03E9DF7727D62696 CRC64;
MKAIRVGLLG LGTVGSGVVK IIQDHQDKLM HQVGCPVTIK KVLVKDLEKK REVDLPKEVL
TTEVYDVIDD PDVDVVIEVI GGVEQTKQYL VDALRSKKHV VTANKDLMAV YGSELLAEAK
ENGCDIYFEA SVAGGIPILR TLEEGLSSDR ITKMMGIVNG TTNFILTKMI KEKSPYEEVL
KEAQDLGFAE ADPTSDVEGL DAARKMAILA RLGFSMNVDL EDVKVKGISQ ITDEDISFSK
RLGYTMKLIG IAQRDGSKIE VSVQPTLLPD HHPLSAVHNE FNAVYVYGEA VGETMFYGPG
AGSMPTATSV VSDLVAVMKN MRLGVTGNSF VGPQYEKNMK SPSDIYAQQF LRIHVKDEVG
SFSKITSVFS ERGVSFEKIL QLPIKGHDEL AEIVIVTHHT SEADFSDILQ NLNDLEVVQE
VKSTYRVEGN GWS
