ID A0A0D5NLN9_9BACL Unreviewed; 428 AA.
AC A0A0D5NLN9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|RuleBase:RU000579};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|RuleBase:RU000579};
GN ORFNames=VN24_17805 {ECO:0000313|EMBL:AJY76075.1};
OS Paenibacillus beijingensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1126833 {ECO:0000313|EMBL:AJY76075.1, ECO:0000313|Proteomes:UP000032633};
RN [1] {ECO:0000313|EMBL:AJY76075.1, ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|EMBL:AJY76075.1,
RC ECO:0000313|Proteomes:UP000032633};
RX PubMed=25937453; DOI=10.1016/j.jbiotec.2015.04.015;
RA Kwak Y., Shin J.H.;
RT "Complete genome sequence of Paenibacillus beijingensis 7188(T) (=DSM
RT 24997(T)), a novel rhizobacterium from jujube garden soil.";
RL J. Biotechnol. 206:75-76(2015).
RN [2] {ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|Proteomes:UP000032633};
RA Kwak Y., Shin J.-H.;
RT "Genome sequence of Paenibacillus beijingensis strain DSM 24997T.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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|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|RuleBase:RU000579}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5. {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; CP011058; AJY76075.1; -; Genomic_DNA.
DR RefSeq; WP_045671503.1; NZ_CP011058.1.
DR AlphaFoldDB; A0A0D5NLN9; -.
DR STRING; 1126833.VN24_17805; -.
DR KEGG; pbj:VN24_17805; -.
DR PATRIC; fig|1126833.4.peg.3910; -.
DR HOGENOM; CLU_009116_1_0_9; -.
DR OrthoDB; 9808167at2; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000032633; 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|RuleBase:RU000579};
KW Methionine biosynthesis {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:UP000032633};
KW Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT DOMAIN 350..425
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT BINDING 9..16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 105
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ SEQUENCE 428 AA; 46307 MW; 2BD2E62263BB184C CRC64;
MKPVKVGLLG LGTVGTGVVR IVEGHQEDLR SQVGSPIVIE KVLVQNKDKA RSISIDASKL
TEDVADIIYN PDIDVVVEVM GGIEHTKQHI LEALSRGKHV VTANKDLMAL HGQEILAKAA
ENRCDVFYEA SVAGGIPIIR TLIEGFSSDR ITKIMGIVNG TTNYILTKMS QEGASYLDVL
KEAQQLGYAE ADPTSDVEGL DAARKMTILA RLGFRAEFAL EDVSVQGISG VSKEDILYAK
RLGYEVKLLG IAERSDDQIA VSVQPTMVKQ SHPIASVNGV FNAVYVHGEA VGETMFYGAG
AGELPTATSI VADLVAVVKN LKIGVNGLQD VASYKETKLK TDEQISSKYF LLLHVDDKAG
VLARITQVFA EYEVSLESVL QQPNPHNPEA EIIVITHDAN KAAMNKVLQA FDSLEVIRKV
KSIYRVEG
//
