ID A0A1J4MZ30_9ACTN Unreviewed; 437 AA.
AC A0A1J4MZ30;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=UG56_022325 {ECO:0000313|EMBL:OIJ24531.1};
OS Nocardioides luteus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1844 {ECO:0000313|EMBL:OIJ24531.1, ECO:0000313|Proteomes:UP000033772};
RN [1] {ECO:0000313|EMBL:OIJ24531.1, ECO:0000313|Proteomes:UP000033772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAFB {ECO:0000313|EMBL:OIJ24531.1,
RC ECO:0000313|Proteomes:UP000033772};
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OIJ24531.1, ECO:0000313|Proteomes:UP000033772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAFB {ECO:0000313|EMBL:OIJ24531.1,
RC ECO:0000313|Proteomes:UP000033772};
RA Brown L., Ruiz O.N., Gunasekera T.;
RT "Draft Genome Sequence of Nocardioides luteus Strain BAFB, an Alkane-
RT Degrading Bacterium Isolated from JP-7 Polluted Soil.";
RL Submitted (OCT-2016) 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|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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OIJ24531.1}.
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DR EMBL; JZDQ02000037; OIJ24531.1; -; Genomic_DNA.
DR RefSeq; WP_071327261.1; NZ_JZDQ02000037.1.
DR AlphaFoldDB; A0A1J4MZ30; -.
DR STRING; 1844.UG56_022325; -.
DR OrthoDB; 9808167at2; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000033772; Unassembled WGS sequence.
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:UP000033772};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697,
KW ECO:0000256|RuleBase:RU000579}.
FT DOMAIN 359..432
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT BINDING 19..26
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 115
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ SEQUENCE 437 AA; 45142 MW; 37AC40C370DD7FEC CRC64;
MSSNKTTAHA VKPLGVAVLG CGVVGSQVVR LLLEGDADLA ARVGAPLEIR GVAVRRLDAP
RDVEVPAELL TTDAHGLVAR DDVDLVVEVI GGIEPARGLI LKALESGASV VTANKALLAE
DGPTLYEAAE KAGTDLYYEA AVAGAIPILR PLRDSLVGDH VTKVMGIVNG TTNYILDKMD
TYGAGFEEAL AEAQELGYAE ADPTADVEGF DAAAKAAILA SLAFHTRVTA SDVYREGITE
VTAGDVASAK AMGSVVKLLA IAELDGDDVS ARVHPVMIPR THALATVRGA YNAVFVESAS
AGDLMFYGQG AGGEPTASAV LGDLVTIGRN KALGARGFGE SAYAARAVRP MGETVTRYHV
SLDVADKAGV LAAVATAFSE HGVSIKAVRQ EGRGEDAQLV VVSHEAPDAA LAATVQHLRE
MEYVRDVASV MRVEGAV
//
