ID A0A024K1Z6_9MYCO Unreviewed; 441 AA.
AC A0A024K1Z6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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 Name=thrA {ECO:0000313|EMBL:CDO89946.1};
GN ORFNames=BN973_04336 {ECO:0000313|EMBL:CDO89946.1};
OS Mycobacterium triplex.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=47839 {ECO:0000313|EMBL:CDO89946.1};
RN [1] {ECO:0000313|EMBL:CDO89946.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO89946.1};
RX PubMed=24874681; DOI=10.1128/genomeA.00499-14;
RA Sassi M., Croce O., Robert C., Raoult D., Drancourt M.;
RT "Draft Genome Sequence of Mycobacterium triplex DSM 44626.";
RL Genome Announc. Announc.2:e00499-e00414(2014).
RN [2] {ECO:0000313|EMBL:CDO89946.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO89946.1};
RA Urmite Genomes U.;
RL Submitted (APR-2014) 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}.
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DR EMBL; HG964446; CDO89946.1; -; Genomic_DNA.
DR RefSeq; WP_036470716.1; NZ_LQPY01000012.1.
DR AlphaFoldDB; A0A024K1Z6; -.
DR STRING; 47839.BN973_04336; -.
DR eggNOG; COG0460; Bacteria.
DR HOGENOM; CLU_009116_1_0_11; -.
DR OrthoDB; 9808167at2; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
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 Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697,
KW ECO:0000256|RuleBase:RU000579}.
FT DOMAIN 356..435
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 207
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT BINDING 13..20
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 107
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ SEQUENCE 441 AA; 45543 MW; 444AFCBA37132206 CRC64;
MSGNGKPVGV AVLGCGNVGS EVVRIIEQSA DDLAARVGAP LALRGIGVRR VAADRGVPVE
LLTDNVEELV SREDVDIVVE LMGPVEPSRK AILAALEHGK SVVTANKALL ATSTGELAQA
AENAHVDLYF EAAVAGAIPV IRPLTQSLAG DTVVRVAGIV NGTTNYILSA MDSTGTDYDS
ALADASALGY AEADPTADVE GYDAAAKAAI LASIAFHTRV TADDVYREGI TKITPADFAS
AHALGCTIKL LSICERITTD DGQQRVSARV YPALVPLEHP LATVNGAFNA VVVEAEAAGR
LMFYGQGAGG APTASAVTGD LVMAARNRVL GSRGPKESKY AQLPIAPMGF ISTRYYVSMN
VADKPGVLSS VAAEFAKREV SIAEVRQEGV ADEGGRRVGA RVVVVTHSAT DAALSETVDA
LADLDVVQRV ASVLRLEGTS I
//
