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Database: UniProt
Entry: L1NJM8_9NEIS
LinkDB: L1NJM8_9NEIS
Original site: L1NJM8_9NEIS 
ID   L1NJM8_9NEIS            Unreviewed;       436 AA.
AC   L1NJM8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE            EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN   ORFNames=HMPREF9120_02591 {ECO:0000313|EMBL:EKY03729.1};
OS   Neisseria sp. oral taxon 020 str. F0370.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=1127694 {ECO:0000313|EMBL:EKY03729.1, ECO:0000313|Proteomes:UP000010457};
RN   [1] {ECO:0000313|EMBL:EKY03729.1, ECO:0000313|Proteomes:UP000010457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0370 {ECO:0000313|EMBL:EKY03729.1,
RC   ECO:0000313|Proteomes:UP000010457};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-2012) 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   -!- 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:EKY03729.1}.
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DR   EMBL; AMER01000199; EKY03729.1; -; Genomic_DNA.
DR   RefSeq; WP_009427245.1; NZ_KB291153.1.
DR   AlphaFoldDB; L1NJM8; -.
DR   STRING; 1127694.HMPREF9120_02591; -.
DR   PATRIC; fig|1127694.3.peg.2407; -.
DR   HOGENOM; CLU_009116_1_0_4; -.
DR   OrthoDB; 9808167at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000010457; 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: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   NADP {ECO:0000256|PIRSR:PIRSR000098-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010457}.
FT   DOMAIN          355..430
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   436 AA;  46728 MW;  C5D7BA6BC1C973F7 CRC64;
     MKPVRIGILG LGTVGSGTVE VLRGNAAEIA RRLGRGVNIF MVSTRDEAKA RALCPDGTRI
     TADPFEVVRH PEVDIVVELF GGTGIAKELV FEAVRHGKHI VTANKKLLAE HGSELFALAE
     KHNVMVQFEA AVAGGIPIIK ARREGLAANR IRSIAGIING TSNFILSEMR EKGSAFADVL
     KEAQALGYAE ADPTFDIEGH DAGHKITIMS ALAFGTPVNF AACYLEGISK LDSRDIKYAE
     ELGYRIKLLG ITRRSEKGIE LRVHPTLLPE SRLLANVNGV MNAVRVNADM VGETLFYGAG
     AGALPTASAV VADIIDISRL IAADSGHRVP YLAFQPAQVQ AQTMLPMDEI TSSYYLRVQA
     EDKPGVLGQI ANLLAAQNVS IEALIQKGVL DGHTAEIVIL THSTVEKHIK AAIAAIEALD
     TVGEKVIMIR MESLHD
//
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