ID A0A261S773_9BORD Unreviewed; 434 AA.
AC A0A261S773;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN ORFNames=CEG14_18260 {ECO:0000313|EMBL:OZI32832.1};
OS Bordetella genomosp. 1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1395607 {ECO:0000313|EMBL:OZI32832.1, ECO:0000313|Proteomes:UP000217005};
RN [1] {ECO:0000313|EMBL:OZI32832.1, ECO:0000313|Proteomes:UP000217005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU17610 {ECO:0000313|EMBL:OZI32832.1,
RC ECO:0000313|Proteomes:UP000217005};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) 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:OZI32832.1}.
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DR EMBL; NEVL01000004; OZI32832.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261S773; -.
DR OrthoDB; 9808167at2; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000217005; 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 ECO:0000313|EMBL:OZI32832.1}.
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 434 AA; 46343 MW; 9E538FE598D6952B CRC64;
MNPMKVGLLG LGVVGGGTWS VLSRNAEEIA RRAGRRIEVS RIAVRDVAKA RARVGDTLEI
STDVHALVRD PDIDIVVELI GGDTLARELV LEAISQGKHV VTANKALLAK HGNEIFAAAS
ARGVMVAFEA AVAGGIPIIK AIREGLTANR IQWVAGIING TTNFILSEMR SRGLAFADVL
AEAQRLGYAE ADPTFDVEGV DAAHKLTLLA SLAFGVPVQF DKAHIEGISN LAQEDIAHAE
RLGYRIKLLG ITKRRAEGIE LRVHPALVPA ERLLANVEGA MNAVLVSGDA VGPTLYYGQG
AGEEPTASAV VADLVDVTRL HTADPGNRVP HLAFQPDAMS DLAILPIEQV STSYYLRLRV
DDQPGVLADI ARLLADRGIS IGSMIQQPSH IGGADIIFLT HEAVEGNVNQ AIERIESLPF
VRSKVTRLRM ENLT
//
