ID D9QNU7_BRESC Unreviewed; 578 AA.
AC D9QNU7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN OrderedLocusNames=Bresu_1068 {ECO:0000313|EMBL:ADL00380.1};
OS Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 /
OS NBRC 16000 / CB 81) (Caulobacter subvibrioides).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=633149 {ECO:0000313|EMBL:ADL00380.1, ECO:0000313|Proteomes:UP000002696};
RN [1] {ECO:0000313|Proteomes:UP000002696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81
RC {ECO:0000313|Proteomes:UP000002696};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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}.
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DR EMBL; CP002102; ADL00380.1; -; Genomic_DNA.
DR RefSeq; WP_013268483.1; NC_014375.1.
DR AlphaFoldDB; D9QNU7; -.
DR STRING; 633149.Bresu_1068; -.
DR KEGG; bsb:Bresu_1068; -.
DR eggNOG; COG0460; Bacteria.
DR eggNOG; COG0527; Bacteria.
DR HOGENOM; CLU_454780_0_0_5; -.
DR InParanoid; D9QNU7; -.
DR OrthoDB; 9808167at2; -.
DR BioCyc; BSUB633149:G1GM8-1067-MONOMER; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000002696; Chromosome.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
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; PF00696; AA_kinase; 1.
DR Pfam; PF00742; Homoserine_dh; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR SUPFAM; SSF53633; Carbamate kinase-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; PS01042; HOMOSER_DHGENASE; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:ADL00380.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002696};
KW Transferase {ECO:0000313|EMBL:ADL00380.1}.
FT DOMAIN 23..232
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT DOMAIN 279..387
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 396..564
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
SQ SEQUENCE 578 AA; 60043 MW; 2014455B8783D534 CRC64;
MPNAPHLAVV EKPKPDPAPA TEVVVLKFGS SILQDRSCAP AVASEVYGHV RAGRKVIAVV
SALGGHTDRL LAEARELGLD HENDLLPAYV ALGEEKAAAL VAIACDRIGL DASALSVREL
GIVAEGPSEH AHPVSLRSEA LRKALADHQV VVVPGFGAVG SSGKVVLLGR GGSDLTAVFL
AAELGLKRVR LVKDVDGLYD RDPASASGKP LRYRRASWDD ARRHGGALVQ HDAIDLGQER
LVEIEVAALG RADCTVVGDA SAPPGPSVPD APLKVAIAGC GVVGGGLLAR LQKDARFQVV
GVLVRDPSKP RDVEAPADLF TSDREALLAL KPDILLEALS EGGAGHDLIR CALERGIDVA
SANKQAISRD PQGLADAARA HGSRLAYSAA VGGGAPMIET LRAAKSAGPV KGFEAVLNGT
VNFMLTRLQA GADFADALAD ARVAGFAEED PSSDLEGRDS AAKVRLLAFE AFGRTPAEAD
VPCAVLSDAF HPAGPVRQIG ACFKEGDGLK ASVSLDVGLD DPFFQALDGE RNGLKVYGED
GRVWSCKGRG AGRWPTTESV LADLADIVRA RHASLGHH
//
