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Database: UniProt
Entry: A0A066ZYP2_HYDMR
LinkDB: A0A066ZYP2_HYDMR
Original site: A0A066ZYP2_HYDMR 
ID   A0A066ZYP2_HYDMR        Unreviewed;       438 AA.
AC   A0A066ZYP2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   16-JAN-2019, entry version 19.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=EI16_02450 {ECO:0000313|EMBL:KDN95185.1};
OS   Hydrogenovibrio marinus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Hydrogenovibrio.
OX   NCBI_TaxID=28885 {ECO:0000313|EMBL:KDN95185.1, ECO:0000313|Proteomes:UP000027341};
RN   [1] {ECO:0000313|EMBL:KDN95185.1, ECO:0000313|Proteomes:UP000027341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MH-110 {ECO:0000313|EMBL:KDN95185.1,
RC   ECO:0000313|Proteomes:UP000027341};
RA   Cha H.J., Jo B.H., Hwang B.H.;
RT   "Draft genome sequence of Hydrogenovibrio marinus MH-110, a model
RT   organism for aerobic H2 metabolism.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-
CC         semialdehyde + NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57476, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:537519; EC=1.1.1.3;
CC         Evidence={ECO:0000256|RuleBase:RU000579};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 3/3.
CC       {ECO:0000256|RuleBase:RU000579}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 3/5.
CC       {ECO:0000256|RuleBase:RU000579}.
CC   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU004171}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KDN95185.1}.
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DR   EMBL; JMIU01000001; KDN95185.1; -; Genomic_DNA.
DR   RefSeq; WP_029909042.1; NZ_JMIU01000001.1.
DR   EnsemblBacteria; KDN95185; KDN95185; EI16_02450.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000027341; 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   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   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; SSF51735; SSF51735; 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
KW   {ECO:0000256|RuleBase:RU000579};
KW   Complete proteome {ECO:0000313|Proteomes:UP000027341};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   Methionine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   NADP {ECO:0000256|PIRSR:PIRSR000098-2, ECO:0000256|RuleBase:RU000579};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000579,
KW   ECO:0000313|EMBL:KDN95185.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027341};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      357    437       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       9     16       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    207    207       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     107    107       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     192    192       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   438 AA;  46768 MW;  3020A4756C42D779 CRC64;
     MKEVRLGLLG LGTVGGGTVN ILQTTQTEIQ RRLGGKVSVK VEQIAVRDLN RARPVDTTGI
     DLTTDPLAVV NNPNVDIVVE LMGGTTLAKT CLEQAIQNKK HIVTANKALI AEHGNELFKT
     AEAQGVMIAY ESAVAGGIPI IKALREGLAA NQIEWLAGII NGTGNYILTE MKKPGADFSQ
     VLKKAQELGY AEADPTFDVE GIDAAHKLTI MASIAFGIEL QFDKVYTEGI SKVTGDDIQF
     AQKLGYQIKH LGIAARADNG FSLRVHPTLV KDSVLIANVN GVMNAVMVAG NHVGQTLYYG
     PGAGAGPTAS AVVADIIDVI RALRQPQEDR VPGLGFALDQ LTSAPVVAID DIKSAYYLRF
     YAKDHAGVLA KVSSIMAQSQ ISIELLHQEP CADNEDDATI VMITNKVQES TINQAISALE
     SMEEIDGDIM RIRVAGFK
//
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