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Database: UniProt
Entry: F5T232_9GAMM
LinkDB: F5T232_9GAMM
Original site: F5T232_9GAMM 
ID   F5T232_9GAMM            Unreviewed;       437 AA.
AC   F5T232;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   16-JAN-2019, entry version 37.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=MAMP_01284 {ECO:0000313|EMBL:EGL53557.1};
OS   Methylophaga aminisulfidivorans MP.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL53557.1, ECO:0000313|Proteomes:UP000003544};
RN   [1] {ECO:0000313|EMBL:EGL53557.1, ECO:0000313|Proteomes:UP000003544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP(T) {ECO:0000313|Proteomes:UP000003544};
RX   PubMed=21685284; DOI=10.1128/JB.05403-11;
RA   Han G.H., Kim W., Chun J., Kim S.W.;
RT   "Draft genome sequence of Methylophaga aminisulfidivorans MP T.";
RL   J. Bacteriol. 193:4265-4265(2011).
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:EGL53557.1}.
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DR   EMBL; AFIG01000003; EGL53557.1; -; Genomic_DNA.
DR   RefSeq; WP_007146807.1; NZ_AFIG01000003.1.
DR   STRING; 1026882.MAMP_01284; -.
DR   EnsemblBacteria; EGL53557; EGL53557; MAMP_01284.
DR   eggNOG; ENOG4105D6E; Bacteria.
DR   eggNOG; COG0460; LUCA.
DR   OrthoDB; 1464088at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000003544; 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:UP000003544};
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   Reference proteome {ECO:0000313|Proteomes:UP000003544};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      355    437       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       9     16       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    205    205       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     105    105       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     190    190       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   437 AA;  46936 MW;  B3C069E651964596 CRC64;
     MQSVKIGILG LGTVGSGTVN VLTRNSREIS RRAGRDIEIY RAADRDLDKP KGCDTSAINL
     TDDAFDIIND PEIQIVVELI GGTGVAKELV IKAIENGKHV VTANKALIAI HGNELFELAQ
     EKGVTISFEA AVAGGIPIIK AMREGLAGNR IEWLAGIING TGNFILTEMR EKGRDFADVL
     AEAQALGYAE ADPTFDIEGI DAAHKLTIMA SIAFGIPLQF DKCYTEGISR IAQEDVLNAN
     ELGYRIKHLG IAKKTTAGVE LRVHPTLIPQ RRLLANVNGV MNAVVVKGDA VGPTLYYGAG
     AGSEATASAV VADIVDIVRA LTTDPENRVP HLAFQPDALK DTPILPMSEV VTSYYLRIHT
     LDKPGVLADI TRILSNEGIN IEAILQKQPE EHEGMVPIIM LTQAVVEKNM DQAIAQIEAL
     DTVPDSIMRI RMESLGG
//
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