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Database: UniProt
Entry: B2HQL8_MYCMM
LinkDB: B2HQL8_MYCMM
Original site: B2HQL8_MYCMM 
ID   B2HQL8_MYCMM            Unreviewed;       441 AA.
AC   B2HQL8;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   16-JAN-2019, entry version 63.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   Name=thrA {ECO:0000313|EMBL:ACC42510.1};
GN   OrderedLocusNames=MMAR_4103 {ECO:0000313|EMBL:ACC42510.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC42510.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC42510.1, ECO:0000313|Proteomes:UP000001190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T.,
RA   Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N.,
RA   Jagels K., Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L.,
RA   Brosch R., Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum
RT   on the evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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}.
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DR   EMBL; CP000854; ACC42510.1; -; Genomic_DNA.
DR   RefSeq; WP_012395684.1; NC_010612.1.
DR   STRING; 216594.MMAR_4103; -.
DR   EnsemblBacteria; ACC42510; ACC42510; MMAR_4103.
DR   KEGG; mmi:MMAR_4103; -.
DR   eggNOG; ENOG4105D6E; Bacteria.
DR   eggNOG; COG0460; LUCA.
DR   HOGENOM; HOG000076615; -.
DR   KO; K00003; -.
DR   OMA; FEASVCG; -.
DR   OrthoDB; 1464088at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000001190; Chromosome.
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:UP000001190};
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:UP000001190};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      356    435       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND      13     20       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   441 AA;  45741 MW;  2B753E57AA396037 CRC64;
     MSGDVKPVGV AVLGLGNVGS EVVRIIEESA DDLAARVGAP LVLRGVGVRR VADDRGVPID
     LLTDDIEKLV SREDVDIVVE VMGPVEPSRK AILTALEHGK SVVTANKALL STSTGELAQA
     AESAHVDLYF EAAVAGAIPV IRPLTQSLAG DTVLRVAGIV NGTTNYILSE MDSTGADYAK
     ALADAGALGY AEADPTADVE GFDAAAKAAI LASIAFHTRV TADDVYREGI TKITPADFAS
     ARALGCTIKL LSICERLTTD EGQQRVSARV YPALVPLSHP LATVNGAFNA VVVEAEAAGR
     LMFYGQGAGG APTASAVTGD LVMAARNRVL GSRGPRESKY AQLPVAPMGF ISTRYYVSMN
     VADKAGVLSA VAAEFAKRDV SIAEVRQEGV VDQDGQRIGA RIVVVTHLAT DAALSETVEA
     LADLDVVENV ASVLRLEGND L
//
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