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Database: UniProt
Entry: A0A1Q7QI45_9CHLR
LinkDB: A0A1Q7QI45_9CHLR
Original site: A0A1Q7QI45_9CHLR 
ID   A0A1Q7QI45_9CHLR        Unreviewed;       321 AA.
AC   A0A1Q7QI45;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, 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=AUI58_07650 {ECO:0000313|EMBL:OLD51430.1};
OS   Chloroflexi bacterium 13_1_40CM_2_70_6.
OC   Bacteria; Chloroflexi.
OX   NCBI_TaxID=1805070 {ECO:0000313|EMBL:OLD51430.1};
RN   [1] {ECO:0000313|EMBL:OLD51430.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C.,
RA   Singh A., Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G.,
RA   Northen T., Pan C., Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
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:OLD51430.1}.
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DR   EMBL; MNHK01000101; OLD51430.1; -; Genomic_DNA.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
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; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
DR   InterPro; IPR022697; HDH_short.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF036497; HDH_short; 1.
DR   SUPFAM; SSF51735; SSF51735; 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   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   Methionine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   NADP {ECO:0000256|PIRSR:PIRSR036497-2, ECO:0000256|RuleBase:RU000579};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000579};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN        7    130       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      138    315       Homoserine_dh. {ECO:0000259|Pfam:
FT                                PF00742}.
FT   NP_BIND       7     12       NADP. {ECO:0000256|PIRSR:PIRSR036497-2}.
FT   ACT_SITE    205    205       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR036497-1}.
FT   BINDING     106    106       NADP. {ECO:0000256|PIRSR:PIRSR036497-2}.
FT   BINDING     190    190       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036497-2}.
SQ   SEQUENCE   321 AA;  34106 MW;  2ADC278671FF19A7 CRC64;
     MRLALFGFGH VGRALARLLL ATRDRHAFTV TAIVTARHGA VVDKRGVDLA AALTRERLGD
     DAAPIGKLPA DVLVEMTTLD ARTGEPALTY IREALGARLH VVTSNKGPLA VAFRDLHERA
     RANKRLLRYE ATVADCLPVF DLARAALPIA EIRELRGIVS STCNHVLSMA ASGASLHTAL
     AEAQRLGIAE ADPSNDLEGH DASAKAAILA NALMGTDLTP TDVSREPIDD EAVADAWNAA
     AQGDRVRPLV HIVREGDGVR ATFGPRRLAP VDPLYAVDGF SMALELTTDL AGKVVVQLHE
     PGVDQVAYAI LIDLLDIAAS R
//
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