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Database: UniProt
Entry: A0A0N1F7B7_9PROT
LinkDB: A0A0N1F7B7_9PROT
Original site: A0A0N1F7B7_9PROT 
ID   A0A0N1F7B7_9PROT        Unreviewed;       445 AA.
AC   A0A0N1F7B7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   16-JAN-2019, entry version 15.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=GLUCOINTEAF2_0203283 {ECO:0000313|EMBL:KPH85630.1};
OS   Komagataeibacter intermedius AF2.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Komagataeibacter.
OX   NCBI_TaxID=1458464 {ECO:0000313|EMBL:KPH85630.1, ECO:0000313|Proteomes:UP000031553};
RN   [1] {ECO:0000313|EMBL:KPH85630.1, ECO:0000313|Proteomes:UP000031553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF2 {ECO:0000313|EMBL:KPH85630.1,
RC   ECO:0000313|Proteomes:UP000031553};
RA   Santos R.A., Berretta A.A., Barud H.S., Ribeiro S.J.,
RA   Gonzalez-Garcia L.N., Zucchi T.D., Goldman G.H., Riano-Pachon D.M.;
RT   "Draft Genome Sequence of Komagataeibacter intermedius Strain AF2,
RT   Isolated from Kombucha Tea.";
RL   Submitted (JUL-2015) 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:KPH85630.1}.
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DR   EMBL; JUFX02000231; KPH85630.1; -; Genomic_DNA.
DR   RefSeq; WP_039736741.1; NZ_JUFX02000231.1.
DR   EnsemblBacteria; KPH85630; KPH85630; GLUCOINTEAF2_0203283.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000031553; 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:UP000031553};
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   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      360    441       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND      19     26       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    216    216       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     116    116       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     201    201       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   445 AA;  46776 MW;  956539AA099477EF CRC64;
     MTSSPCKPAP KPPLRIGIAG LGTVGAGVVK LLRENAELIR ARAGRELVVT AVSARNRTRD
     RGIDLSGVAW CDTPEELATH PDVDVVAELI GGAEGAARLT VTRALENRRP VVTANKALIA
     IHGAELACTA QAAGVPLMFE AAVAGGIPAI KTVREGLAAD RILKIGGILN GTCNYILTVM
     HETGRDFAEI LSDAQKLGYA EADPSTDVDG VDTAHKLAIL AGLAFGRPVV FASIYIEGIR
     RIGALDLQFA RKMGYRIKLL GIACQHENGI EARVHPCLVP QDAPIAEVNG VFNAVVAEGA
     FAGRLMLEGR GAGEGPTATA VCADLIDIAR GSAMPVWGCA ADSLTQAVAL PSKSFMGEYY
     LRLNVEDRPG VIADITAVLR DNGVSLRSML QHADAHEVRP DGAHAVPLVL LTHRTNEAAM
     QHALHHIAEL PAVLDEPVMI RIDAG
//
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