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Database: UniProt
Entry: A6Q5A1_NITSB
LinkDB: A6Q5A1_NITSB
Original site: A6Q5A1_NITSB 
ID   A6Q5A1_NITSB            Unreviewed;       420 AA.
AC   A6Q5A1;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   OrderedLocusNames=NIS_1553 {ECO:0000313|EMBL:BAF70660.1};
OS   Nitratiruptor sp. (strain SB155-2).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Nitratiruptor.
OX   NCBI_TaxID=387092 {ECO:0000313|EMBL:BAF70660.1, ECO:0000313|Proteomes:UP000001118};
RN   [1] {ECO:0000313|EMBL:BAF70660.1, ECO:0000313|Proteomes:UP000001118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB155-2 {ECO:0000313|EMBL:BAF70660.1,
RC   ECO:0000313|Proteomes:UP000001118};
RX   PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA   Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA   Horikoshi K.;
RT   "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT   emergence of pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009178; BAF70660.1; -; Genomic_DNA.
DR   RefSeq; WP_012082923.1; NC_009662.1.
DR   STRING; 387092.NIS_1553; -.
DR   EnsemblBacteria; BAF70660; BAF70660; NIS_1553.
DR   KEGG; nis:NIS_1553; -.
DR   eggNOG; ENOG4105D6E; Bacteria.
DR   eggNOG; COG0460; LUCA.
DR   HOGENOM; HOG000076615; -.
DR   KO; K00003; -.
DR   OMA; FEASVCG; -.
DR   OrthoDB; 1464088at2; -.
DR   BioCyc; NSP387092:G1G2O-1661-MONOMER; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000001118; 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:UP000001118};
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:BAF70660.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001118};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      343    420       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       7     14       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    198    198       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     100    100       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     183    183       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   420 AA;  45706 MW;  C386ADF83F09D3FB CRC64;
     MINVGIIGVG TVGTSVVKVL EKNRDIISAR AGKEIQVVKG VVRNLEKKRN IDIPLTTDPF
     EVTDDPNIDI VVELMGGVEE AYEVVQRALK NKKAVVTANK ALLAYHRYEL QQLAGDIPFE
     FEASVAGGIP IIKALREGLS ANHIDAIRGI MNGTCNYILT KMANEGAEFS AILKEAQELG
     YAEADPTFDI EGYDAAHKLL ILASIAYGID AKPEDILIEG ITKINTLDFE FANEFGYSIK
     LLTIAKKRGN EVELRVHPTL VPNEQMIAKV DGVMNGVSVI GDVVGETMYY GPGAGGDATA
     SAVVSNIIDI ARGGKCSPML GFKRPLESGM ELASKDSILS NYYLRLLVED RPGILAKIAS
     IFGEYNISIE SMLQKPGPDR LAHLLLSTHQ CQESEIHKAL NEIKQQAFLK EEPAMIRIEV
//
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