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Database: UniProt
Entry: A0A099TPQ2_9HELI
LinkDB: A0A099TPQ2_9HELI
Original site: A0A099TPQ2_9HELI 
ID   A0A099TPQ2_9HELI        Unreviewed;       422 AA.
AC   A0A099TPQ2;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   10-APR-2019, entry version 20.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=LS70_08895 {ECO:0000313|EMBL:KGL10467.1};
OS   Helicobacter sp. MIT 11-5569.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1548151 {ECO:0000313|EMBL:KGL10467.1, ECO:0000313|Proteomes:UP000029923};
RN   [1] {ECO:0000313|EMBL:KGL10467.1, ECO:0000313|Proteomes:UP000029923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 11-5569 {ECO:0000313|EMBL:KGL10467.1,
RC   ECO:0000313|Proteomes:UP000029923};
RA   Sheh A., Shen Z., Fox J.G.;
RT   "Genome sequencing of Helicobacter and Campylobacter species isolated
RT   from rodents.";
RL   Submitted (SEP-2014) 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:KGL10467.1}.
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DR   EMBL; JRPB01000014; KGL10467.1; -; Genomic_DNA.
DR   RefSeq; WP_034290872.1; NZ_JRPB01000014.1.
DR   STRING; 1548151.LS70_08895; -.
DR   EnsemblBacteria; KGL10467; KGL10467; LS70_08895.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000029923; 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:UP000029923};
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:UP000029923};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      344    419       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       9     16       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    201    201       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     103    103       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     186    186       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   422 AA;  45196 MW;  EDD242D5BF8F88E1 CRC64;
     MKELILGIIG LGTVGSSVAK ILHDNQSLIA ARAGCAMRIK KGAVKDLSKS REIFDFPITN
     NVDEILDDPE IDIVVELTGG VDAPFEIAKK ALRASKALVT ANKAMLAYHR YTLQQIAGDL
     PIGFEASVAG GIPIIKALRD GLGANHILSI RGIINGTCNF ILTKMKDEGA GFQEVLKEAQ
     DLGYAEADPT FDIGGFDAAH KLLILASIAY GIDARPDDIL IEGITQITQE DIAFAKEFGY
     HLKLLGIAKK DGDCIELRVH PTFLPKNAML GKVDGVMNAI SVVGDCVGET LYYGAGAGGE
     ATASAVISDI IEIARTKSSP MLGFKTISNT LKLKPINAIK SAYYLRLLVL DKPGVLAQIA
     KVFGEVGISI DTFLQRNAKD KNHSVLLLST HTCTEADIKL AIERISSLEV VKTSPVMIRI
     EK
//
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