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Database: UniProt
Entry: A0A1X9SQY1_9PROT
LinkDB: A0A1X9SQY1_9PROT
Original site: A0A1X9SQY1_9PROT 
ID   A0A1X9SQY1_9PROT        Unreviewed;       421 AA.
AC   A0A1X9SQY1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   05-JUN-2019, entry version 7.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   Name=hom {ECO:0000313|EMBL:ARQ98674.1};
GN   ORFNames=CIGN_0364 {ECO:0000313|EMBL:ARQ98674.1};
OS   Campylobacter sp. NCTC 13003.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=1660064 {ECO:0000313|EMBL:ARQ98674.1, ECO:0000313|Proteomes:UP000194309};
RN   [1] {ECO:0000313|Proteomes:UP000194309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13003 {ECO:0000313|Proteomes:UP000194309};
RX   PubMed=28854596; DOI=10.1093/gbe/evx093;
RA   Miller W.G., Yee E., Lopes B.S., Chapman M.H., Huynh S., Bono J.L.,
RA   Parker C.T., Strachan N.J.C., Forbes K.J.;
RT   "Comparative Genomic Analysis Identifies a Campylobacter Clade
RT   Deficient in Selenium Metabolism.";
RL   Genome Biol. Evol. 9:1843-1858(2017).
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; CP018788; ARQ98674.1; -; Genomic_DNA.
DR   BioCyc; GCF_002139915:CIGN_RS01790-MONOMER; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000194309; 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:UP000194309};
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:ARQ98674.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194309};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      342    421       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       6     13       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    197    197       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING      99     99       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     182    182       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   421 AA;  45648 MW;  49B41E074B259756 CRC64;
     MRVAILGVGT VGTEVANVLI KNSDLIVSRA GVSITPVVGV VRNLSKHKDS IIPLTDDIDS
     VINRDDIDVF IELMGGIDKP YEIISKILER KKAVVTANKA LLAYYRNELE ALAGDTAFGY
     EASVAGGIPI IKALREGLSA NHIQKIMGIM NGTSNYILTN MMNSGVQFDE ALKKAQELGY
     AEADPTFDIG GFDTAHKLLI LASIAYCVHA KPEDILIEGI SQISSEDIYF ANEFEYAIKL
     LAIAKRGEGT LELRVHPAFI SKDKMLANVN GVMNAVSVVG DAVGESLFYG AGAGGSATAS
     AVISDLIDIA REIRNPMLGY KAPLESAPLK LLKPNQIRTK YYLRLKVADE VGVLAKITNL
     MSQNNLSIDS FLQKAKSKDE GCATLFFTTH TCLEADMLRV INSLENENFI KAKPFMIRIE
     S
//
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