GenomeNet

Database: UniProt
Entry: A0A1W6BIU8_9PROT
LinkDB: A0A1W6BIU8_9PROT
Original site: A0A1W6BIU8_9PROT 
ID   A0A1W6BIU8_9PROT        Unreviewed;       429 AA.
AC   A0A1W6BIU8;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   08-MAY-2019, entry version 8.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=B8063_06855 {ECO:0000313|EMBL:ARJ49724.1};
OS   Candidatus Pelagibacter sp. RS40.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC   Pelagibacteraceae; Candidatus Pelagibacter.
OX   NCBI_TaxID=1977865 {ECO:0000313|EMBL:ARJ49724.1, ECO:0000313|Proteomes:UP000192922};
RN   [1] {ECO:0000313|EMBL:ARJ49724.1, ECO:0000313|Proteomes:UP000192922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS40 {ECO:0000313|EMBL:ARJ49724.1,
RC   ECO:0000313|Proteomes:UP000192922};
RA   Jimenez-Infante F., Ngugi D.K., Stingl U.;
RT   "Genomic Characterization of Two Novel SAR11 Isolates From the Red
RT   Sea, Including the First Strain of the SAR11 Ib clade.";
RL   Submitted (APR-2017) 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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP020778; ARJ49724.1; -; Genomic_DNA.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000192922; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000192922};
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      351    429       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   COILED      167    187       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    207    207       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     106    106       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     191    191       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   429 AA;  47814 MW;  9CE16692987A53D7 CRC64;
     MRQINIAIVG LGQIGNYLYN ELLSKKKDIE IKTGKRIQIV AISAKNKNKK RKFKINKKIF
     YKNPLDIINN KKVDILIEAI GFADGLSKKI VENALKNKIH VITPNKALIS KHGDYLSFLA
     EKNKVNLEFE AAVAGGIPIV RTIKEGLATN KITKVYGILN GTCNYILSQM EKTKDSFKNV
     LKNAQKLGYA EPGNPKLDLN GYDALAKVKI LSALAFNCKI SKSQSLMEGI EKIEATDFDI
     VEKLNLRIKL LGITEIINNK IFERVHPCLV SRDSYIGNVT DVMNAVILEG KPVGESVMQG
     EGAGPGPTTS ALMSDLLSIL RGNIKFPFGI SNKKRNLSIS YNYNSYENSL YLRVEVKDKP
     GVLSSITNIL AKNNISVQRL IQIPDNKRKT ASIIIITHKC KEINSNKCIK MLKKDSNILK
     EPNLIRLFN
//
DBGET integrated database retrieval system