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Database: UniProt
Entry: A0A220W9T7_9SPHN
LinkDB: A0A220W9T7_9SPHN
Original site: A0A220W9T7_9SPHN 
ID   A0A220W9T7_9SPHN        Unreviewed;       432 AA.
AC   A0A220W9T7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-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:ASK89620.1};
GN   ORFNames=SPHFLASMR4Y_02886 {ECO:0000313|EMBL:ASK89620.1};
OS   Sphingorhabdus flavimaris.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingorhabdus.
OX   NCBI_TaxID=266812 {ECO:0000313|EMBL:ASK89620.1, ECO:0000313|Proteomes:UP000198359};
RN   [1] {ECO:0000313|EMBL:ASK89620.1, ECO:0000313|Proteomes:UP000198359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMR4y {ECO:0000313|EMBL:ASK89620.1,
RC   ECO:0000313|Proteomes:UP000198359};
RA   Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Godhe A.,
RA   Clarke A.K.;
RT   "Genome Sequence of Sphingorhabdus flavimaris Strain SMR4y Isolated
RT   from a culture of the Diatom Skeletonema marinoi.";
RL   Submitted (JUL-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}.
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DR   EMBL; CP022336; ASK89620.1; -; Genomic_DNA.
DR   KEGG; sfla:SPHFLASMR4Y_02886; -.
DR   KO; K00003; -.
DR   BioCyc; GCF_002218195:SPHFLASMR4Y_RS14230-MONOMER; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000198359; 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:UP000198359};
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:ASK89620.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198359};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      351    423       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND      10     17       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    207    207       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     107    107       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     192    192       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   432 AA;  45553 MW;  F623130291ADE781 CRC64;
     MTAPLRIALA GLGTVGTGVI RLIEENGAMI TQRAGRPIVV TAVSARNRDR DRGIDLASYS
     WCDKTEDLAT HDDVDCVVEL IGGSEGTALE LARKSLAAGK SFVTANKAMV AHHGMELATA
     AENANLSLRY EAAVAGGIPV IKGLRDGASA NRIERVYGIL NGTCNYILTA MEKYGRDFDD
     VLREAQEIGY AEADPSFDID GVDAAHKLAI LAALSFGKAL DFDGVEIDGI RHIMAADIGQ
     AKALGYRIRL LGMARIDNGK LFQRVNPYLV PENHPLAHIE GSTNAVVAEG NFSGRLMFQG
     AGAGEGPTAS AVVADLIDIA RGDAGTVFAA PASKMEACER AESGNRTGKS YVRFIVADKP
     GVLAEITAAM RDANVSIESL IQTAKTDEGS VLISMVTHDS RERNVSESLA ALSSSTSLQA
     APVVMHLLSD QD
//
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