GenomeNet

Database: UniProt
Entry: W4DW36_9BACL
LinkDB: W4DW36_9BACL
Original site: W4DW36_9BACL 
ID   W4DW36_9BACL            Unreviewed;       428 AA.
AC   W4DW36;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   03-JUL-2019, entry version 27.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=C173_14235 {ECO:0000313|EMBL:ETT72204.1};
OS   Paenibacillus sp. FSL R7-277.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1227352 {ECO:0000313|EMBL:ETT72204.1, ECO:0000313|Proteomes:UP000019051};
RN   [1] {ECO:0000313|EMBL:ETT72204.1, ECO:0000313|Proteomes:UP000019051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R7-277 {ECO:0000313|EMBL:ETT72204.1,
RC   ECO:0000313|Proteomes:UP000019051};
RX   PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA   Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA   den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT   "Genomic comparison of sporeforming bacilli isolated from milk.";
RL   BMC Genomics 15:26-26(2014).
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:ETT72204.1}.
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; ASPX01000037; ETT72204.1; -; Genomic_DNA.
DR   RefSeq; WP_036725890.1; NZ_ASPX01000037.1.
DR   STRING; 1227352.C173_14235; -.
DR   EnsemblBacteria; ETT72204; ETT72204; C173_14235.
DR   PATRIC; fig|1227352.4.peg.2855; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000019051; 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:UP000019051};
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      350    425       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       9     16       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    205    205       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     105    105       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     190    190       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   428 AA;  46491 MW;  4ED7356651599F9A CRC64;
     MKPVKVGLLG LGTVGTGVVR IVEGNQEDLS SQVGSPILIE RIAVKNTEKP RDIEVDPSKI
     TDDPWAVIRD PEIDVIVEVM GGVAGTKEYI LEALERGKHI VTANKDLMAL HGSEILAKAQ
     EKQCDVFYEA SVAGGIPIIR TLIEGFSSDK IMKIMGIVNG TTNYILSKMS QEGASYLDAL
     QEAQELGYAE SDPTSDVEGL DAARKMAILG TLGFRTNVEL SDVSVSGISG VSKEDMAFAK
     RLGYEMKLLG IAERQDEEFS ISVQPTMIRT NHPIASVNGV FNAVYVYGEA VGETMFYGAG
     AGAMPTATSI VADLVAVIKN LKLGVNGLKQ IVPYKQKKLK SDEDIYYKNF LLLHVDDKAG
     VLAKITQVFA EYDVSLDSVV QQANPNNPDA EIIIVTHNAS RASMNKVLRH LEQLNVIHRI
     KSHYRVEG
//
DBGET integrated database retrieval system