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Database: UniProt
Entry: V4RJ64_9RHIZ
LinkDB: V4RJ64_9RHIZ
Original site: V4RJ64_9RHIZ 
ID   V4RJ64_9RHIZ            Unreviewed;       428 AA.
AC   V4RJ64;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   10-APR-2019, entry version 26.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=N177_3378 {ECO:0000313|EMBL:ESR23310.1};
OS   Lutibaculum baratangense AMV1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhodobiaceae; Lutibaculum.
OX   NCBI_TaxID=631454 {ECO:0000313|EMBL:ESR23310.1, ECO:0000313|Proteomes:UP000017819};
RN   [1] {ECO:0000313|EMBL:ESR23310.1, ECO:0000313|Proteomes:UP000017819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMV1 {ECO:0000313|EMBL:ESR23310.1,
RC   ECO:0000313|Proteomes:UP000017819};
RX   PubMed=25059877;
RA   Singh A., Sreenivas A., Sathyanarayana Reddy G., Pinnaka A.K.,
RA   Shivaji S.;
RT   "Draft Genome Sequence of Lutibaculum baratangense Strain AMV1T,
RT   Isolated from a Mud Volcano in Andamans, India.";
RL   Genome Announc. Announc.2:e00735-14(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:ESR23310.1}.
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DR   EMBL; AWXZ01000039; ESR23310.1; -; Genomic_DNA.
DR   STRING; 631454.N177_3378; -.
DR   EnsemblBacteria; ESR23310; ESR23310; N177_3378.
DR   PATRIC; fig|631454.5.peg.3338; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000017819; 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:UP000017819};
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:ESR23310.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017819};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      345    425       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       4     11       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    201    201       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     101    101       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     186    186       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   428 AA;  45319 MW;  D52B153337644D96 CRC64;
     MGIAGLGTVG ASVVRLLGDK TDHLSKRSGR DVAVTAVCAR DRGRDRGVSL DGLSWHDDPV
     ALAESDGIDL FVELMGGEGD PAAAAVSTAL RRGRPVVTAN KALLAARGTE LARLAEENGT
     TIGFEAAVAG GIPIVKTMRE AMAGNRVERV YGILNGTCNY ILTRMEEEGL SFADCLAEAQ
     RLGYAEADPT FDIEGHDSAH KLALLSSLAF GVTTDFDSIH LEGIASITTE DLKAAAELGY
     RIKLLGVARR TDTGIEQRVT PTMMPRNLAL ANVDGVLNAV AVDGDEVGEI TMVGPGAGGS
     ATASAVVADI VDIARGRCLP VFGIPAAELE PYRRARMRKH AGGYYIRLSV YDRPGAFAAI
     AQRMAEEQIS LESIVQKEAK GAKGAQSARR VVLITHDTME AQIRKALQAI EDDGQIAERP
     HVIRIEKP
//
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