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Database: UniProt
Entry: A0A0Q9KXX5_9MICO
LinkDB: A0A0Q9KXX5_9MICO
Original site: A0A0Q9KXX5_9MICO 
ID   A0A0Q9KXX5_9MICO        Unreviewed;       443 AA.
AC   A0A0Q9KXX5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   10-APR-2019, entry version 14.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=ASG74_06095 {ECO:0000313|EMBL:KRE43027.1};
OS   Knoellia sp. Soil729.
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; Knoellia.
OX   NCBI_TaxID=1736394 {ECO:0000313|EMBL:KRE43027.1, ECO:0000313|Proteomes:UP000051965};
RN   [1] {ECO:0000313|Proteomes:UP000051965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil729 {ECO:0000313|Proteomes:UP000051965};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE43027.1, ECO:0000313|Proteomes:UP000051965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil729 {ECO:0000313|EMBL:KRE43027.1,
RC   ECO:0000313|Proteomes:UP000051965};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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   -!- 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:KRE43027.1}.
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DR   EMBL; LMSA01000002; KRE43027.1; -; Genomic_DNA.
DR   RefSeq; WP_056143211.1; NZ_LMSA01000002.1.
DR   EnsemblBacteria; KRE43027; KRE43027; ASG74_06095.
DR   OrthoDB; 1464088at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000051965; 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:UP000051965};
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      362    440       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND      17     24       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    212    212       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     112    112       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     197    197       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   443 AA;  45701 MW;  E5CE1AEF4265E7C6 CRC64;
     MASPTSTPLP TLKVALLGCG VVGSAVATML VRNGDDLASR VGARLELIGI AVRRPERPRP
     DVPVDPSLFT ADADTLVRSA DVVIEVIGGI DPARELILTA MKHGASVVTA NKALLAEDGP
     TLYAAAAENN VDLYYEAAVA GAIPIVRPMR ESLVGDDVQR VLGIVNGTTN FVLDKMDSTG
     AGFAETVEQA QALGYAEADP TADVEGFDAA AKAAILASLA FHTRVSIDQV HREGITEVSA
     ADIQAAREMD AVVKLLAICE LVRDDSGAPS AVSVRVHPAM IARSHPLASV RDAYNAVFVE
     ASAAGELMFY GKGAGGEPTS SAVLGDVVAV ARHRLAGGHG PAESAYADLP VAAMGQATTR
     YHISLAVADR PGVLAQVASA FAEHGVSIET VRQRVLGEGD ESRASLVIVT HHATDSALAA
     TVDALTGLDT VDAVVSWMRV EGA
//
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