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Database: UniProt
Entry: A0A1J4MZ30_9ACTN
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ID   A0A1J4MZ30_9ACTN        Unreviewed;       437 AA.
AC   A0A1J4MZ30;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   16-JAN-2019, entry version 9.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=UG56_022325 {ECO:0000313|EMBL:OIJ24531.1};
OS   Nocardioides luteus.
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=1844 {ECO:0000313|EMBL:OIJ24531.1, ECO:0000313|Proteomes:UP000033772};
RN   [1] {ECO:0000313|EMBL:OIJ24531.1, ECO:0000313|Proteomes:UP000033772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAFB {ECO:0000313|EMBL:OIJ24531.1,
RC   ECO:0000313|Proteomes:UP000033772};
RA   Murphy D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OIJ24531.1, ECO:0000313|Proteomes:UP000033772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAFB {ECO:0000313|EMBL:OIJ24531.1,
RC   ECO:0000313|Proteomes:UP000033772};
RA   Brown L., Ruiz O.N., Gunasekera T.;
RT   "Draft Genome Sequence of Nocardioides luteus Strain BAFB, an Alkane-
RT   Degrading Bacterium Isolated from JP-7 Polluted Soil.";
RL   Submitted (OCT-2016) 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:OIJ24531.1}.
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DR   EMBL; JZDQ02000037; OIJ24531.1; -; Genomic_DNA.
DR   RefSeq; WP_071327261.1; NZ_JZDQ02000037.1.
DR   OrthoDB; 1464088at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000033772; 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:UP000033772};
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   Reference proteome {ECO:0000313|Proteomes:UP000033772};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      359    432       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND      19     26       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    215    215       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     115    115       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     200    200       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   437 AA;  45142 MW;  37AC40C370DD7FEC CRC64;
     MSSNKTTAHA VKPLGVAVLG CGVVGSQVVR LLLEGDADLA ARVGAPLEIR GVAVRRLDAP
     RDVEVPAELL TTDAHGLVAR DDVDLVVEVI GGIEPARGLI LKALESGASV VTANKALLAE
     DGPTLYEAAE KAGTDLYYEA AVAGAIPILR PLRDSLVGDH VTKVMGIVNG TTNYILDKMD
     TYGAGFEEAL AEAQELGYAE ADPTADVEGF DAAAKAAILA SLAFHTRVTA SDVYREGITE
     VTAGDVASAK AMGSVVKLLA IAELDGDDVS ARVHPVMIPR THALATVRGA YNAVFVESAS
     AGDLMFYGQG AGGEPTASAV LGDLVTIGRN KALGARGFGE SAYAARAVRP MGETVTRYHV
     SLDVADKAGV LAAVATAFSE HGVSIKAVRQ EGRGEDAQLV VVSHEAPDAA LAATVQHLRE
     MEYVRDVASV MRVEGAV
//
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