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Database: UniProt
Entry: A0A1Q5E419_9ACTN
LinkDB: A0A1Q5E419_9ACTN
Original site: A0A1Q5E419_9ACTN 
ID   A0A1Q5E419_9ACTN        Unreviewed;       435 AA.
AC   A0A1Q5E419;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   16-JAN-2019, entry version 7.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=AMK18_13690 {ECO:0000313|EMBL:OKJ02829.1};
OS   Streptomyces sp. CB01249.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1703929 {ECO:0000313|EMBL:OKJ02829.1, ECO:0000313|Proteomes:UP000186839};
RN   [1] {ECO:0000313|EMBL:OKJ02829.1, ECO:0000313|Proteomes:UP000186839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01249 {ECO:0000313|EMBL:OKJ02829.1,
RC   ECO:0000313|Proteomes:UP000186839};
RX   PubMed=27999165;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural
RT   Products.";
RL   MBio 7:e02104-16(2016).
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:OKJ02829.1}.
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DR   EMBL; LISW01000002; OKJ02829.1; -; Genomic_DNA.
DR   RefSeq; WP_037785905.1; NZ_LISW01000002.1.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000186839; 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:UP000186839};
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:UP000186839};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      352    431       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND      11     18       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    206    206       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     106    106       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     191    191       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   435 AA;  45094 MW;  120632F6CC74E370 CRC64;
     MRTRPLKVAL LGCGVVGSEV ARIMTTHADD LAARIGAPVE LAGVAVRRPS KVREGIDPAL
     ITTDATALVK RGDIDVVIEV IGGIEPARTL IRTAFEHGAS VVSANKALLA EDGAALHAAA
     EQHGRDLYYE AAVAGAIPLV RPLRESLAGD KVNRVLGIVN GTTNFILDKM DTSGAGYSEA
     LDEATALGYA EADPTADVEG FDAAAKAAIL AGIAFHTRVR IGDVHREGIT EVTAADIASA
     RRMGCTVKLL AICERAADGA SVTARVHPAM IPLSHPLASV REAYNAVFVE AEAAGQLMFY
     GPGAGGAPTA SAVLGDLVAV CRNKLNEAPG PGESAYTRLP VSPMGDVVTR YHISLDVADK
     PGVLAQVATV FADQGVSIDT VRQQSRPDSQ ETDGEASLVV VTHRAPDAAL SGTVEALRKL
     DTVRGVASIM RVEGE
//
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