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Database: UniProt
Entry: U5RXI1_9CLOT
LinkDB: U5RXI1_9CLOT
Original site: U5RXI1_9CLOT 
ID   U5RXI1_9CLOT            Unreviewed;       432 AA.
AC   U5RXI1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   16-JAN-2019, entry version 32.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=CAETHG_3099 {ECO:0000313|EMBL:AGY77302.1};
OS   Clostridium autoethanogenum DSM 10061.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY77302.1, ECO:0000313|Proteomes:UP000017590};
RN   [1] {ECO:0000313|EMBL:AGY77302.1, ECO:0000313|Proteomes:UP000017590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY77302.1};
RX   PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA   Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA   Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT   "Comparison of single-molecule sequencing and hybrid approaches for
RT   finishing the genome of Clostridium autoethanogenum and analysis of
RT   CRISPR systems in industrial relevant Clostridia.";
RL   Biotechnol. Biofuels 7:40-40(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}.
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DR   EMBL; CP006763; AGY77302.1; -; Genomic_DNA.
DR   RefSeq; WP_023163007.1; NZ_CP012395.1.
DR   EnsemblBacteria; AGY77302; AGY77302; CAETHG_3099.
DR   GeneID; 33107444; -.
DR   KEGG; cah:CAETHG_3099; -.
DR   PATRIC; fig|1341692.11.peg.3111; -.
DR   KO; K00003; -.
DR   BioCyc; CAUT1341692:G1HL9-3079-MONOMER; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000017590; Chromosome.
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:UP000017590};
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:UP000017590};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      351    427       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   432 AA;  48120 MW;  B07A1C1F25729141 CRC64;
     MKKVRIALMG LGNVGAGVWT ILNSNKKEIM KRSGYEVEVA KILVRDRNKQ RDVEVPDEIV
     TTDFNDILED DSIKIVVEVM GGINPAREYM LKCMDRKKQI VTANKMLLAT GGDELFEKAD
     SKGVMFNYEA SVAGGIPIIN GIDESLTANK IEELYGIVNG TTNYILTKMQ LEKLDFDVAL
     KQAQDMGYAE ADPTSDIEGF DAQYKLAILS SLAFGTKINV DNVYREGITK IKSIDIRYAK
     KFNMVIKLLA IAKENEGKLE LKVHPTMIPE SHPLANVYDS FNAIFIKGNA VGDLMFYGRG
     AGSLPTGSAV VSDIIAILRS NVDIENFNSV VKNNLWHRKI KDIKDCASKF YIRLSVMDQS
     GVLGEITTIL GKHNVSLRSV MQKGREESKD KVTIVLITHK IEEAEINSAI EEIINLKSVM
     QIDNIIRIED FK
//
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