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Database: UniProt
Entry: A0A1I1PRH5_9CLOT
LinkDB: A0A1I1PRH5_9CLOT
Original site: A0A1I1PRH5_9CLOT 
ID   A0A1I1PRH5_9CLOT        Unreviewed;       433 AA.
AC   A0A1I1PRH5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-2019, entry version 6.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=SAMN05421842_12070 {ECO:0000313|EMBL:SFD12345.1};
OS   Clostridium uliginosum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=119641 {ECO:0000313|EMBL:SFD12345.1, ECO:0000313|Proteomes:UP000199263};
RN   [1] {ECO:0000313|EMBL:SFD12345.1, ECO:0000313|Proteomes:UP000199263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12992 {ECO:0000313|EMBL:SFD12345.1,
RC   ECO:0000313|Proteomes:UP000199263};
RA   de Groot N.N.;
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}.
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DR   EMBL; FOMG01000020; SFD12345.1; -; Genomic_DNA.
DR   BioCyc; GCF_900112485:BM027_RS12775-MONOMER; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000199263; 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:UP000199263};
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:UP000199263};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      351    424       ACT. {ECO:0000259|PROSITE:PS51671}.
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   433 AA;  47877 MW;  001787FB783BE686 CRC64;
     MKKVRIALLG LGNVGRGVCM ILNSNKEEIM KRSGYEVEIA KILVRDKNKP RGVKVPDEIV
     TTNFNEIIED DSIKIVIEVM GGIDPAREYM LKCMDAGKHI VTANKMLLAT DGDALFEKAD
     SKGLMFKYEA SVAGGIPIIN GIDESLTANK IKELYGIING TTNYILTKME SEGLGFDEAL
     KEAQDMGYAE ADPTSDIEGY DAQYKLAILS SLAFGTKIVV DNVYREGITK IKPIDMEYAK
     EFKMVIKLLA IVKEKDDKLE LRVHPTMIPK KHPLANVYDS FNAVFVKGNA VGDLMFYGRG
     AGDLPTGSAV VSDVISILRS NVDLENCNPV VKNNLWDRKI GSIRDVESKF YIRATVLDEP
     GVLGEITAIL GKHNVSLRSV IQKGEENEKG QVTIVLVTHT VTQAQIFDAF HKISELKSVN
     NIDNIIRIED FKN
//
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