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Database: UniProt
Entry: A0A0M2NHN9_9FIRM
LinkDB: A0A0M2NHN9_9FIRM
Original site: A0A0M2NHN9_9FIRM 
ID   A0A0M2NHN9_9FIRM        Unreviewed;       424 AA.
AC   A0A0M2NHN9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   16-JAN-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=CHK_0845 {ECO:0000313|EMBL:KKI51678.1};
OS   Catabacter hongkongensis.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Catabacteriaceae;
OC   Catabacter.
OX   NCBI_TaxID=270498 {ECO:0000313|EMBL:KKI51678.1, ECO:0000313|Proteomes:UP000034076};
RN   [1] {ECO:0000313|EMBL:KKI51678.1, ECO:0000313|Proteomes:UP000034076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKU16 {ECO:0000313|EMBL:KKI51678.1,
RC   ECO:0000313|Proteomes:UP000034076};
RA   Lau S.K., Teng J.L., Huang Y., Curreem S.O., Tsui S.K., Woo P.C.;
RT   "Draft genome sequence of bacteremic isolate Catabacter hongkongensis
RT   type strain HKU16T.";
RL   Submitted (APR-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:KKI51678.1}.
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DR   EMBL; LAYJ01000068; KKI51678.1; -; Genomic_DNA.
DR   RefSeq; WP_046442766.1; NZ_LLYX01000024.1.
DR   EnsemblBacteria; KKI51678; KKI51678; CHK_0845.
DR   PATRIC; fig|270498.16.peg.444; -.
DR   OrthoDB; 1464088at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000034076; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034076};
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   ECO:0000313|EMBL:KKI51678.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034076};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      345    421       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       9     16       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   COILED      393    413       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    201    201       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     101    101       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     186    186       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   424 AA;  46444 MW;  49C14B09B6F87715 CRC64;
     MKDIKVAILG MGTVGGGIYQ LIEKEQKNIE HKENIHLEVK KTLALNYAVD VPDSKKAKDI
     DEIINDPEIT IVAEVMGGLK PSKEFIIKAL EAGKTVVSAN KDMISQNWPD LEAAAKRGNA
     GFYFEAAVGG GIPILRALND SMQANSIDRI YGIVNGTTNY ILTKMDDEGR DFDDVLKEAQ
     ELGYAEANPT SDVEGYDARY KLSILASMAF HARVPVDKIY CEGITKITKL DIEIGRELGY
     VVKLLAIGKK DENGEIEVRV HPTMIPKDHA LASIKGSFNA IFINGSAVGE MMWYGKGAGD
     FPTASALVSD MIYSVGAPNP RYVTFENSYD ANQVKFNDNW LTEYFVRTNV LDKPGVLAKI
     AGILGKHDVS IESVIQKGAK KGEQSAPLIL VTHKAHEKDL QKAIEEIKEL DAVVNVPSCI
     RVEK
//
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