(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BIW0_GEOS0

ID   A0A0F6BIW0_GEOS0        Unreviewed;       433 AA.
AC   A0A0F6BIW0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 23.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   OrderedLocusNames=GY4MC1_0529 {ECO:0000313|EMBL:ADP73361.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73361.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73361.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73361.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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; CP002293; ADP73361.1; -; Genomic_DNA.
DR   RefSeq; WP_003248309.1; NC_014650.1.
DR   EnsemblBacteria; ADP73361; ADP73361; GY4MC1_0529.
DR   GeneID; 29236816; -.
DR   KEGG; gmc:GY4MC1_0529; -.
DR   KO; K00003; -.
DR   OMA; FEASVCG; -.
DR   OrthoDB; 1464088at2; -.
DR   BioCyc; GSP581103:G1GOQ-580-MONOMER; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000002034; 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;
DR   PRODOM; A0A0F6BIW0.
DR   SWISS-2DPAGE; A0A0F6BIW0.
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:UP000002034};
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   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      351    426       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND      10     17       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   COILED      398    418       {ECO:0000256|SAM:Coils}.
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   433 AA;  47422 MW;  B1B6BD8F766EFD54 CRC64;
     MAKPIFVGLL GLGTVGSGVV KIIENHQERL MHQVGCPVQV KKILVRDIYK QRDVRVDPSL
     LTTDVADVID DPEIDVVIEV MGGIEETREY LLRALQQGKH VVTANKDLMA LHGSELLAVA
     AENHCDLFFE ASVAGGIPIL RSLVDGLASD RITKMMGIVN GTTNYILTKM SKYGASYEEV
     LAEAQALGYA EADPTSDVEG LDAARKMAIL ARLGFSMNID LEDVQAKGIT SITEEDLNYS
     KRLGYTMKLI GIAQRDGNKV EVSVQPTLLP DSHPLASVND EYNAVYVYGE AVGETMFYGP
     GAGSLPTATA VVSDLVAVMK NMRLGVNGCN AVAPQYEKQL KSPSEIFSKY FLRIRVKDQV
     GAFAKITTLF SERGVSFEKI LQLPLKEDGL AEIVIVTHRA SQQDYEEILQ QLRELEIVHE
     VKSSYRVEGE GKE
//

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