DHOM_EMENI
ID DHOM_EMENI Reviewed; 368 AA.
AC Q5B998; C8VJA1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Homoserine dehydrogenase;
DE Short=HDH;
DE EC=1.1.1.3;
GN ORFNames=AN2882;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17258477; DOI=10.1016/j.fgb.2006.12.001;
RA Kim Y., Nandakumar M.P., Marten M.R.;
RT "Proteome map of Aspergillus nidulans during osmoadaptation.";
RL Fungal Genet. Biol. 44:886-895(2007).
CC -!- FUNCTION: Involved in osmoadaptation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADH; Xref=Rhea:RHEA:15757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5.
CC -!- INDUCTION: Down-regulated when grown with elevated levels of potassium
CC chloride. {ECO:0000269|PubMed:17258477}.
CC -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AACD01000051; EAA63453.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF83817.1; -; Genomic_DNA.
DR RefSeq; XP_660486.1; XM_655394.1.
DR AlphaFoldDB; Q5B998; -.
DR SMR; Q5B998; -.
DR STRING; 162425.CADANIAP00010207; -.
DR EnsemblFungi; CBF83817; CBF83817; ANIA_02882.
DR EnsemblFungi; EAA63453; EAA63453; AN2882.2.
DR GeneID; 2873909; -.
DR KEGG; ani:AN2882.2; -.
DR VEuPathDB; FungiDB:AN2882; -.
DR eggNOG; KOG0455; Eukaryota.
DR HOGENOM; CLU_009116_0_1_1; -.
DR InParanoid; Q5B998; -.
DR OMA; FNEFSTT; -.
DR OrthoDB; 998704at2759; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:InterPro.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009067; P:aspartate family amino acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0071470; P:cellular response to osmotic stress; IEP:AspGD.
DR GO; GO:0009090; P:homoserine biosynthetic process; IBA:GO_Central.
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; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR011147; Bifunc_aspartokin/hSer_DH.
DR InterPro; IPR001342; HDH_cat.
DR InterPro; IPR019811; HDH_CS.
DR InterPro; IPR022697; HDH_short.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43070; PTHR43070; 1.
DR Pfam; PF00742; Homoserine_dh; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR PIRSF; PIRSF036497; HDH_short; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Isoleucine biosynthesis; Methionine biosynthesis; NADP; Oxidoreductase;
KW Reference proteome; Stress response; Threonine biosynthesis.
FT CHAIN 1..368
FT /note="Homoserine dehydrogenase"
FT /id="PRO_0000348284"
FT ACT_SITE 227
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 10..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 368 AA; 38652 MW; 487985B2CF176A79 CRC64;
MSAPIYLGVI GVGGVGTAFL NQLARLPNAP KLILLARSSQ TLLSPTPSYS PTIPAAEWKT
AVETPSLTKS GALTPDEIAT YLASAPGRSI LVDNTSDPAL ASNYPVFLRK GISVVTPNKK
GFSSDLSLWK EIFAAAAEGK ALVYHESTVG AGLPVISTLK DLVNTGDEVT RIEGVFSGTL
SFLFNTFAPA SGSSSAKWSE VVSQAKELGY TEPDPRDDLN GMDVARKLTI LARIAGLDVQ
SPDSFPIESL IPAELTSLPS SADGIAQFMA RLPEFDSQMA AIKEGAEKAG KVVRYVGSVD
VAKKEVRVGL QQFDKDSAIA GLKGSDNIIS FYTRRYGSNP LIVQGAGAGG DVTAMGVTAD
LLKVIERL
