ID A0A2H1A6V9_CANAR Unreviewed; 359 AA.
AC A0A2H1A6V9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|PIRNR:PIRNR036497};
DE Short=HDH {ECO:0000256|PIRNR:PIRNR036497};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|PIRNR:PIRNR036497};
GN ORFNames=B9J08_000055 {ECO:0000313|EMBL:PIS58609.1};
OS Candida auris (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=498019 {ECO:0000313|EMBL:PIS58609.1, ECO:0000313|Proteomes:UP000230249};
RN [1] {ECO:0000313|EMBL:PIS58609.1, ECO:0000313|Proteomes:UP000230249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B8441 {ECO:0000313|EMBL:PIS58609.1,
RC ECO:0000313|Proteomes:UP000230249};
RX PubMed=27988485; DOI=.1093/cid/ciw691;
RA Lockhart S.R., Etienne K.A., Vallabhaneni S., Farooqi J., Chowdhary A.,
RA Govender N.P., Colombo A.L., Calvo B., Cuomo C.A., Desjardins C.A.,
RA Berkow E.L., Castanheira M., Magobo R.E., Jabeen K., Asghar R.J.,
RA Meis J.F., Jackson B., Chiller T., Litvintseva A.P.;
RT "Simultaneous emergence of multidrug-resistant Candida auris on 3
RT continents confirmed by whole-genome sequencing and epidemiological
RT analyses.";
RL Clin. Infect. Dis. 64:134-140(2017).
RN [2] {ECO:0007829|PDB:7M92}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RG Center for Structural Genomics of Infectious Diseases (CSGID);
RA Chang C., Evdokimova E., Savchenko A., Joachimiak A.;
RT "Crystal structure of unknown function protein protein B9J08_000055 Candida
RT auris.";
RL Submitted (MAR-2021) to the PDB data bank.
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 Evidence={ECO:0000256|PIRNR:PIRNR036497};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00005062}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5. {ECO:0000256|ARBA:ARBA00005056}.
CC -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC {ECO:0000256|PIRNR:PIRNR036497}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIS58609.1}.
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DR EMBL; PEKT02000001; PIS58609.1; -; Genomic_DNA.
DR PDB; 7M92; X-ray; 2.35 A; A/B=1-359.
DR AlphaFoldDB; A0A2H1A6V9; -.
DR SMR; A0A2H1A6V9; -.
DR STRING; 498019.A0A2H1A6V9; -.
DR EnsemblFungi; B9J08_000055-t37_1; B9J08_000055-t37_1-p1; B9J08_000055.
DR VEuPathDB; FungiDB:B9J08_000055; -.
DR VEuPathDB; FungiDB:CJI96_0001492; -.
DR VEuPathDB; FungiDB:CJI97_000061; -.
DR VEuPathDB; FungiDB:CJJ07_002903; -.
DR VEuPathDB; FungiDB:CJJ09_002021; -.
DR VEuPathDB; FungiDB:QG37_05767; -.
DR OMA; DWQSAFS; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000230249; Unassembled WGS sequence.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:InterPro.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009090; P:homoserine biosynthetic process; IEA:EnsemblFungi.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR011147; Bifunc_aspartokin/hSer_DH.
DR InterPro; IPR001342; HDH_cat.
DR InterPro; IPR022697; HDH_short.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43070; -; 1.
DR PANTHER; PTHR43070:SF5; HOMOSERINE DEHYDROGENASE; 1.
DR Pfam; PF00742; Homoserine_dh; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR PIRSF; PIRSF036497; HDH_short; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7M92};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR036497};
KW Branched-chain amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR036497};
KW Isoleucine biosynthesis {ECO:0000256|PIRNR:PIRNR036497};
KW Methionine biosynthesis {ECO:0000256|PIRNR:PIRNR036497};
KW NADP {ECO:0000256|PIRNR:PIRNR036497, ECO:0000256|PIRSR:PIRSR036497-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR036497};
KW Reference proteome {ECO:0000313|Proteomes:UP000230249};
KW Threonine biosynthesis {ECO:0000256|PIRNR:PIRNR036497}.
FT DOMAIN 11..135
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 149..351
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
FT ACT_SITE 221
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-1"
FT BINDING 11..16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT BINDING 89
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT BINDING 113
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
SQ SEQUENCE 359 AA; 38560 MW; B571ED4D99CDC53F CRC64;
MSKSVNVAII GAGVVGSAFI NQLANLKAPV AFKVVYLARS SKEAVFSKDY SAVDLKNYKT
APAQAVLPLD ELTSYLTAAK RPTILVDNTS NSSIADFYPK FVEAGISIAT PNKKAFSSDL
ATWNDIFKKS AAANGGLVYH EATVGAGLPI IGPLRDLVLT GDKVEKIEGI LSGSLSYVFN
TLSTSEKSDK KFSDVVKVAK DLGYLERDPR DDLNGMDFAR KVTILARIAG FEVESPNSFA
VDSLVPQPLE SLATGAEFLE KLPEYDNDFQ KRKDDALAEN KVLRYVGQVD FKANKVSVGI
AKYDFDHPFA SLKGSDNVVS IKTERYPNPL IIQGAGAGAE VTAHGVLADA IKIAERIAN
//
