UniProt: C1G1C3

Database: UniProt
Entry: C1G1C3_PARBD

LinkDB:  C1G1C3_PARBD 
Original site:  C1G1C3_PARBD

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
Enzyme (1)   
   BRENDA (1)   
All databases (22)   

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ID   C1G1C3_PARBD            Unreviewed;       372 AA.
AC   C1G1C3;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
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=PADG_00663 {ECO:0000313|EMBL:EEH44374.1};
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH44374.1, ECO:0000313|Proteomes:UP000001628};
RN   [1] {ECO:0000313|EMBL:EEH44374.1, ECO:0000313|Proteomes:UP000001628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18 {ECO:0000313|EMBL:EEH44374.1,
RC   ECO:0000313|Proteomes:UP000001628};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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         ECO:0000256|RuleBase:RU000579};
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, ECO:0000256|RuleBase:RU000579}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 3/5. {ECO:0000256|ARBA:ARBA00005056,
CC       ECO:0000256|RuleBase:RU000579}.
CC   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC       {ECO:0000256|PIRNR:PIRNR036497, ECO:0000256|RuleBase:RU004171}.
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DR   EMBL; KN275957; EEH44374.1; -; Genomic_DNA.
DR   RefSeq; XP_010756447.1; XM_010758145.1.
DR   AlphaFoldDB; C1G1C3; -.
DR   SMR; C1G1C3; -.
DR   STRING; 502780.C1G1C3; -.
DR   GeneID; 22580469; -.
DR   KEGG; pbn:PADG_00663; -.
DR   VEuPathDB; FungiDB:PADG_00663; -.
DR   eggNOG; KOG0455; Eukaryota.
DR   HOGENOM; CLU_009116_0_1_1; -.
DR   InParanoid; C1G1C3; -.
DR   OMA; DWQSAFS; -.
DR   OrthoDB; 5487989at2759; -.
DR   BRENDA; 1.1.1.3; 6937.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000001628; 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: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; IPR019811; HDH_CS.
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.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR036497};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW   ECO:0000256|RuleBase:RU000579};
KW   Isoleucine biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW   ECO:0000256|RuleBase:RU000579};
KW   Methionine biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW   ECO:0000256|RuleBase:RU000579};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR036497};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036497};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW   Threonine biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW   ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN          12..149
FT                   /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03447"
FT   DOMAIN          158..365
FT                   /note="Homoserine dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00742"
FT   ACT_SITE        234
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-1"
FT   BINDING         12..17
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT   BINDING         99
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT   BINDING         123
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT   BINDING         219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
SQ   SEQUENCE   372 AA;  39368 MW;  9D41C4FAE588C3E8 CRC64;
     MSGKTIYLGV IGVGGVGAHF LTQLSRLPNA PSLVLLARSS QTVTSPAPSY SPAIAPSDWQ
     SAFSTSSSAS YTQSGAWNPD QIAAYLSKAP GRAVLVDNTS DPTVADAYPL FLSKGISIVT
     PNKKAFSSSF NLWKNIFNTA ASTSSLVYHE STVGAGLPVV STLRDLVATG DRITRIEGVF
     SGTLSFLFNS FAPATAQSGV SAQKWSQVVA QAKDLGYTEP DPRDDLNGMD VARKVTILAR
     IAGLEVQSPE SFPVESLIPA KLRGLTSAAE FMQRLPDFDD QMEAIKNQAE AEGKIVRYVG
     RVDVEGKVVK VGLQQFDKDS AIAGLKGSDN IISFYTERYG KNPLIIQGAG AGGAVTAMGV
     TADLIKVLER LH
//

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