ID Q5ALM0_CANAL Unreviewed; 365 AA.
AC Q5ALM0;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120};
DE EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120};
GN Name=HOM2 {ECO:0000313|CGD:CAL0000179646,
GN ECO:0000313|EMBL:AOW27277.1};
GN OrderedLocusNames=CAALFM_C202370CA {ECO:0000313|EMBL:AOW27277.1},
GN orf19.9132 {ECO:0000313|CGD:CAL0000179646};
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561 {ECO:0000313|EMBL:AOW27277.1, ECO:0000313|Proteomes:UP000000559};
RN [1] {ECO:0000313|EMBL:AOW27277.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2] {ECO:0000313|EMBL:AOW27277.1, ECO:0000313|Proteomes:UP000000559}
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=17419877; DOI=.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3] {ECO:0007829|PDB:3HSK}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NADP(+).
RX PubMed=20124701; DOI=10.1107/S0907444909052834;
RA Arachea B.T., Liu X., Pavlovsky A.G., Viola R.E.;
RT "Expansion of the aspartate beta-semialdehyde dehydrogenase family: the
RT first structure of a fungal ortholog.";
RL Acta Crystallogr. D 66:205-212(2010).
RN [4] {ECO:0000313|EMBL:AOW27277.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=24025428; DOI=.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-
CC L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00001636};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00005076}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00005021}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 2/5. {ECO:0000256|ARBA:ARBA00005097}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010584}.
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DR EMBL; CP017624; AOW27277.1; -; Genomic_DNA.
DR RefSeq; XP_722601.1; XM_717508.2.
DR PDB; 3HSK; X-ray; 2.20 A; A/B=1-365.
DR PDBsum; 3HSK; -.
DR AlphaFoldDB; Q5ALM0; -.
DR SMR; Q5ALM0; -.
DR STRING; 237561.Q5ALM0; -.
DR EnsemblFungi; C2_02370C_A-T; C2_02370C_A-T-p1; C2_02370C_A.
DR GeneID; 3635826; -.
DR KEGG; cal:CAALFM_C202370CA; -.
DR CGD; CAL0000179646; HOM2.
DR VEuPathDB; FungiDB:C2_02370C_A; -.
DR eggNOG; KOG4777; Eukaryota.
DR HOGENOM; CLU_049966_1_0_1; -.
DR InParanoid; Q5ALM0; -.
DR OMA; CEEEMKM; -.
DR OrthoDB; 6339at2759; -.
DR BRENDA; 1.2.1.11; 1096.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR EvolutionaryTrace; Q5ALM0; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0009090; P:homoserine biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009088; P:threonine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000319; Asp-semialdehyde_DH_CS.
DR InterPro; IPR005676; Asp_semi-ald_DH_pep-lack.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR NCBIfam; TIGR00978; asd_EA; 1.
DR PANTHER; PTHR46718; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR46718:SF1; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR PIRSF; PIRSF000148; ASA_dh; 1.
DR SMART; SM00859; Semialdhyde_dh; 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; PS01103; ASD; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3HSK}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0007829|PDB:3HSK};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000559}.
FT DOMAIN 5..132
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 156
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT BINDING 12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:3HSK"
FT BINDING 13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:3HSK"
FT BINDING 14
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:3HSK"
FT BINDING 37
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:3HSK"
FT BINDING 86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007829|PDB:3HSK"
SQ SEQUENCE 365 AA; 39225 MW; 74C1DD511829C5EB CRC64;
MSVKKAGVLG ATGSVGQRFI LLLSKHPEFE IHALGASSRS AGKKYKDAAS WKQTETLPET
EQDIVVQECK PEGNFLECDV VFSGLDADVA GDIEKSFVEA GLAVVSNAKN YRREKDVPLV
VPIVNPEHID VVENKVKQAV SKGGKKPGFI ICISNCSTAG LVAPLKPLVE KFGPIDALTT
TTLQAISGAG FSPGVSGMDI LDNIVPYISG EEDKLEWETK KILGGVNAEG TEFVPIPESE
MKVSAQCNRV PVIDGHTECI SLRFANRPAP SVEDVKQCLR EYECAASKLG CHSAPKQTIH
VLDQPDRPQP RLDRDRDSGY GVSVGRIRED SLLDFKMVVL SHNTIIGAAG AGILIAEILK
AKNII
//
