ID A0A0S7DNS0_9EURO Unreviewed; 582 AA.
AC A0A0S7DNS0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN ORFNames=ALT_001246 {ECO:0000313|EMBL:GIM38854.1}, CNMCM8060_005621
GN {ECO:0000313|EMBL:KAF4170381.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM38854.1};
RN [1] {ECO:0000313|EMBL:GIM38854.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM38854.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
RN [2] {ECO:0000313|EMBL:KAF4170381.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4170381.1};
RA dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT fumigatiaffinis.";
RL bioRxiv 0:0-0(2020).
RN [3] {ECO:0000313|EMBL:KAF4170381.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4170381.1};
RA Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+)
CC + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95;
CC Evidence={ECO:0000256|ARBA:ARBA00001878,
CC ECO:0000256|RuleBase:RU363003};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 1/3. {ECO:0000256|ARBA:ARBA00005216,
CC ECO:0000256|RuleBase:RU363003}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU363003}.
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:GIM38854.1}.
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DR EMBL; BCLY01000008; GIM38854.1; -; Genomic_DNA.
DR EMBL; JAAAPS010000343; KAF4170381.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DNS0; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_4523; -.
DR OrthoDB; 6392at2759; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000713487; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd04902; ACT_3PGDH-xct; 1.
DR CDD; cd12173; PGDH_4; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR029009; ASB_dom_sf.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006236; PGDH.
DR InterPro; IPR045626; PGDH_ASB_dom.
DR NCBIfam; TIGR01327; PGDH; 1.
DR PANTHER; PTHR42938:SF22; D-3-PHOSPHOGLYCERATE DEHYDROGENASE; 1.
DR PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF19304; PGDH_inter; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF143548; Serine metabolism enzymes domain; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU363003};
KW NAD {ECO:0000256|RuleBase:RU363003};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363003};
KW Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT DOMAIN 11..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..291
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT DOMAIN 334..440
FT /note="D-3-phosphoglycerate dehydrogenase ASB"
FT /evidence="ECO:0000259|Pfam:PF19304"
FT REGION 443..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 582 AA; 60932 MW; 54EF734285E1B93E CRC64;
MPSAKPPPPK VLVPEKLSPD GLALLRASLE VDERKGLDAD ELLQIIPEYE ALVVRSETKV
TASLLRAAKQ LKVVARAGVG VDNVDVEEAT KLGIVVVNSP SGNIGAAAEH TIALLMAMAR
NIPEACSSLK SGKWERSKFV GVEVKGKTLS IIGLGKVGLT VARLAKGLGM NVNALDPYAS
PAVAASASVT LVSSLSELLT TADFLTIHTP LIASTKGMIS TAELAQMKAG SRILNVARGG
TIDEAALLEA LDAGHLAAAA IDVFTSEPPQ PDSTAARLIA HPRAVVTPHL GASTVEAQEN
VSIDVCEQVL QILNGSLPRS AVNAPLILPE EYRKLQPFVR LVEKMGSLYT QHYASTVGGS
MTRNTFDLIY HGEVAGISNT RPLFAALIKG LLAPISSSEG ININIVNAEL VARERGIFVN
EQHSRDPADH SYSSLVTLVA RPPSRASSRA PAPEATSQVG PVPQDQRIIS GTCSGDQPLI
NRLGRFETSF VPEGTLLICE NYDSPGKIGA VGSLLGQEGV NINFMTVAPV SRKFALASGE
TDDGGSKHEA LMILGIDKVV DQRVADGLVK GGGVLSASVI SL
//
