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Database: UniProt
Entry: A0A2I2G6N8_9EURO
LinkDB: A0A2I2G6N8_9EURO
Original site: A0A2I2G6N8_9EURO 
ID   A0A2I2G6N8_9EURO        Unreviewed;       388 AA.
AC   A0A2I2G6N8;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=D-serine dehydratase-like domain-containing protein {ECO:0000259|SMART:SM01119};
GN   ORFNames=P170DRAFT_438118 {ECO:0000313|EMBL:PLB48536.1};
OS   Aspergillus steynii IBT 23096.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB48536.1, ECO:0000313|Proteomes:UP000234275};
RN   [1] {ECO:0000313|EMBL:PLB48536.1, ECO:0000313|Proteomes:UP000234275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB48536.1,
RC   ECO:0000313|Proteomes:UP000234275};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DSD1 family.
CC       {ECO:0000256|ARBA:ARBA00005323}.
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:PLB48536.1}.
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DR   EMBL; MSFO01000005; PLB48536.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2G6N8; -.
DR   VEuPathDB; FungiDB:P170DRAFT_438118; -.
DR   OrthoDB; 5473289at2759; -.
DR   Proteomes; UP000234275; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProt.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   Gene3D; 2.40.37.20; D-serine dehydratase-like domain; 1.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR026956; D-ser_dehydrat-like_dom.
DR   InterPro; IPR042208; D-ser_dehydrat-like_sf.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR28004:SF2; D-SERINE DEHYDRATASE; 1.
DR   PANTHER; PTHR28004; ZGC:162816-RELATED; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   Pfam; PF14031; D-ser_dehydrat; 1.
DR   SMART; SM01119; D-ser_dehydrat; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000234275}.
FT   DOMAIN          253..364
FT                   /note="D-serine dehydratase-like"
FT                   /evidence="ECO:0000259|SMART:SM01119"
SQ   SEQUENCE   388 AA;  42108 MW;  86AEC33D15DAF027 CRC64;
     MQMGSSETFD VNLVASTVNE IHHLVPLLQE FQAQHRRVNV LYGIPLVPSQ VPRLASLART
     LGEDTIAVMI DHPAQIDFLS EFHRLAGLPA SVFIKVDTGY HRAGLPPTGL NKADLLKRLA
     QAERDGHARL LGVYSHSSLS YAGSTPEEAM GHLTAEITGC RDAVRHHVDL LPDRELVISV
     GATPQAASVQ NLLQGQTSAA ASAEARGLRE LLRDPLPGAR VKVELHAGNY AVLDMQQLET
     QAESRGRPDD EVAISVVAEV CSLYNGGERA QPEALLAAGT LALGREPCHS YPGWGVIGQW
     RREAASRRLI LARISQEHSI VTWEKGRDGD EVPDIPLEVG QAVRVYPNHS CVTGAMHGWY
     LVVDSDLEEG SKVVDVWVRA RGYSALPA
//
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