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Database: UniProt
Entry: D2NRG6_ROTMD
LinkDB: D2NRG6_ROTMD
Original site: D2NRG6_ROTMD 
ID   D2NRG6_ROTMD            Unreviewed;       404 AA.
AC   D2NRG6;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120};
DE            EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120};
GN   OrderedLocusNames=RMDY18_04100 {ECO:0000313|EMBL:BAI64242.1};
OS   Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Rothia.
OX   NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI64242.1, ECO:0000313|Proteomes:UP000001883};
RN   [1] {ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA   Fukushima H.;
RT   "Complete genome sequence of Rothia mucilaginosa DJ.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAI64242.1, ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|EMBL:BAI64242.1,
RC   ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H.,
RA   Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., Fukushima H.;
RT   "Isolation and identification of Rothia mucilaginosa from persistent apical
RT   periodontitis lesions.";
RL   J Osaka Dent Univ 44:93-98(2010).
RN   [3] {ECO:0000313|EMBL:BAI64242.1, ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|EMBL:BAI64242.1,
RC   ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., Leung K.-P.,
RA   Fukushima H.;
RT   "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate
RT   with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis
RT   Lesion.";
RL   Sequencing 2010:457236-457236(2010).
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; AP011540; BAI64242.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2NRG6; -.
DR   STRING; 680646.RMDY18_04100; -.
DR   KEGG; rmu:RMDY18_04100; -.
DR   eggNOG; COG0136; Bacteria.
DR   HOGENOM; CLU_066397_0_0_11; -.
DR   OMA; MFDVPDE; -.
DR   UniPathway; UPA00034; UER00016.
DR   UniPathway; UPA00050; UER00463.
DR   UniPathway; UPA00051; UER00464.
DR   Proteomes; UP000001883; Chromosome.
DR   GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
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:0009097; P:isoleucine biosynthetic process; IEA:InterPro.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
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; IPR000319; Asp-semialdehyde_DH_CS.
DR   InterPro; IPR011534; Asp_ADH_gamma-type.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR   NCBIfam; TIGR01745; asd_gamma; 1.
DR   PANTHER; PTHR46278:SF4; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR46278; DEHYDROGENASE, PUTATIVE-RELATED; 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   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001883}.
FT   DOMAIN          33..154
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        167
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT   ACT_SITE        308
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ   SEQUENCE   404 AA;  44259 MW;  75953090FAE468B5 CRC64;
     MFRSEYQIFC TVLSRMRQPE STLGTMNFNP GDSVGFVGWR GMVGSVLMKR MVEEGDFEGI
     TPVFFTTSNV GGQAPTFDGV LEPSELKDAY DIDELRKHSI IVTAQGGSYT EAVHPKLRAA
     GWDGLWIDAA STLRMNDDSI IVLDPINRDV IDRGLASGVK DYIGGNCTVS CLLMGLGGLF
     KNDLVEWATS MTYQAASGGG ARHMREVLAQ FRDLGNEVAA ELDDPASAIL DIDRKVLAKQ
     RSGELDSTQF GVPLSGSLIP WIDSDLGNGQ SREEWKAEVE TNKILGRFAD DKVTMDGLCV
     RIAAMRSHSQ ALTIKLKKDL PLEEIERIIA EDNPWVRFVP NEREASMEQL TPVAASGSLE
     IPVGRVRKLA MGPEYISAFT VGDQLLWGAA EPIRRMLQIA VGKL
//
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