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Database: UniProt
Entry: A0A2Z5R318_9MICC
LinkDB: A0A2Z5R318_9MICC
Original site: A0A2Z5R318_9MICC 
ID   A0A2Z5R318_9MICC        Unreviewed;       191 AA.
AC   A0A2Z5R318;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:BAV88944.1};
GN   ORFNames=RA11412_2645 {ECO:0000313|EMBL:BAV88944.1};
OS   Rothia aeria.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Rothia.
OX   NCBI_TaxID=172042 {ECO:0000313|EMBL:BAV88944.1, ECO:0000313|Proteomes:UP000250241};
RN   [1] {ECO:0000313|EMBL:BAV88944.1, ECO:0000313|Proteomes:UP000250241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 11412 {ECO:0000313|EMBL:BAV88944.1,
RC   ECO:0000313|Proteomes:UP000250241};
RA   Nambu T.;
RT   "Genome sequence of Rothia aeria strain JCM11412.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00010584}.
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DR   EMBL; AP017895; BAV88944.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z5R318; -.
DR   KEGG; raj:RA11412_2645; -.
DR   Proteomes; UP000250241; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
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   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000250241}.
FT   DOMAIN          2..51
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01118"
FT   DOMAIN          75..182
FT                   /note="Semialdehyde dehydrogenase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02774"
SQ   SEQUENCE   191 AA;  20795 MW;  68BB366FA1522244 CRC64;
     MTAQGGDYTK EVHPKLRESG WEGLWIDAAS ALRMNDDAII VLDPINRDVI DRGLESGVKD
     FIGGNCTVSC LLMGLGGLFK QGLVEWTTSM TYQAASGGGA RHMREVLGQF RDLGNEVSAE
     LNDPAAAILE IDRKVLAKQR SGELDTAQFG VPLSGSLIPW IDSDLGNGQS REEWKSDAET
     NKFWVLRAIT V
//
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