ID   Q1DG19_MYXXD            Unreviewed;       494 AA.
AC   Q1DG19;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   08-OCT-2025, entry version 113.
DE   SubName: Full=Methylmalonate-semialdehyde dehydrogenase {ECO:0000313|EMBL:ABF91275.1};
DE            EC=1.2.1.27 {ECO:0000313|EMBL:ABF91275.1};
GN   Name=mmsA {ECO:0000313|EMBL:ABF91275.1};
GN   OrderedLocusNames=MXAN_0121 {ECO:0000313|EMBL:ABF91275.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF91275.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF91275.1, ECO:0000313|Proteomes:UP000002402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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DR   EMBL; CP000113; ABF91275.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1DG19; -.
DR   STRING; 246197.MXAN_0121; -.
DR   EnsemblBacteria; ABF91275; ABF91275; MXAN_0121.
DR   KEGG; mxa:MXAN_0121; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_10_7; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006574; P:L-valine catabolic process; IEA:TreeGrafter.
DR   GO; GO:0006210; P:thymine catabolic process; IEA:TreeGrafter.
DR   CDD; cd07085; ALDH_F6_MMSDH; 1.
DR   FunFam; 3.40.309.10:FF:000002; Methylmalonate-semialdehyde dehydrogenase (Acylating); 1.
DR   Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1.
DR   Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR010061; MeMal-semiAld_DH.
DR   NCBIfam; TIGR01722; MMSDH; 1.
DR   PANTHER; PTHR43866; MALONATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43866:SF4; MALONATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABF91275.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002402}.
FT   DOMAIN          28..480
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   494 AA;  52030 MW;  C1874D4E63BA9E3B CRC64;
     MSFIQLPRSV VSCRNLVGGS WQVPPGAAHL DVRSPYTGTV IGRVPLTPAS GVAQAVEAAK
     AAAAAWKNTS LRERTQYLYR FRQFLERDLD ALAQLAASEA GKTVAEARAG LLKGMEVCDF
     ALSLQNLDTG AHLEVSRGIS CEYRREPLGV VAGITPFNFP AMVPMWMFPI AVTLGNAFIL
     KPSEKVPLTA CALGELMCEA GYPAGVFSVV HGGKEAVDAL VAHPDVQAVG FVGSSAVARH
     LYAEGCKRGK RVLALGSAKN HLIVVPDADP ELTPQAVVDS FTGCAGQRCM AASVLLAVGN
     VESLLQEVVR RAAKLELGPG MGALIDRGSL DRLETAIARA EAEGARVLLD GRGHKPQGEP
     WSGGNWLGPT LLDGVRPEME AARRELFGPV LSIVRVPTLS AALAVENASP YGNAASIFTT
     NGGVAQTVVE GVRAGMVGVN VGVPVPREPF SFGGTGDSRF GHGDITGPSS LDFWTQVKKV
     TRKWSARTDG SWMS
//