ID Q1DEM9_MYXXD Unreviewed; 483 AA.
AC Q1DEM9;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN OrderedLocusNames=MXAN_0626 {ECO:0000313|EMBL:ABF90874.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF90874.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF90874.1, 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).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP000113; ABF90874.1; -; Genomic_DNA.
DR RefSeq; WP_011550757.1; NC_008095.1.
DR AlphaFoldDB; Q1DEM9; -.
DR STRING; 246197.MXAN_0626; -.
DR EnsemblBacteria; ABF90874; ABF90874; MXAN_0626.
DR GeneID; 41358104; -.
DR KEGG; mxa:MXAN_0626; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_3_1_7; -.
DR OrthoDB; 9762436at2; -.
DR Proteomes; UP000002402; Chromosome.
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:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR CDD; cd07134; ALDH_AlkH-like; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR036492};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402}.
FT DOMAIN 11..450
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 225
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 259
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 483 AA; 53049 MW; ED70537298CDF92C CRC64;
MLEAASQANT QPTADTERIR AVFEAQRAHR WTMSRTTAAE RIARLKRLRE AIIARRAELA
DAIHADFRKP AMEVDLTELH PTLEELNHTV RHLKSWMKPM RVGTPMLLAG SSSHVRYEAR
GTVLLLSPWN YPFNLLVSPL VAAIAAGNTV ICKPSEKTPH TSRFLAQLVK DVFPENEVAL
FEGGAETAEA LLELPFDHIF FTGNTRIGRK VMEAAAKHLA SVTLELGGKS PVIVDETADV
AAAAERLCWG KFVNGGQTCV APDYVFVHAS KERAFLDALK ASITRFYGGT EQERQASPDL
TRLVDPVAWR RVKDLLKRSV AAGAKVEVGG ETDEPSRYIA PTVLSGVTAE NPVMEGEIFG
PVLPVLTFQS REEVYAHIRA GGKPLALYVF SQDKRAVEDI FQNTTSGGAV VNNVLVHLAN
PNLPFGGVGT SGLGNYHGHF GFKTFSHERA VMVQWMKSLA SVFFPPYRGK AQELASRATR
LME
//
