ID B9EA36_MACCJ Unreviewed; 492 AA. AC B9EA36; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 75. DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:BAH17097.1}; GN Name=aldA {ECO:0000313|EMBL:BAH17097.1}; GN OrderedLocusNames=MCCL_0390 {ECO:0000313|EMBL:BAH17097.1}; OS Macrococcus caseolyticus (strain JCSC5402). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Macrococcus. OX NCBI_TaxID=458233 {ECO:0000313|EMBL:BAH17097.1, ECO:0000313|Proteomes:UP000001383}; RN [1] {ECO:0000313|EMBL:BAH17097.1, ECO:0000313|Proteomes:UP000001383} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCSC5402 {ECO:0000313|EMBL:BAH17097.1, RC ECO:0000313|Proteomes:UP000001383}; RX PubMed=19074389; DOI=10.1128/JB.01058-08; RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.; RT "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402, RT reflecting the ancestral genome of the human-pathogenic staphylococci."; RL J. Bacteriol. 191:1180-1190(2009). CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|RuleBase:RU003345}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP009484; BAH17097.1; -; Genomic_DNA. DR RefSeq; WP_012656298.1; NC_011999.1. DR AlphaFoldDB; B9EA36; -. DR STRING; 458233.MCCL_0390; -. DR KEGG; mcl:MCCL_0390; -. DR eggNOG; COG1012; Bacteria. DR HOGENOM; CLU_005391_0_2_9; -. DR OrthoDB; 9762913at2; -. DR Proteomes; UP000001383; 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 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 PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1. DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1. DR Pfam; PF00171; Aldedh; 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 Coiled coil {ECO:0000256|SAM:Coils}; NAD {ECO:0000256|ARBA:ARBA00023027}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU003345}; KW Reference proteome {ECO:0000313|Proteomes:UP000001383}. FT DOMAIN 20..479 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT COILED 67..94 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 252 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007" SQ SEQUENCE 492 AA; 53677 MW; 9C9FC507757F88F1 CRC64; MSNLLKEQYG LFINGEFKDS AAGETLDVTN PATGEVLAKI AKATEQDVDA AVKSAEEAFK TWRHTSHNEK AKLLNQIADK MEEHREELAK IESLNSGKAI RESLNIDIPM AIEHFRYFAG VILADEGTNK EIDADAISII KHEPIGVVGA VVAWNFPMLL ASWKLAPALA AGNAVVIQPS SSTPLSLLKF AEIVQDILPK GVLNVVTGKG SESGNAIFNH EDVAKVSFTG STEVGYGVAE AAAKRIVPAT LELGGKSANI IFDDANIEQA IEGAQLGILF NQGEVCSAGS RLYVQEGIYD EFVAKLKDAF EKVRVGDPMD ENNHYGSQTG QAQIDKIEEY IEVAKQEGLN IVTGGKRLMD NGRDKGFFFP PTIIEFEDNK SRLVQEEIFG PVVLVSKFKT KEEVIEKAND SEYGLAGGIF TANLNDALQV ANAMDTGRIW INTYNQIPAG SPFGGYKKSG IGRETYKDTL RHYQQVKNIY IDYSDKAKGI YQ //