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
//