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Database: UniProt
Entry: Q2KY44_BORA1
LinkDB: Q2KY44_BORA1
Original site: Q2KY44_BORA1 
ID   Q2KY44_BORA1            Unreviewed;       497 AA.
AC   Q2KY44;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 93.
DE   RecName: Full=methylmalonate-semialdehyde dehydrogenase (CoA acylating) {ECO:0000256|ARBA:ARBA00013048};
DE            EC=1.2.1.27 {ECO:0000256|ARBA:ARBA00013048};
GN   OrderedLocusNames=BAV1141 {ECO:0000313|EMBL:CAJ48750.1};
OS   Bordetella avium (strain 197N).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ48750.1, ECO:0000313|Proteomes:UP000001977};
RN   [1] {ECO:0000313|EMBL:CAJ48750.1, ECO:0000313|Proteomes:UP000001977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N {ECO:0000313|EMBL:CAJ48750.1,
RC   ECO:0000313|Proteomes:UP000001977};
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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DR   EMBL; AM167904; CAJ48750.1; -; Genomic_DNA.
DR   RefSeq; WP_012416824.1; NC_010645.1.
DR   AlphaFoldDB; Q2KY44; -.
DR   STRING; 360910.BAV1141; -.
DR   GeneID; 41393045; -.
DR   KEGG; bav:BAV1141; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_10_4; -.
DR   OMA; QCEVEGF; -.
DR   OrthoDB; 6187633at2; -.
DR   Proteomes; UP000001977; Chromosome.
DR   GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity; IEA:UniProtKB-EC.
DR   CDD; cd07085; ALDH_F6_MMSDH; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
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:SF3; METHYLMALONATE-SEMIALDEHYDE DEHYDROGENASE [ACYLATING], MITOCHONDRIAL; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CAJ48750.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001977}.
FT   DOMAIN          18..479
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   497 AA;  53305 MW;  4EB0A54C95DAFCBF CRC64;
     MSEVPRVPLL IGGKLVQSKT THWRDVINPA NQEVVAQVPF ATREELDLAV ADAKQAFQTW
     RNAGQGQRMR VMLRFQQLLR ENSGKLAEMI TREHGKTLPD AEGEVGRGLE VVEHACSIAS
     LQLGEYAENA ASGIDVYTLI QPLGVCAGIT AFNFPVMLPC FMFPIAVSCG NTFVLKPSEQ
     DPTASLYLAQ LALEAGLPPG VLNVVHGGPD IANGLCEHPD IKAVSFIGST RVGTEIYDRA
     SKAGKRCQSM MGAKNHCVVL PDADPEVALN QLVGAAFGAA GQRCMATSVA VLVGEARNWL
     PDFVERSRKL KVNVGTDREA DLGPLVSINA RKRVESLIQQ GVDEGAKLLL DGRGVKVEGY
     AAGNFVGPTI FDGVTEAMSI YQEEIFGPVL CVVGVETLEE AVAFINRNPN GNGVALFTQD
     GGAARYFQNH IDVGQVGINI PIPVPVAWFS FTGSRGSKLG DLGPNGKQAV QFWTQTKTVT
     ARWSAHGRSV NTTITMR
//
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