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
//