ID Q2L0E9_BORA1 Unreviewed; 501 AA.
AC Q2L0E9;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=methylmalonate-semialdehyde dehydrogenase (CoA acylating) {ECO:0000256|ARBA:ARBA00013048};
DE EC=1.2.1.27 {ECO:0000256|ARBA:ARBA00013048};
GN Name=mmsA {ECO:0000313|EMBL:CAJ49526.1};
GN OrderedLocusNames=BAV1917 {ECO:0000313|EMBL:CAJ49526.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ49526.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ49526.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ49526.1,
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; CAJ49526.1; -; Genomic_DNA.
DR RefSeq; WP_012417585.1; NC_010645.1.
DR AlphaFoldDB; Q2L0E9; -.
DR STRING; 360910.BAV1917; -.
DR GeneID; 41393758; -.
DR KEGG; bav:BAV1917; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_10_4; -.
DR OrthoDB; 8639924at2; -.
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:SF4; MALONATE-SEMIALDEHYDE DEHYDROGENASE; 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:CAJ49526.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001977}.
FT DOMAIN 21..482
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 52516 MW; EF4D3513AF04B711 CRC64;
MDAQVTHWIN GRPEVGAEHG HQSIHDPATA EVVAQVDMGG AGAVDRAVAA ACAAQPAWAA
KSPLHRARVL TRFLGLLERN KEELARLITR EHGKVHADAQ GEVMRGIEVV EFACGAPQLL
KGAMSINVGG GIDNWVQREP LGVVAGVTPF NFPVMVPLWM MPVALVTGNA FVLKPSPLDA
SPSLMLAALL REAGLPDGLA SVVQGGEQAV NALLDHPDVK ALSFVGSTAI ARKIYERGAR
AGKRVQALGG AKNHLVIMPD ADPQAAADAV VGAAFGSAGE RCMAASVAVF VGGAGAAVLP
QILSRARALK VARGTQPDAD MGPIVSEAAR DRIAAYIACG MAEGADLLLD GRAIDGRACG
PGCENGYWLG PTVFDSVQPS MRIYREEIFG PVLSCLHVDS LQEAIRLINS HEFANGVSLY
TDSGTAAHTF AQGIEVGMVG VNVPIPVPAS WQGFGGWKQS LFGDLHVYGE EGVRFYTRQK
SVMQRWAAQA AGLSLTMPRS G
//
