ID B9B6P2_9BURK Unreviewed; 508 AA.
AC B9B6P2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 54.
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:EEE00187.1};
GN ORFNames=BURMUCGD1_4757 {ECO:0000313|EMBL:EEE00187.1};
OS Burkholderia multivorans CGD1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=513051 {ECO:0000313|EMBL:EEE00187.1, ECO:0000313|Proteomes:UP000005493};
RN [1] {ECO:0000313|EMBL:EEE00187.1, ECO:0000313|Proteomes:UP000005493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGD1 {ECO:0000313|EMBL:EEE00187.1,
RC ECO:0000313|Proteomes:UP000005493};
RX PubMed=23105085; DOI=10.1128/JB.01306-12;
RA Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., Radune D.,
RA Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., Greenberg D.E.,
RA Holland S.M., Goldberg J.B.;
RT "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic
RT Granulomatous Disease Burkholderia multivorans Isolates.";
RL J. Bacteriol. 194:6356-6357(2012).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEE00187.1}.
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; ACFB01000005; EEE00187.1; -; Genomic_DNA.
DR RefSeq; WP_006399746.1; NZ_ACFB01000005.1.
DR AlphaFoldDB; B9B6P2; -.
DR Proteomes; UP000005493; Unassembled WGS sequence.
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:EEE00187.1}.
FT DOMAIN 23..487
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 508 AA; 53917 MW; A6F232781E348DF3 CRC64;
MNAAVPQTAL ALPTAKLLID GSFVDSRSTE WGDIVNPATQ QVIGRVPYAT LDEIDAAIAA
AQRAFHTWKT TPIGTRVRIM LKFQDLVRRH LERIAQTLTA EQGKTLPDAQ GDIFRGLEVI
EHACSIGTLQ LGEFAENVAG GVDTYTLRQP LGVCAGITPF NFPAMIPLWM FPMAIVCGNT
FVLKPSEQDP LSTMQLVELA LEAGVPPGVL NVVHGGKTAV DRLCTHPDVK AISFVGSTRV
GTHVYQLGSQ HGKRVQSMMG AKNHAVVLPD AHREQTLNAL VGAGFGAAGQ RCMATSVVVL
VGAARDWLPE LVEKAKALKV NAGHEPGTDV GPVVSKAAHA RIAALIDEGV KAGATLELDG
RGVKVPGYEH GNFIGPTIFS GVTTDMSIYT EEIFGPVVVV LEADTLDDAI ALVNRNPMGN
GVGLFTQSGA AARKFQSEID IGQVGINIPI PVPVPYFSFT GSRGSKLGDL GPYGKQVVQF
YTQTKTVTAR WFDDEATAGG VNTTIALR
//
