MMSA_PSEAE
ID MMSA_PSEAE Reviewed; 497 AA.
AC P28810;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Methylmalonate-semialdehyde dehydrogenase [acylating] {ECO:0000303|PubMed:1339433};
DE Short=MMSDH {ECO:0000303|PubMed:1339433};
DE EC=1.2.1.27 {ECO:0000269|PubMed:1339433};
GN Name=mmsA {ECO:0000303|PubMed:1339433}; OrderedLocusNames=PA3570;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-30, CATALYTIC
RP ACTIVITY, PATHWAY, AND INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=1339433; DOI=10.1016/s0021-9258(18)42252-1;
RA Steele M.I., Lorenz D., Hatter K., Park A., Sokatch J.R.;
RT "Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO
RT encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate
RT dehydrogenase.";
RL J. Biol. Chem. 267:13585-13592(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP PROTEIN SEQUENCE OF 186-197 AND 335-351.
RC STRAIN=ATCC 33467 / type 1 smooth;
RA Liddor M.;
RT "Biofouling in water treatment systems: effect of membrane properties on
RT biofilm formation.";
RL Thesis (2005), Ben-Gurion University, Israel.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methyl-3-oxopropanoate + CoA + H2O + NAD(+) = H(+) +
CC hydrogencarbonate + NADH + propanoyl-CoA; Xref=Rhea:RHEA:20804,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57700, ChEBI:CHEBI:57945; EC=1.2.1.27;
CC Evidence={ECO:0000269|PubMed:1339433};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC {ECO:0000269|PubMed:1339433}.
CC -!- SUBUNIT: Homodimer.
CC -!- INDUCTION: By valine. {ECO:0000269|PubMed:1339433}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M84911; AAA25891.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06958.1; -; Genomic_DNA.
DR PIR; B42902; B42902.
DR RefSeq; NP_252260.1; NC_002516.2.
DR RefSeq; WP_003104350.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; P28810; -.
DR SMR; P28810; -.
DR STRING; 287.DR97_4369; -.
DR PaxDb; P28810; -.
DR PRIDE; P28810; -.
DR EnsemblBacteria; AAG06958; AAG06958; PA3570.
DR GeneID; 878814; -.
DR KEGG; pae:PA3570; -.
DR PATRIC; fig|208964.12.peg.3736; -.
DR PseudoCAP; PA3570; -.
DR HOGENOM; CLU_005391_1_10_6; -.
DR InParanoid; P28810; -.
DR OMA; QCEVEGF; -.
DR PhylomeDB; P28810; -.
DR BioCyc; MetaCyc:MON-11663; -.
DR BioCyc; PAER208964:G1FZ6-3638-MON; -.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IBA:GO_Central.
DR GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating) activity; IBA:GO_Central.
DR GO; GO:0006210; P:thymine catabolic process; IBA:GO_Central.
DR GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
DR CDD; cd07085; ALDH_F6_MMSDH; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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 PANTHER; PTHR43866; PTHR43866; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01722; MMSDH; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1339433"
FT CHAIN 2..497
FT /note="Methylmalonate-semialdehyde dehydrogenase
FT [acylating]"
FT /id="PRO_0000056584"
FT ACT_SITE 282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
SQ SEQUENCE 497 AA; 53663 MW; 3DB6BFC300AACA4D CRC64;
MSVPVRHLIA GAFVEGLGAQ RIPVSNPLDN STLAEIACAS AEQVEQAVAS ARETFASWKE
TPVSERARVM LRYQALLKEH HDELAKIVSS ELGKTFEDAK GDVWRGIEVV EHACNVPSLL
MGETVENVAR NIDTYSITQP LGVCVGITPF NFPAMIPLWM FPLAIACGNA FILKPSEQVP
LTSVRLAELF LEAGAPKGVL QVVHGGKEQV DQLLKHPQVK AVSFVGSVAV GQYVYHTGTA
HNKRVQSFAG AKNHMVIMPD ADKAQVISNL VGASVGAAGQ RCMAISVAVL VGAAREWIPE
IRDALAKVRP GPWDDSGASY GPVINPQAKA RIERLIGQGV EEGAQLLLDG RGYKVEGYPD
GNWVGPTLFA GVRPDMAIYR EEVFGPVLCL AEVDSLEQAI RLINESPYGN GTSIFTSSGA
AARTFQHHIE VGQVGINIPI PVPLPFFSFT GWKGSFYGDL HAYGKQGVRF YTETKTVTAR
WFDSDSVAGT NFSIQMR
