MMSB_PSEAE
ID MMSB_PSEAE Reviewed; 298 AA.
AC P28811;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=3-hydroxyisobutyrate dehydrogenase {ECO:0000303|PubMed:1339433};
DE Short=HIBADH {ECO:0000305};
DE EC=1.1.1.31 {ECO:0000269|PubMed:1339433};
GN Name=mmsB {ECO:0000303|PubMed:1339433}; OrderedLocusNames=PA3569;
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], CATALYTIC ACTIVITY, PATHWAY, AND
RP 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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-
CC oxopropanoate + H(+) + NADH; Xref=Rhea:RHEA:17681, ChEBI:CHEBI:11805,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57700,
CC ChEBI:CHEBI:57945; EC=1.1.1.31;
CC Evidence={ECO:0000269|PubMed:1339433};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC {ECO:0000269|PubMed:1339433}.
CC -!- INDUCTION: By valine. {ECO:0000269|PubMed:1339433}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. {ECO:0000305}.
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DR EMBL; M84911; AAA25892.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06957.1; -; Genomic_DNA.
DR PIR; C42902; C42902.
DR RefSeq; NP_252259.1; NC_002516.2.
DR RefSeq; WP_003113890.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; P28811; -.
DR SMR; P28811; -.
DR STRING; 287.DR97_4370; -.
DR PaxDb; P28811; -.
DR PRIDE; P28811; -.
DR DNASU; 879097; -.
DR EnsemblBacteria; AAG06957; AAG06957; PA3569.
DR GeneID; 879097; -.
DR KEGG; pae:PA3569; -.
DR PATRIC; fig|208964.12.peg.3735; -.
DR PseudoCAP; PA3569; -.
DR HOGENOM; CLU_035117_6_0_6; -.
DR InParanoid; P28811; -.
DR OMA; WSSEVNN; -.
DR PhylomeDB; P28811; -.
DR BioCyc; PAER208964:G1FZ6-3637-MON; -.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0006574; P:valine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR011548; HIBADH.
DR InterPro; IPR015815; HIBADH-related.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029154; NADP-bd.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000103; HIBADH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01692; HIBADH; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 1: Evidence at protein level;
KW Branched-chain amino acid catabolism; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..298
FT /note="3-hydroxyisobutyrate dehydrogenase"
FT /id="PRO_0000173058"
FT ACT_SITE 171
FT /evidence="ECO:0000250"
FT BINDING 2..30
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P31937"
FT BINDING 65..66
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P31937"
FT BINDING 96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P31937"
FT BINDING 246
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P31937"
SQ SEQUENCE 298 AA; 30486 MW; 0C4D7B5A7C870730 CRC64;
MTDIAFLGLG NMGGPMAANL LKAGHRVNVF DLQPKAVLGL VEQGAQGADS ALQCCEGAEV
VISMLPAGQH VESLYLGDDG LLARVAGKPL LIDCSTIAPE TARKVAEAAA AKGLTLLDAP
VSGGVGGARA GTLSFIVGGP AEGFARARPV LENMGRNIFH AGDHGAGQVA KICNNMLLGI
LMAGTAEALA LGVKNGLDPA VLSEVMKQSS GGNWALNLYN PWPGVMPQAP ASNGYAGGFQ
VRLMNKDLGL ALANAQAVQA STPLGALARN LFSLHAQADA EHEGLDFSSI QKLYRGKD
