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Database: UniProt
Entry: A2SMC7_METPP
LinkDB: A2SMC7_METPP
Original site: A2SMC7_METPP 
ID   A2SMC7_METPP            Unreviewed;       297 AA.
AC   A2SMC7;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=2-hydroxy-3-oxopropionate reductase {ECO:0000313|EMBL:ABM96716.1};
DE            EC=1.1.1.31 {ECO:0000313|EMBL:ABM96716.1};
GN   OrderedLocusNames=Mpe_A3763 {ECO:0000313|EMBL:ABM96716.1};
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Methylibium.
OX   NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM96716.1, ECO:0000313|Proteomes:UP000000366};
RN   [1] {ECO:0000313|EMBL:ABM96716.1, ECO:0000313|Proteomes:UP000000366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC   {ECO:0000313|Proteomes:UP000000366};
RX   PubMed=17158667; DOI=10.1128/JB.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
CC   -!- SIMILARITY: Belongs to the HIBADH-related family.
CC       {ECO:0000256|ARBA:ARBA00009080}.
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DR   EMBL; CP000555; ABM96716.1; -; Genomic_DNA.
DR   RefSeq; WP_011831336.1; NC_008825.1.
DR   AlphaFoldDB; A2SMC7; -.
DR   STRING; 420662.Mpe_A3763; -.
DR   KEGG; mpt:Mpe_A3763; -.
DR   eggNOG; COG2084; Bacteria.
DR   HOGENOM; CLU_035117_1_0_4; -.
DR   Proteomes; UP000000366; 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:0016054; P:organic acid catabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR029154; HIBADH-like_NADP-bd.
DR   InterPro; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43060:SF15; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000103; HIBADH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000313|EMBL:ABM96716.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000366}.
FT   DOMAIN          13..171
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          176..294
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ   SEQUENCE   297 AA;  30623 MW;  D6BB3AA7D39CB130 CRC64;
     MTSKTYDPVP SQRVAFLGLG VMGHPMAGHL ARAGHSVCVY NRTAAKAQAW VNEYGGRSAP
     TPCAAAQDAD IVFACVGNDA DLRSVTTGAD GAFQAMKAGA VFVDHTTASA DIARELAAAA
     RARGLGFVDA PVSGGNLGAI NGALTVMCGG DAADFAKIQP VAMAFSKAVT LLGEAGAGQL
     AKMVNQIAIA GLVQGLSEAI AFGQKAGLDM KAVLGVIGKG AAQSWQMDNR GPTMVDGKFD
     FGFAVDWMRK DLGLCLDEAK RNGARLPVTA LVDQFYADVQ ADDGGRRDTS SLIQRLK
//
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