MMSB_MYCTO
ID MMSB_MYCTO Reviewed; 294 AA.
AC P9WNY4; L0T7L8; O53814; P63935;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Probable 3-hydroxyisobutyrate dehydrogenase;
DE Short=HIBADH;
DE EC=1.1.1.31;
GN Name=mmsB; OrderedLocusNames=MT0775;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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 -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. {ECO:0000305}.
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DR EMBL; AE000516; AAK45016.1; -; Genomic_DNA.
DR PIR; B70825; B70825.
DR RefSeq; WP_003403844.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WNY4; -.
DR SMR; P9WNY4; -.
DR EnsemblBacteria; AAK45016; AAK45016; MT0775.
DR GeneID; 45424715; -.
DR KEGG; mtc:MT0775; -.
DR PATRIC; fig|83331.31.peg.833; -.
DR HOGENOM; CLU_035117_6_0_11; -.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000001020; 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: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 3: Inferred from homology;
KW Branched-chain amino acid catabolism; NAD; Oxidoreductase.
FT CHAIN 1..294
FT /note="Probable 3-hydroxyisobutyrate dehydrogenase"
FT /id="PRO_0000427046"
FT ACT_SITE 168
FT /evidence="ECO:0000250"
FT BINDING 3..31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 294 AA; 29679 MW; 68DEF129A8BA3E68 CRC64;
MTTIAFLGLG NMGAPMSANL VGAGHVVRGF DPAPTAASGA AAHGVAVFRS APEAVAEADV
VITMLPTGEV VRRCYTDVLA AARPATLFID SSTISVTDAR EVHALAESHG MLQLDAPVSG
GVKGAAAATL AFMVGGDEST LRRARPVLEP MAGKIIHCGA AGAGQAAKVC NNMVLAVQQI
AIAEAFVLAE KLGLSAQSLF DVITGATGNC WAVHTNCPVP GPVPTSPANN DFKPGFSTAL
MNKDLGLAMD AVAATGATAP LGSHAADIYA KFAADHADLD FSAVIHTLRA RADA