ID   ACT_BACMT               Reviewed;         185 AA.
AC   Q8KP10; Q7M0S6;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Methanol dehydrogenase activator {ECO:0000303|PubMed:12089158};
DE            EC=3.-.-.- {ECO:0000305|PubMed:12089158};
DE   AltName: Full=MDH activator {ECO:0000303|PubMed:1995643};
GN   Name=act {ECO:0000303|PubMed:12089158};
OS   Bacillus methanolicus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND SUBSTRATE
RP   SPECIFICITY.
RC   STRAIN=C1;
RX   PubMed=12089158; DOI=10.1074/jbc.m205617200;
RA   Kloosterman H., Vrijbloed J.W., Dijkhuizen L.;
RT   "Molecular, biochemical, and functional characterization of a Nudix
RT   hydrolase protein that stimulates the activity of a nicotinoprotein alcohol
RT   dehydrogenase.";
RL   J. Biol. Chem. 277:34785-34792(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-36, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP   AND COFACTOR.
RC   STRAIN=C1;
RX   PubMed=1995643; DOI=10.1016/s0021-9258(19)67886-5;
RA   Arfman N., Van Beeumen J., De Vries G.E., Harder W., Dijkhuizen L.;
RT   "Purification and characterization of an activator protein for methanol
RT   dehydrogenase from thermotolerant Bacillus spp.";
RL   J. Biol. Chem. 266:3955-3960(1991).
CC   -!- FUNCTION: Involved in the activation of the NAD-dependent methanol
CC       dehydrogenase (MDH). MDH activation by Act involves hydrolytic removal
CC       of the nicotinamide mononucleotide (NMN) moiety of the NAD cofactor,
CC       changing its ping-pong type of reaction mechanism into a ternary
CC       complex reaction mechanism. It requires the presence of magnesium ions
CC       and is also able to use ADP-ribose. {ECO:0000269|PubMed:12089158,
CC       ECO:0000269|PubMed:1995643}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:1995643};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=63 uM for ADP-ribose (at pH 9.5 and 50 degrees Celsius)
CC         {ECO:0000269|PubMed:12089158};
CC         KM=8.28 mM for NAD (at pH 9.5 and 50 degrees Celsius)
CC         {ECO:0000269|PubMed:12089158};
CC         Vmax=10.6 umol/min/mg enzyme with NAD as substrate (at pH 9.5 and 50
CC         degrees Celsius) {ECO:0000269|PubMed:12089158};
CC         Vmax=347.8 umol/min/mg enzyme with ADP-ribose as substrate (at pH 9.5
CC         and 50 degrees Celsius) {ECO:0000269|PubMed:12089158};
CC         Note=kcat is 129 sec(-1) for hydrolase activity with ADP-ribose (at
CC         pH 9.5 and 50 degrees Celsius). kcat is 3.9 sec(-1) for hydrolase
CC         activity with NAD (at pH 9.5 and 50 degrees Celsius).
CC         {ECO:0000269|PubMed:12089158};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12089158,
CC       ECO:0000269|PubMed:1995643}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC       {ECO:0000255|RuleBase:RU003476}.
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DR   EMBL; AY128667; AAM98772.1; -; Genomic_DNA.
DR   PIR; A38659; A38659.
DR   AlphaFoldDB; Q8KP10; -.
DR   SMR; Q8KP10; -.
DR   SABIO-RK; Q8KP10; -.
DR   GO; GO:0016787; F:hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   InterPro; IPR004385; NDP_pyrophosphatase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   TIGRFAMs; TIGR00052; TIGR00052; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1995643"
FT   CHAIN           2..185
FT                   /note="Methanol dehydrogenase activator"
FT                   /id="PRO_0000431552"
FT   CONFLICT        28
FT                   /note="V -> R (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        30
FT                   /note="L -> Y (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36
FT                   /note="S -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   185 AA;  21048 MW;  02CA1C996C72A21C CRC64;
     MGKLFEEKTI KTEQIFSGRV VKLQVDDVEL PNGQTSKREI VRHPGAVAVI AITNENKIVM
     VEQYRKPLEK SIVEIPAGKL EKGEDPRVTA LRELEEETGY ECEQMEWLIS FATSPGFADE
     IIHLYVAKGL SKKENAAGLD EDEFVDLIEL TLDEALQYIK EKRIYDSKTV IAVQYLQLQE
     ALKHK