HMD_METKA
ID HMD_METKA Reviewed; 358 AA.
AC Q02394;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=5,10-methenyltetrahydromethanopterin hydrogenase;
DE EC=1.12.98.2 {ECO:0000269|PubMed:1772345};
DE AltName: Full=H(2)-dependent methylene-H(4)MPT dehydrogenase;
DE AltName: Full=H(2)-forming N(5),N(10)-methylenetetrahydromethanopterin dehydrogenase;
DE AltName: Full=N(5),N(10)-methenyltetrahydromethanopterin dehydrogenase {ECO:0000303|PubMed:1772345};
GN Name=hmd {ECO:0000303|PubMed:1521540}; OrderedLocusNames=MK0013;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1521540; DOI=10.1111/j.1432-1033.1992.tb17215.x;
RA Zirngibl C., van Dongen W., Schwoerer B., von Buenau R., Richter M.,
RA Klein A., Thauer R.K.;
RT "H2-forming methylenetetrahydromethanopterin dehydrogenase, a novel type of
RT hydrogenase without iron-sulfur clusters in methanogenic archaea.";
RL Eur. J. Biochem. 208:511-520(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9151968; DOI=10.1111/j.1432-1033.1997.t01-1-00386.x;
RA Klein A.R., Thauer R.K.;
RT "Overexpression of the coenzyme-F420-dependent N5,N10-
RT methylenetetrahydromethanopterin dehydrogenase gene from the
RT hyperthermophilic Methanopyrus kandleri.";
RL Eur. J. Biochem. 245:386-391(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
RN [4]
RP PROTEIN SEQUENCE OF 2-24, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND PATHWAY.
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=1772345; DOI=10.1007/bf00418186;
RA Ma K., Zirngibl C., Linder D., Stetter K.O., Thauer R.K.;
RT "N5, N10-methylenetetrahydromethanopterin dehydrogenase (H2-forming) from
RT the extreme thermophile Methanopyrus kandleri.";
RL Arch. Microbiol. 156:43-48(1991).
CC -!- FUNCTION: Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to
CC methylene-H(4)MPT. {ECO:0000269|PubMed:1772345}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2 = 5,10-
CC methylenetetrahydromethanopterin + H(+); Xref=Rhea:RHEA:20017,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:57818,
CC ChEBI:CHEBI:58337; EC=1.12.98.2;
CC Evidence={ECO:0000269|PubMed:1772345};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20018;
CC Evidence={ECO:0000269|PubMed:1772345};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20019;
CC Evidence={ECO:0000269|PubMed:1772345};
CC -!- ACTIVITY REGULATION: Activity requires salt; 100 mM potassium
CC phosphate, potassium chloride, and sodium chloride are equally
CC effective. {ECO:0000269|PubMed:1772345}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 uM for H(+) {ECO:0000269|PubMed:1772345};
CC KM=50 uM for 5,10-methylenetetrahydromethanopterin
CC {ECO:0000269|PubMed:1772345};
CC Temperature dependence:
CC Thermolabile at 90 degrees Celsius. {ECO:0000269|PubMed:1772345};
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); 5,10-
CC methylene-5,6,7,8-tetrahydromethanopterin from 5,10-methenyl-5,6,7,8-
CC tetrahydromethanopterin (hydrogen route): step 1/1.
CC {ECO:0000269|PubMed:1772345}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:1772345}.
CC -!- SIMILARITY: Belongs to the HMD family. {ECO:0000305}.
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DR EMBL; X60719; CAA43127.1; -; Genomic_DNA.
DR EMBL; Y10251; CAA71299.1; -; Genomic_DNA.
DR EMBL; AE009439; AAM01230.1; -; Genomic_DNA.
DR PIR; S30603; S30603.
DR AlphaFoldDB; Q02394; -.
DR SMR; Q02394; -.
DR STRING; 190192.MK0013; -.
DR EnsemblBacteria; AAM01230; AAM01230; MK0013.
DR KEGG; mka:MK0013; -.
DR PATRIC; fig|190192.8.peg.12; -.
DR HOGENOM; CLU_772960_0_0_2; -.
DR OMA; HACTIPT; -.
DR BRENDA; 1.12.98.2; 3274.
DR UniPathway; UPA00640; UER00696.
DR Proteomes; UP000001826; Chromosome.
DR GO; GO:0047068; F:N5,N10-methenyltetrahydromethanopterin hydrogenase activity; IDA:MENGO.
DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.1300; -; 1.
DR HAMAP; MF_01090; HMD; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR010062; HMD.
DR InterPro; IPR004889; HMD_C.
DR InterPro; IPR038182; HMD_C_sf.
DR InterPro; IPR024190; METHMP_Hmd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF03201; HMD; 1.
DR PIRSF; PIRSF016158; HMD; 1.
DR PIRSF; PIRSF500165; HMDI; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01723; hmd_TIGR; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Methanogenesis; One-carbon metabolism;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1772345"
FT CHAIN 2..358
FT /note="5,10-methenyltetrahydromethanopterin hydrogenase"
FT /id="PRO_0000218509"
SQ SEQUENCE 358 AA; 39038 MW; 9B8491B2A5A20771 CRC64;
MVEINKVAIL GAGCWRTHAA TGITTFKRAC EVADETGIKE AALTHSSVTY AVELKHLAGV
DEVVLSDPVF DADGFTVVDI EEDCDVDLDE FIKAHLEGNP EDVMPKLRDY VNDIADDVPK
PPKGAIHFLS PEEMEDKLDI VVTTDDAEAV EDADMIISWL PKGGVQPDIF KKIIDDIPEG
CIVANTCTIP TRQFKEMFED MGRDDLQVTS YHPATVPEHK GQVFVAEGYA DEEVVEAVYE
LGEKARGLAF KVPGYLLGPV CDMASAVTAI VYAGLLTFRD ACTDILGAPV DFTQNMAVEA
LQMMAKFMEE EGLDKLEEAL DPAALTNTAD SMNFGPLADT EILPKALEVL EKYSKKAE
