MCH_ARCFU
ID MCH_ARCFU Reviewed; 316 AA.
AC O28344;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Methenyltetrahydromethanopterin cyclohydrolase;
DE EC=3.5.4.27;
DE AltName: Full=Methenyl-H4MPT cyclohydrolase;
GN Name=mch; OrderedLocusNames=AF_1935;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP PROTEIN SEQUENCE OF 1-40, AND CHARACTERIZATION.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=8481088; DOI=10.1007/bf00248474;
RA Klein A.R., Breitung J., Linder D., Stetter K.O., Thauer R.K.;
RT "N5,N10-methenyltetrahydromethanopterin cyclohydrolase from the extremely
RT thermophilic sulfate reducing Archaeoglobus fulgidus: comparison of its
RT properties with those of the cyclohydrolase from the extremely thermophilic
RT Methanopyrus kandleri.";
RL Arch. Microbiol. 159:213-219(1993).
CC -!- FUNCTION: Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-
CC H(4)MPT.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) +
CC N(5)-formyl-5,6,7,8-tetrahydromethanopterin; Xref=Rhea:RHEA:19053,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58018,
CC ChEBI:CHEBI:58337; EC=3.5.4.27;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius. Requires a high salt
CC concentration for optimal thermostability at 90 degrees Celsius.;
CC -!- PATHWAY: Metabolic intermediate metabolism; lactate oxidation.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the MCH family. {ECO:0000305}.
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DR EMBL; AE000782; AAB89320.1; -; Genomic_DNA.
DR PIR; F69491; F69491.
DR RefSeq; WP_010879428.1; NC_000917.1.
DR PDB; 4GVQ; X-ray; 1.30 A; A/B/C=1-316.
DR PDB; 4GVR; X-ray; 1.52 A; A/B/C=1-316.
DR PDB; 4GVS; X-ray; 1.75 A; A/B/C=1-316.
DR PDBsum; 4GVQ; -.
DR PDBsum; 4GVR; -.
DR PDBsum; 4GVS; -.
DR AlphaFoldDB; O28344; -.
DR SMR; O28344; -.
DR STRING; 224325.AF_1935; -.
DR EnsemblBacteria; AAB89320; AAB89320; AF_1935.
DR GeneID; 24795679; -.
DR KEGG; afu:AF_1935; -.
DR eggNOG; arCOG02675; Archaea.
DR HOGENOM; CLU_876031_0_0_2; -.
DR OMA; DKGMFAP; -.
DR OrthoDB; 31274at2157; -.
DR PhylomeDB; O28344; -.
DR BioCyc; MetaCyc:AF_RS09720-MON; -.
DR BRENDA; 3.5.4.27; 414.
DR UniPathway; UPA00701; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0018759; F:methenyltetrahydromethanopterin cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019516; P:lactate oxidation; IEA:UniProtKB-UniPathway.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00545; MCH; 1.
DR HAMAP; MF_00486; McH; 1.
DR InterPro; IPR003209; METHMP_CycHdrlase.
DR Pfam; PF02289; MCH; 1.
DR TIGRFAMs; TIGR03120; one_C_mch; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase;
KW One-carbon metabolism; Reference proteome.
FT CHAIN 1..316
FT /note="Methenyltetrahydromethanopterin cyclohydrolase"
FT /id="PRO_0000140877"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:4GVQ"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:4GVQ"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:4GVQ"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:4GVQ"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:4GVQ"
FT STRAND 73..83
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:4GVQ"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:4GVQ"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:4GVQ"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:4GVQ"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:4GVQ"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:4GVQ"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 174..181
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:4GVQ"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 218..232
FT /evidence="ECO:0007829|PDB:4GVQ"
FT STRAND 234..241
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 244..248
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:4GVQ"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:4GVQ"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:4GVQ"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:4GVQ"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:4GVQ"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:4GVQ"
FT HELIX 303..309
FT /evidence="ECO:0007829|PDB:4GVQ"
SQ SEQUENCE 316 AA; 34852 MW; E4B6F6BFB6C91CF9 CRC64;
MLSVNEIAAE IVEDMLDYEE ELRIESKKLE NGAIVVDCGV NVPGSYDAGI MYTQVCMGGL
ADVDIVVDTI NDVPFAFVTE YTDHPAIACL GSQKAGWQIK VDKYFAMGSG PARALALKPK
KTYERIEYED DADVAVIALE ANQLPDEKVM EFIAKECDVD PENVYALVAP TASIVGSVQI
SGRIVETAIF KMNEIGYDPK LIVSGAGRCP ISPILENDLK AMGSTNDSMM YYGSVFLTVK
KYDEILKNVP SCTSRDYGKP FYEIFKAANY DFYKIDPNLF APAQIAVNDL ETGKTYVHGK
LNAEVLFQSY QIVLEE
