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MCH_METKA
ID   MCH_METKA               Reviewed;         316 AA.
AC   P94954;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   25-MAY-2022, entry version 134.
DE   RecName: Full=Methenyltetrahydromethanopterin cyclohydrolase;
DE            EC=3.5.4.27;
DE   AltName: Full=Methenyl-H4MPT cyclohydrolase;
GN   Name=mch; OrderedLocusNames=MK0625;
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], AND CHARACTERIZATION.
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=9676239; DOI=10.1007/s007920050038;
RA   Vaupel M., Vorholt J.A., Thauer R.K.;
RT   "Overproduction and one-step purification of the N5,N10-
RT   methenyltetrahydromethanopterin cyclohydrolase (Mch) from the
RT   hyperthermophilic Methanopyrus kandleri.";
RL   Extremophiles 2:15-22(1998).
RN   [2]
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   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=10545331; DOI=10.1016/s0969-2126(00)80059-3;
RA   Grabarse W., Vaupel M., Vorholt J.A., Shima S., Thauer R.K.,
RA   Wittershagen A., Bourenkov G., Bartunik H.D., Ermler U.;
RT   "The crystal structure of methenyltetrahydromethanopterin cyclohydrolase
RT   from the hyperthermophilic archaeon Methanopyrus kandleri.";
RL   Structure 7:1257-1268(1999).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of 5-formyl-H(4)MPT
CC       to methenyl-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   -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); 5,10-
CC       methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 3/3.
CC   -!- SUBUNIT: Homotrimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the MCH family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM01840.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA70072.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Y08849; CAA70072.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE009439; AAM01840.1; ALT_INIT; Genomic_DNA.
DR   PIR; T45099; T45099.
DR   PDB; 1QLM; X-ray; 2.00 A; A=1-316.
DR   PDBsum; 1QLM; -.
DR   AlphaFoldDB; P94954; -.
DR   SMR; P94954; -.
DR   STRING; 190192.MK0625; -.
DR   EnsemblBacteria; AAM01840; AAM01840; MK0625.
DR   KEGG; mka:MK0625; -.
DR   PATRIC; fig|190192.8.peg.663; -.
DR   HOGENOM; CLU_876031_0_0_2; -.
DR   OMA; DKGMFAP; -.
DR   UniPathway; UPA00640; UER00694.
DR   EvolutionaryTrace; P94954; -.
DR   Proteomes; UP000001826; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0018759; F:methenyltetrahydromethanopterin cyclohydrolase activity; IEA:UniProtKB-UniRule.
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   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; Hydrolase; Methanogenesis; One-carbon metabolism;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..316
FT                   /note="Methenyltetrahydromethanopterin cyclohydrolase"
FT                   /id="PRO_0000140882"
FT   HELIX           4..17
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           19..22
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   STRAND          25..28
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   STRAND          34..42
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           46..56
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   TURN            57..59
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   STRAND          61..70
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   STRAND          73..84
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           85..89
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   TURN            90..93
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   STRAND          97..101
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   STRAND          104..110
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           113..116
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           120..126
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   STRAND          135..140
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           147..157
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   STRAND          164..169
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           174..181
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           184..194
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           200..202
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   STRAND          203..211
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           219..233
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   STRAND          235..240
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           246..252
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           255..257
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   TURN            259..262
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           265..271
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   TURN            272..274
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           276..278
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           281..283
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   STRAND          287..293
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   TURN            294..296
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   STRAND          299..303
FT                   /evidence="ECO:0007829|PDB:1QLM"
FT   HELIX           307..313
FT                   /evidence="ECO:0007829|PDB:1QLM"
SQ   SEQUENCE   316 AA;  34044 MW;  D6D4097DE6BE0500 CRC64;
     MVSVNENALP LVERMIERAE LLNVEVQELE NGTTVIDCGV EAAGGFEAGL LFSEVCMGGL
     ATVELTEFEH DGLCLPAVQV TTDHPAVSTL AAQKAGWQVQ VGDYFAMGSG PARALALKPK
     ETYEEIDYED DADVAILCLE SSELPDEDVA EHVADECGVD PENLYLLVAP TASIVGSVQV
     SARVVETGLY KLLEVLEYDV TRVKYATGTA PIAPVADDDG EAMGRTNDCI LYGGTVYLYV
     EGDDELPEVV EELPSEASED YGKPFMKIFE EADYDFYKID PGVFAPARVV VNDLSTGKTY
     TAGEINVDVL KESFGL
 
 
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