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MVHA_METTH
ID   MVHA_METTH              Reviewed;         472 AA.
AC   Q50783; O27206;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=F420-non-reducing hydrogenase subunit A;
DE            EC=1.12.99.-;
DE   AltName: Full=Methyl viologen-reducing hydrogenase subunit alpha;
DE            Short=MVH subunit A;
GN   Name=mvhA; OrderedLocusNames=MTH_1134;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=2654933; DOI=10.1073/pnas.86.9.3031;
RA   Reeve J.N., Beckler G.S., Cram D.S., Hamilton P.T., Brown J.W.,
RA   Krzycki J.A., Kolodziej A.F., Alex L., Orme-Johnson W.H., Walsh C.T.;
RT   "A hydrogenase-linked gene in Methanobacterium thermoautotrophicum strain
RT   delta H encodes a polyferredoxin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:3031-3035(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
CC   -!- FUNCTION: Part of a complex that provides reducing equivalents for
CC       heterodisulfide reductase. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000305};
CC   -!- SUBUNIT: The F420-non-reducing hydrogenase is composed of three
CC       subunits; MvhA, MvhD and MvhG. It forms a complex with the
CC       heterodisulfide reductase (hdr) (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000305}.
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DR   EMBL; J04540; AAB02351.1; -; Genomic_DNA.
DR   EMBL; AE000666; AAB85623.1; -; Genomic_DNA.
DR   PIR; A69018; A69018.
DR   PIR; F30315; F30315.
DR   RefSeq; WP_010876758.1; NC_000916.1.
DR   AlphaFoldDB; Q50783; -.
DR   SMR; Q50783; -.
DR   IntAct; Q50783; 2.
DR   STRING; 187420.MTH_1134; -.
DR   EnsemblBacteria; AAB85623; AAB85623; MTH_1134.
DR   GeneID; 1471542; -.
DR   KEGG; mth:MTH_1134; -.
DR   PATRIC; fig|187420.15.peg.1111; -.
DR   HOGENOM; CLU_044556_0_0_2; -.
DR   OMA; VQNNPAM; -.
DR   BioCyc; MetaCyc:MVHAMAUTO-MON; -.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   Gene3D; 1.10.645.10; -; 1.
DR   InterPro; IPR001501; Ni-dep_hyd_lsu.
DR   InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   Pfam; PF00374; NiFeSe_Hases; 2.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   PROSITE; PS00507; NI_HGENASE_L_1; 1.
DR   PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Nickel; Oxidoreductase; Reference proteome.
FT   CHAIN           1..472
FT                   /note="F420-non-reducing hydrogenase subunit A"
FT                   /id="PRO_0000199726"
FT   BINDING         61
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         64
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         442
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         445
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        21
FT                   /note="H -> R (in Ref. 1; AAB02351)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        267
FT                   /note="K -> T (in Ref. 1; AAB02351)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   472 AA;  52916 MW;  81A50D0D3156CD90 CRC64;
     MVKLTMEPVT RIEGHAKITV HLDDAGNVED TRLHVMEFRG FEKFLQGRPI EEAPRIVPRI
     CGICDVQHHL AAAKAVDACF GFEPEDVLPA AYKMREIMNW GSYMHSHGLH FYFLAAPDFI
     AGKDRKTRNV FQIIKDAPDI ALQAIELRKN ALELVRATGG RPIHPTSSTP GGISTELDDE
     TQKDLLKKAQ RNVELAEATL ELAVPIFEEN IDLVNSLGNI ETYHTGLVKD GVWDVYDGIV
     RIKDKEGNMF REFKPADYAD TIAEHVKPYS WLKFPYIKDL GYPDGVYRVS PLSRLNVADK
     MPDAAPKAQE HFKEFRENFG YAQQTLLYHW ARLIELLACA ECAADALEGD LSGEKFPDSL
     ERQAGDGVGI VEAPRGTLTH HYTCDENGLI TKANIVVATI QNNPAMEMGI QKVAQDYIKP
     GVEVDDKIFN LMEMVIRAYD PCLSCATHTI DSQMRLATLE VYDSEGDLVK RI
 
 
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