ID   VHUU_METMP              Reviewed;          44 AA.
AC   P0C1V5;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=F420-non-reducing hydrogenase vhu subunit U;
DE            EC=1.12.99.-;
DE   Flags: Precursor;
GN   Name=vhuU; OrderedLocusNames=MMP1693;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000305};
CC   -!- SUBUNIT: The F420-non-reducing hydrogenase vhu is composed of four
CC       subunits; VhuA, VhuD, VhuG and VhuU. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The large subunit of Vhu is split into VhuA and VhuU.
CC       Each contributes two ligands to the [NiFeSe] center.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000305}.
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DR   EMBL; BX950229; CAF31249.1; -; Genomic_DNA.
DR   STRING; 267377.MMP1693; -.
DR   KEGG; mmp:MMP1693; -.
DR   eggNOG; arCOG06685; Archaea.
DR   HOGENOM; CLU_3113140_0_0_2; -.
DR   BioCyc; MMAR267377:MMP_RS08925-MON; -.
DR   Proteomes; UP000000590; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.645.10; -; 1.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   SUPFAM; SSF56762; SSF56762; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Nickel; Oxidoreductase; Reference proteome; Selenocysteine.
FT   CHAIN           1..25
FT                   /note="F420-non-reducing hydrogenase vhu subunit U"
FT                   /id="PRO_0000249592"
FT   PROPEP          26..44
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000249593"
FT   BINDING         20
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         23
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   NON_STD         20
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   44 AA;  5083 MW;  DC05EDF4147317EE CRC64;
     MVDEAKLNLI EIVLRAYDPU YSCAAHMIVK DEQGKVLLEV KKEE