ID   VHUU_METVO              Reviewed;          44 AA.
AC   Q00410; P95319; Q7M534;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 6.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=F420-non-reducing hydrogenase vhu subunit U;
DE            EC=1.12.99.-;
DE   Flags: Precursor;
GN   Name=vhuU;
OS   Methanococcus voltae.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=2188;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RX   PubMed=1603063; DOI=10.1007/bf00587582;
RA   Halboth S., Klein A.;
RT   "Methanococcus voltae harbors four gene clusters potentially encoding two
RT   [NiFe] and two [NiFeSe] hydrogenases, each of the cofactor F420-reducing or
RT   F420-non-reducing types.";
RL   Mol. Gen. Genet. 233:217-224(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-26, AND PROTEOLYTIC PROCESSING.
RX   PubMed=8504827; DOI=10.1111/j.1432-1033.1993.tb17888.x;
RA   Sorgenfrei O., Linder D., Karas M., Klein A.;
RT   "A novel very small subunit of a selenium containing [NiFe] hydrogenase of
RT   Methanococcus voltae is postranslationally processed by cleavage at a
RT   defined position.";
RL   Eur. J. Biochem. 213:1355-1358(1993).
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   -!- MISCELLANEOUS: The peptide is so short that about 65% of the chains are
CC       released from the ribosome before the initiator Met can be removed.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000305}.
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DR   EMBL; X61204; CAA43511.1; -; Genomic_DNA.
DR   PIR; S32463; S32463.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Metal-binding; Nickel; Oxidoreductase;
KW   Selenocysteine.
FT   INIT_MET        1
FT                   /note="Removed; partial"
FT   CHAIN           2..26
FT                   /note="F420-non-reducing hydrogenase vhu subunit U"
FT                   /id="PRO_0000013411"
FT   PROPEP          27..44
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000013412"
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;  5020 MW;  AE001A84B7F714B0 CRC64;
     MVDETKLNLI EIVLRAYDPU YSCAAHMIVE DAEGNVVFEI VNDE