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Database: UniProt
Entry: Q8TRN3_METAC
LinkDB: Q8TRN3_METAC
Original site: Q8TRN3_METAC 
ID   Q8TRN3_METAC            Unreviewed;       595 AA.
AC   Q8TRN3;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   SubName: Full=F420-nonreducing hydrogenase {ECO:0000313|EMBL:AAM04563.1};
GN   Name=vhtA {ECO:0000313|EMBL:AAM04563.1};
GN   OrderedLocusNames=MA_1142 {ECO:0000313|EMBL:AAM04563.1};
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937 {ECO:0000313|EMBL:AAM04563.1, ECO:0000313|Proteomes:UP000002487};
RN   [1] {ECO:0000313|EMBL:AAM04563.1, ECO:0000313|Proteomes:UP000002487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC   {ECO:0000313|Proteomes:UP000002487};
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A., Hedderich R., Ingram-Smith C.,
RA   Kuettner C.H., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B.,
RA   Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H.,
RA   de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L.,
RA   Paulsen I., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H.,
RA   Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601501-1};
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000256|ARBA:ARBA00001967,
CC         ECO:0000256|PIRSR:PIRSR601501-1};
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000256|ARBA:ARBA00009292, ECO:0000256|RuleBase:RU003896}.
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DR   EMBL; AE010299; AAM04563.1; -; Genomic_DNA.
DR   RefSeq; WP_011021166.1; NC_003552.1.
DR   AlphaFoldDB; Q8TRN3; -.
DR   STRING; 188937.MA_1142; -.
DR   EnsemblBacteria; AAM04563; AAM04563; MA_1142.
DR   GeneID; 1473030; -.
DR   KEGG; mac:MA_1142; -.
DR   HOGENOM; CLU_030087_0_0_2; -.
DR   InParanoid; Q8TRN3; -.
DR   OrthoDB; 42371at2157; -.
DR   PhylomeDB; Q8TRN3; -.
DR   Proteomes; UP000002487; 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; Cytochrome-c3 Hydrogenase, chain B; 1.
DR   InterPro; IPR001501; Ni-dep_hyd_lsu.
DR   InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR42958:SF4; HYDROGENASE EXPRESSION_FORMATION PROTEIN HUPK; 1.
DR   PANTHER; PTHR42958; HYDROGENASE-2 LARGE CHAIN; 1.
DR   Pfam; PF00374; NiFeSe_Hases; 2.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR   PROSITE; PS00507; NI_HGENASE_L_1; 1.
DR   PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601501-1};
KW   Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|PIRSR:PIRSR601501-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003896};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002487}.
FT   BINDING         42
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         61
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         64
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         64
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         573
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         576
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         579
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ   SEQUENCE   595 AA;  64656 MW;  0300BBDF975FFD64 CRC64;
     MVNVTVDPLT RIEGHLRLST EVDANGVITD SQSSCLMFRG FERILQNQDP RDAALLVQRI
     CGVCPTSHSL TAANALDDLF GVADTIPKDA LVARNINQAL NFLASHATHI YILWGPDLAN
     PAYRDVLTPL GETGTAVWKE MVGRFAPISY KIDGESVPVG SSYLAAIPEK KRLQEAIAVI
     GGKMPHQVTS YPGGYTYKPN VADIGKLSSY YLQVMDFVSS YTLRVPFDTW IENTYKASSP
     QKAVNFVVEH LTDLVDKSVT SNDFSREAGW GDTEFYAAFG SELVGETLLG LPASLKHDKI
     GGYSDPSKIA FLAYGGFFNP ENGDGYDPSS PAGERFLTSG IVTGSLEYQN LDTSKITESV
     AHAFYEDTAD LHPSKGETNP FTDPDAIRFD QGSDSRYSWN KAPRYDGIPC EVGPLARMLA
     AKEPLVTGLA LAFNENGYSA ANVYTRMMAR IQETAIIANE LLKWVTEDYD PNGRIAVDTD
     LSMAKDSTGM GLWEAPRGAL GHWVSTDSNS KVVNYQPVVP STWNLSPRDS AGVPGPLEQS
     LIGAKINAAE NSLGVNYTNP VNILHIGRSY DPCVSCAVHT IDLTGKNTPR TLRIV
//
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