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Database: UniProt
Entry: K4LIK3_THEPS
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ID   K4LIK3_THEPS            Unreviewed;       578 AA.
AC   K4LIK3;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Formate hydrogenlyase subunit 5 {ECO:0000313|EMBL:AFV12801.1};
GN   Name=hycE {ECO:0000313|EMBL:AFV12801.1};
GN   OrderedLocusNames=Tph_c26330 {ECO:0000313|EMBL:AFV12801.1};
OS   Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermacetogenium.
OX   NCBI_TaxID=1089553 {ECO:0000313|EMBL:AFV12801.1, ECO:0000313|Proteomes:UP000000467};
RN   [1] {ECO:0000313|EMBL:AFV12801.1, ECO:0000313|Proteomes:UP000000467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-254 / DSM 26808 / PB
RC   {ECO:0000313|Proteomes:UP000000467};
RX   PubMed=23259483; DOI=10.1186/1471-2164-13-723;
RA   Oehler D., Poehlein A., Leimbach A., Muller N., Daniel R., Gottschalk G.,
RA   Schink B.;
RT   "Genome-guided analysis of physiological and morphological traits of the
RT   fermentative acetate oxidizer Thermacetogenium phaeum.";
RL   BMC Genomics 13:723-723(2012).
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|PIRSR:PIRSR601501-1};
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DR   EMBL; CP003732; AFV12801.1; -; Genomic_DNA.
DR   RefSeq; WP_015051661.1; NZ_KI912609.1.
DR   AlphaFoldDB; K4LIK3; -.
DR   STRING; 1089553.Tph_c26330; -.
DR   KEGG; tpz:Tph_c26330; -.
DR   eggNOG; COG3261; Bacteria.
DR   eggNOG; COG3262; Bacteria.
DR   HOGENOM; CLU_015134_3_1_9; -.
DR   OrthoDB; 9801496at2; -.
DR   Proteomes; UP000000467; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR   Gene3D; 3.30.460.80; NADH:ubiquinone oxidoreductase, 30kDa subunit; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR   InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR   InterPro; IPR001501; Ni-dep_hyd_lsu.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR43485:SF1; FORMATE HYDROGENLYASE SUBUNIT 5-RELATED; 1.
DR   PANTHER; PTHR43485; HYDROGENASE-4 COMPONENT G; 1.
DR   Pfam; PF00329; Complex1_30kDa; 1.
DR   Pfam; PF00346; Complex1_49kDa; 2.
DR   Pfam; PF00374; NiFeSe_Hases; 1.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR   SUPFAM; SSF143243; Nqo5-like; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Lyase {ECO:0000313|EMBL:AFV12801.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Nickel {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000467}.
FT   DOMAIN          42..161
FT                   /note="NADH:ubiquinone oxidoreductase 30kDa subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00329"
FT   DOMAIN          304..472
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
FT   DOMAIN          473..545
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
FT   BINDING         229
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         249
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         252
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         252
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         539
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         542
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ   SEQUENCE   578 AA;  66091 MW;  7EBDA5391C6DE755 CRC64;
     MNPQTEPVKS NGKKEEVESL RSGFGQAILD ETWQTPDQVT LTVDLDYLPQ VVAAAYYRLG
     GWLSSVIGND ERRLNGAFAL YYVLSMEHER PEENFWLTIK ALVPPEKLEF PSVTPLVPAA
     AWYERDVRDL LGIHPVNHPD PRRLVLPDDW PDGLHPLRKD AMDYRFRPEA ATDEETYEFV
     NVEGEGIMEV PLGPLHVTSD EPGHFRLFVD GETIVDADYR LFYCHRGLEK LAENRMDYDQ
     VHFLAERICG ICGYAHSIAY TTAVERAIGL EVPERARYLR TILLEVERLH SHLLNLGLAC
     HFTGFDSGFM QFFRVREKAM RIAEILSGAR KTYGVNLIGG VRRDILKEER DQVVDLLAEC
     RRETDDLIAI LLNTPNLRKR TVGVGVLDRK VARDFSPVGP NVRGSGFQRD TRSDHPYLAY
     DSIPWEVVTA EGCDVFSRVL VRAKEVYETF NIIQHCLQEL PGGPVLVEGF TYKPHRYALG
     YVEAPRGEDI HWVMTCDNQK LYRWRPRASS YNNWPAIRFM LRGNAISDAP LIIASIDPCY
     SCTERVTVVD IKKKKAKDIS YKELERYCIE KKDSPLKG
//
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