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PORD_METTH
ID   PORD_METTH              Reviewed;          81 AA.
AC   P56815;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Pyruvate synthase subunit PorD;
DE   AltName: Full=Pyruvate oxidoreductase delta chain;
DE            Short=POR;
DE   AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit delta;
GN   Name=porD; OrderedLocusNames=MTH_1740.1;
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 [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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P94692};
CC       Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250|UniProtKB:P94692};
CC   -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC       chain.
CC   -!- CAUTION: There seems to be a sequencing error that fuses together porC
CC       and porD. We have cut the ORF into its two constituents. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB86210.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000666; AAB86210.1; ALT_INIT; Genomic_DNA.
DR   PIR; G69099; G69099.
DR   RefSeq; WP_048061324.1; NC_000916.1.
DR   AlphaFoldDB; P56815; -.
DR   SMR; P56815; -.
DR   EnsemblBacteria; AAB86210; AAB86210; MTH_1740.
DR   GeneID; 62611433; -.
DR   KEGG; mth:MTH_1740; -.
DR   PATRIC; fig|187420.15.peg.1699; -.
DR   HOGENOM; CLU_060916_0_0_2; -.
DR   OMA; GSWRTFK; -.
DR   BioCyc; MetaCyc:MON-14532; -.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IEA:InterPro.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR011898; PorD_KorD.
DR   PANTHER; PTHR43724; PTHR43724; 1.
DR   TIGRFAMs; TIGR02179; PorD_KorD; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Reference proteome; Repeat; Transport.
FT   CHAIN           1..81
FT                   /note="Pyruvate synthase subunit PorD"
FT                   /id="PRO_0000099919"
FT   DOMAIN          25..50
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          51..80
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         34
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         37
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         40
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         44
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         60
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         63
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         66
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         70
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
SQ   SEQUENCE   81 AA;  9121 MW;  219A9CCAE8A41604 CRC64;
     MESLGATVKK PGSTVKNKTG SWRTFKPVLD KDKCIDCDNC ILFCPEGCIN REHEIDYDYC
     KGCGICAEKC PVKAIKMERE K
 
 
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