PORD_METTM
ID PORD_METTM Reviewed; 81 AA.
AC P80903; D9PUM3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 89.
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=MTBMA_c03150;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
RN [2]
RP PROTEIN SEQUENCE OF 1-12, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=9108258; DOI=10.1111/j.1432-1033.1997.00862.x;
RA Tersteegen A., Linder D., Thauer R.K., Hedderich R.;
RT "Structures and functions of four anabolic 2-oxoacid oxidoreductases in
RT Methanobacterium thermoautotrophicum.";
RL Eur. J. Biochem. 244:862-868(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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 10.0. {ECO:0000269|PubMed:9108258};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius.
CC {ECO:0000269|PubMed:9108258};
CC -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC chain. {ECO:0000269|PubMed:9108258}.
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DR EMBL; CP001710; ADL57921.1; -; Genomic_DNA.
DR RefSeq; WP_013295148.1; NC_014408.1.
DR AlphaFoldDB; P80903; -.
DR SMR; P80903; -.
DR STRING; 79929.MTBMA_c03150; -.
DR EnsemblBacteria; ADL57921; ADL57921; MTBMA_c03150.
DR GeneID; 9704021; -.
DR KEGG; mmg:MTBMA_c03150; -.
DR PATRIC; fig|79929.8.peg.309; -.
DR HOGENOM; CLU_139698_1_1_2; -.
DR OMA; GSWRTFK; -.
DR OrthoDB; 125632at2157; -.
DR Proteomes; UP000000345; 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 Pfam; PF00037; Fer4; 2.
DR TIGRFAMs; TIGR02179; PorD_KorD; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Repeat; Transport.
FT CHAIN 1..81
FT /note="Pyruvate synthase subunit PorD"
FT /id="PRO_0000099920"
FT DOMAIN 25..54
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 REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 9201 MW; 90EC77B79308A5E1 CRC64;
MESLGATVKE PGSTRKNKTG SWRTFKPFLD KDKCIDCDNC ILFCPEGCID KEHEIDYDYC
KGCGICAEEC PVKAIKMERE K
