PORD_THEMA
ID PORD_THEMA Reviewed; 99 AA.
AC Q56316;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 145.
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=TM_0016;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=8550425; DOI=10.1128/jb.178.1.248-257.1996;
RA Kletzin A., Adams M.W.W.;
RT "Molecular and phylogenetic characterization of pyruvate and 2-
RT ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and
RT pyruvate ferredoxin oxidoreductase from Thermotoga maritima.";
RL J. Bacteriol. 178:248-257(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAD35110.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X85171; CAA59456.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35110.1; ALT_INIT; Genomic_DNA.
DR PIR; A59427; B72427.
DR RefSeq; NP_227832.1; NC_000853.1.
DR RefSeq; WP_004082458.1; NZ_CP011107.1.
DR AlphaFoldDB; Q56316; -.
DR SMR; Q56316; -.
DR STRING; 243274.THEMA_04720; -.
DR EnsemblBacteria; AAD35110; AAD35110; TM_0016.
DR KEGG; tma:TM0016; -.
DR PATRIC; fig|243274.5.peg.14; -.
DR eggNOG; COG1144; Bacteria.
DR InParanoid; Q56316; -.
DR OMA; GSWRTFK; -.
DR BioCyc; MetaCyc:MON-426; -.
DR BRENDA; 1.2.7.1; 6331.
DR Proteomes; UP000008183; 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 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8550425"
FT CHAIN 2..99
FT /note="Pyruvate synthase subunit PorD"
FT /id="PRO_0000099924"
FT DOMAIN 32..60
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 61..91
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 41
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="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 47
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 71
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 74
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 77
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
SQ SEQUENCE 99 AA; 11257 MW; C4253752589812F9 CRC64;
MSLKSWKEIP IGGVIDKPGT AREYKTGAWR VMRPILHKEK CIDCMFCWLY CPDQAIIQEG
GIMKGFNYDY CKGCGLCANV CPKQAIEMRP ETEFLSEEG
