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Database: UniProt
Entry: Q2RMD6_MOOTA
LinkDB: Q2RMD6_MOOTA
Original site: Q2RMD6_MOOTA 
ID   Q2RMD6_MOOTA            Unreviewed;      1171 AA.
AC   Q2RMD6;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   12-SEP-2018, entry version 98.
DE   RecName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000256|PIRNR:PIRNR000159};
DE            EC=1.2.7.- {ECO:0000256|PIRNR:PIRNR000159};
GN   OrderedLocusNames=Moth_0064 {ECO:0000313|EMBL:ABC18403.1};
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC18403.1, ECO:0000313|Proteomes:UP000007053};
RN   [1] {ECO:0000313|Proteomes:UP000007053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320 {ECO:0000313|Proteomes:UP000007053};
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f.
RT   Clostridium thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
RN   [2] {ECO:0000213|PDB:6CIN, ECO:0000213|PDB:6CIO, ECO:0000213|PDB:6CIP}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).
RX   PubMed=29581263; DOI=10.1073/pnas.1722329115;
RA   Chen P.Y.-T., Aman H., Can M., Ragsdale S.W., Drennan C.L.;
RT   "Binding site for coenzyme A revealed in the structure of
RT   pyruvate:ferredoxin oxidoreductase from Moorella thermoacetica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:3846-3851(2018).
CC   -!- FUNCTION: Oxidoreductase required for the transfer of electrons
CC       from pyruvate to flavodoxin. {ECO:0000256|PIRNR:PIRNR000159}.
CC   -!- CATALYTIC ACTIVITY: Pyruvate + CoA + oxidized flavodoxin = acetyl-
CC       CoA + CO(2) + reduced flavodoxin. {ECO:0000256|PIRNR:PIRNR000159}.
CC   -!- SIMILARITY: Belongs to the nifJ family.
CC       {ECO:0000256|PIRNR:PIRNR000159}.
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DR   EMBL; CP000232; ABC18403.1; -; Genomic_DNA.
DR   RefSeq; WP_011391612.1; NC_007644.1.
DR   RefSeq; YP_428946.1; NC_007644.1.
DR   PDB; 6CIN; X-ray; 2.60 A; A/B/C/D/E/F=1-1171.
DR   PDB; 6CIO; X-ray; 3.00 A; A/B/C/D/E/F=1-1171.
DR   PDB; 6CIP; X-ray; 3.19 A; A/B/C/D/E/F=1-1171.
DR   PDB; 6CIQ; X-ray; 3.30 A; A/B/C=1-1171.
DR   PDBsum; 6CIN; -.
DR   PDBsum; 6CIO; -.
DR   PDBsum; 6CIP; -.
DR   PDBsum; 6CIQ; -.
DR   ProteinModelPortal; Q2RMD6; -.
DR   STRING; 264732.Moth_0064; -.
DR   EnsemblBacteria; ABC18403; ABC18403; Moth_0064.
DR   GeneID; 3830814; -.
DR   KEGG; mta:Moth_0064; -.
DR   PATRIC; fig|264732.11.peg.68; -.
DR   eggNOG; ENOG4105D95; Bacteria.
DR   eggNOG; COG0674; LUCA.
DR   eggNOG; COG1013; LUCA.
DR   eggNOG; COG1014; LUCA.
DR   HOGENOM; HOG000266425; -.
DR   KO; K03737; -.
DR   OMA; NTVMQVC; -.
DR   OrthoDB; POG091H02IV; -.
DR   BioCyc; MTHE264732:G1G5J-72-MONOMER; -.
DR   Proteomes; UP000007053; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.920.10; -; 1.
DR   Gene3D; 4.10.780.10; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR037112; Pyrv-flavodox_OxR_EKR_sf.
DR   InterPro; IPR019456; Pyrv-flavodox_OxRtase_EKR.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR011895; Pyrv_flavodox_OxRed.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   Pfam; PF10371; EKR; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01558; POR; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   PIRSF; PIRSF000159; NifJ; 1.
DR   SMART; SM00890; EKR; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   SUPFAM; SSF53323; SSF53323; 1.
DR   TIGRFAMs; TIGR02176; pyruv_ox_red; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0000213|PDB:6CIN, ECO:0000213|PDB:6CIO,
KW   ECO:0000213|PDB:6CIP, ECO:0000213|PDB:6CIQ};
KW   4Fe-4S {ECO:0000256|PIRSR:PIRSR000159-50};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007053};
KW   Electron transport {ECO:0000256|PIRNR:PIRNR000159};
KW   Iron {ECO:0000256|PIRSR:PIRSR000159-50};
KW   Iron-sulfur {ECO:0000256|PIRSR:PIRSR000159-50};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000159-50};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000159};
KW   Pyruvate {ECO:0000313|EMBL:ABC18403.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007053};
KW   Transport {ECO:0000256|PIRNR:PIRNR000159}.
FT   DOMAIN      677    706       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   DOMAIN      733    764       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   REGION      966    969       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   REGION      995   1000       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   METAL       686    686       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       689    689       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       692    692       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       696    696       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       742    742       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       745    745       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       748    748       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       752    752       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       809    809       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       812    812       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       837    837       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL      1075   1075       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   BINDING      29     29       Pyruvate. {ECO:0000256|PIRSR:PIRSR000159-
FT                                1}.
FT   BINDING      62     62       Thiamine pyrophosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   BINDING     112    112       Pyruvate. {ECO:0000256|PIRSR:PIRSR000159-
FT                                1}.
FT   BINDING     814    814       Thiamine pyrophosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   BINDING     837    837       Thiamine pyrophosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   SITE         29     29       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE         62     62       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE        112    112       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE       1000   1000       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
SQ   SEQUENCE   1171 AA;  127277 MW;  3F171E506F8D9B6E CRC64;
     MPKQTLDGNT AAAHVAYAMS EVATIYPITP SSPMAEIADE WAAHGRKNIF GKTLQVAEMQ
     SEAGAAGAVH GSLAAGALTT TFTASQGLLL MIPNMYKIAG ELLPCVFHVA ARALSTHALS
     IFGDHADVMA ARQTGFAMLS SASVQEVMDL ALVAHLATLK ARVPFVHFFD GFRTSHEVQK
     IDVIEYEDMA KLVDWDAIRA FRQRALNPEH PHQRGTAQNP DIYFQSREAA NPYYLATPGI
     VAQVMEQVAG LTGRHYHLFD YAGAPDAERV IVSMGSSCEV IEETVNYLVE KGEKVGLIKV
     RLFRPFSAEH FLKVLPASVK RIAVLDRTKE PGSLGEPLYE DVQTVLAEHG KNILVVGGRY
     GLGSKEFNPS MVKAVFDNLA ATTPKNKFTV GITDDVTHTS LEIKEHIDTS PKGTFRCKFF
     GLGSDGTVGA NKNSIKIIGD HTDMYAQGYF VYDSKKSGGV TISHLRFGKQ PIQSAYLIDQ
     ADLIACHNPS YVGRYNLLEG IKPGGIFLLN STWSAEEMDS RLPADMKRTI ATKKLKFYNI
     DAVKIAQEIG LGSRINVIMQ TAFFKIANVI PVDEAIKYIK DSIVKTYGKK GDKILNMNFA
     AVDRALEALE EIKYPASWAD AVDEAAATVT EEPEFIQKVL RPINALKGDE LPVSTFTPDG
     VFPVGTTKYE KRGIAVNIPQ WQPENCIQCN QCSLVCPHAA IRPYLAKPAD LAGAPETFVT
     KDAIGKEAAG LKFRIQVSPL DCTGCGNCAD VCPAKVKALT MVPLEEVTAV EEANYNFAEQ
     LPEVKVNFNP ATVKGSQFRQ PLLEFSGACA GCGETPYVKL VTQLFGDRMI IANATGCSSI
     WGGSAPACPY TVNRQGHGPA WASSLFEDNA EFGYGMALAV AKRQDELATA ISKALEAPVS
     AAFKAACEGW LAGKDDADRS REYGDRIKAL LPGEISQASG EVKDLLLDID RQKDYLTKKS
     IWIIGGDGWA YDIGYGGLDH VLASGANVNV LVLDTEVYSN TGGQSSKATQ TGAVARFAAG
     GKFTKKKDLG LMAMSYGYVY VASVAMGASH SQLMKALIEA EKYDGPSLII AYAPCINHGI
     NMTYSQREAK KAVEAGYWPL YRYNPQLAQE GKNPFILDYK TPTASFRDFL MGEIRYTSLK
     KQFPEKAEQL FAKAEADAKA RLEQYKKLAE G
//
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