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Database: UniProt
Entry: R6PHW1_9CLOT
LinkDB: R6PHW1_9CLOT
Original site: R6PHW1_9CLOT 
ID   R6PHW1_9CLOT            Unreviewed;      1178 AA.
AC   R6PHW1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   12-SEP-2018, entry version 20.
DE   RecName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000256|PIRNR:PIRNR000159};
DE            EC=1.2.7.- {ECO:0000256|PIRNR:PIRNR000159};
GN   ORFNames=BN618_01555 {ECO:0000313|EMBL:CDC23938.1};
OS   Clostridium nexile CAG:348.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium; environmental samples.
OX   NCBI_TaxID=1263069 {ECO:0000313|EMBL:CDC23938.1, ECO:0000313|Proteomes:UP000018368};
RN   [1] {ECO:0000313|EMBL:CDC23938.1, ECO:0000313|Proteomes:UP000018368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:348 {ECO:0000313|Proteomes:UP000018368};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CDC23938.1}.
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DR   EMBL; CBEY010000107; CDC23938.1; -; Genomic_DNA.
DR   Proteomes; UP000018368; Unassembled WGS sequence.
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   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR033412; PFOR_II.
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   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|PIRSR:PIRSR000159-50};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018368};
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:CDC23938.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018368};
KW   Transport {ECO:0000256|PIRNR:PIRNR000159}.
FT   DOMAIN      684    713       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   DOMAIN      738    758       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   REGION      969    972       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   REGION      998   1003       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   METAL       693    693       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       696    696       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       699    699       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       703    703       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       747    747       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       750    750       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       753    753       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       757    757       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       818    818       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       821    821       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       846    846       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL      1078   1078       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   BINDING      31     31       Pyruvate. {ECO:0000256|PIRSR:PIRSR000159-
FT                                1}.
FT   BINDING      64     64       Thiamine pyrophosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   BINDING     114    114       Pyruvate. {ECO:0000256|PIRSR:PIRSR000159-
FT                                1}.
FT   BINDING     823    823       Thiamine pyrophosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   BINDING     846    846       Thiamine pyrophosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   SITE         31     31       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE         64     64       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE        114    114       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE       1003   1003       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
SQ   SEQUENCE   1178 AA;  127785 MW;  6E1C446A91AB3431 CRC64;
     MGRKMKTMDG NHAAAHASYA FTDVAAIYPI TPSSVMAEAT DEWATQGRTN IFGQTVQVTE
     MQSEAGAAGT VHGSLAAGAL TTTYTASQGL LLMIPNLYKI AGEQLPGVFN VSARALASHA
     LSIFGDHSDV YACRQTGCAM LCESSVQEVM DLTPVAHLSA IKGKIPFINF FDGFRTSHEI
     QKIETWDYED LKDMADMDAI DAFRKHALNP NHPCQRGSAQ NPDIFFQARE ACNPFYDAMP
     AIVQEYMDKV NEKIGTNYKL FNYHGAEDAE HVIIAMGSVC DTIDETVDYL LAAGRKVGVV
     KVRLYRPFCA EALINAIPES VKQITVLDRT KEPGALGEPL YLDVVASLKG TKFDAVPVFT
     GRYGLGSKDT TPAQIVAVYD NTEKQKFTIG IVDDVTNLSL EVGAPLVTTP EGTINCKFWG
     LGADGTVGAN KNSIKIIGDN TDMYAQAYFD YDSKKSGGVT MSHLRFGKSP IKSTYLIKQA
     NFVACHNPSY INKYNMVQEL VDGGTFLLNC PWDMEGIEKH LPGQVKAFIA NHNIKFYVID
     GIKIGKEIGL GGRINTVLQS AFFKLANIIP EEHAIELMKA AAKASYGKKG DKIVQMNYDA
     IDAGAKQVVE IEVPESWKDA EDEGLFTPEV KGGREDVVDF VKNIQAKVNA QEGNSLPVSA
     FTEYVDGTTP SGSSAYEKRG IAVDIPVWQP ENCIQCNRCA YVCPHAVIRP VALTEEEVAN
     APEGLETIDM VGMPGLKFTM TVSAYDCTGC GSCANVCPGK KGEKALVMKN MEENAGKQDF
     FDYGREIPVK PEVVAKFKET TVKGSQFKQP LLEFSGACAG CGETPYAKLI TQLFGDRMYI
     ANATGCSSIW GNSSPSTPYT VNEKGQGPAW SNSLFEDNAE FGYGMLLAQK ALRNGLKAKV
     ESVAASEAAS EEVKAACKEW LDTFNCGATN GTATDNLVAA LEGADCEVCK DIVNNKDFLA
     KKSQWIFGGD GWAYDIGFGG VDHVLASGQD INIMVFDTEV YSNTGGQSSK STPTGAIAQF
     AAGGKEVKKK DMASIAMSYG YVYVAQIAMG ADFNQTVKAI AEAEAYPGPS LIIAYAPCIN
     HGIKKGMSKA QTEEELAVKS GYWHNFRFNP AAENKFTLDS KAPTEDYKEF LNGEVRYNAL
     ARMNPERAEE LFAKSEEAAK ERYAYLNKLV TLYGNDAE
//
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