(data stored in ACNUC7421 zone)

SWISSPROT: C8W2Q3_DESAS

ID   C8W2Q3_DESAS            Unreviewed;      1174 AA.
AC   C8W2Q3;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   SubName: Full=Pyruvate ferredoxin/flavodoxin oxidoreductase {ECO:0000313|EMBL:ACV61059.1};
GN   OrderedLocusNames=Dtox_0096 {ECO:0000313|EMBL:ACV61059.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61059.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61059.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000159-50};
CC       Note=Binds 3 [4Fe-4S] clusters per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000159-50};
CC   -!- SIMILARITY: Belongs to the pyruvate:ferredoxin/flavodoxin
CC       oxidoreductase family. {ECO:0000256|PIRNR:PIRNR000159}.
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DR   EMBL; CP001720; ACV61059.1; -; Genomic_DNA.
DR   RefSeq; WP_012813511.1; NC_013216.1.
DR   STRING; 485916.Dtox_0096; -.
DR   EnsemblBacteria; ACV61059; ACV61059; Dtox_0096.
DR   KEGG; dae:Dtox_0096; -.
DR   eggNOG; ENOG4105D95; Bacteria.
DR   eggNOG; COG0674; LUCA.
DR   eggNOG; COG1013; LUCA.
DR   eggNOG; COG1014; LUCA.
DR   HOGENOM; HOG000266425; -.
DR   OMA; PMNALEG; -.
DR   OrthoDB; 10483at2; -.
DR   BioCyc; DACE485916:G1GFV-102-MONOMER; -.
DR   Proteomes; UP000002217; 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   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; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
DR   PRODOM; C8W2Q3.
DR   SWISS-2DPAGE; C8W2Q3.
KW   4Fe-4S {ECO:0000256|PIRSR:PIRSR000159-50};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
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:ACV61059.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transport {ECO:0000256|PIRNR:PIRNR000159}.
FT   DOMAIN      680    709       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   DOMAIN      738    769       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   REGION      967    970       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   REGION      996   1001       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
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       695    695       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       699    699       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       814    814       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       817    817       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       842    842       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL      1076   1076       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     819    819       Thiamine pyrophosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   BINDING     842    842       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       1001   1001       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
SQ   SEQUENCE   1174 AA;  128115 MW;  3964DA28E32EC4A0 CRC64;
     MAKVTKTMDG NEAAAYMSYA FTEVAAIYPI TPSSLMAELV DEWSAYGKRN IFGQPLKVVE
     MQSEGGAAGA VHGSLAAGTL TTTYTCSQGL LLMVPNMYKI SGELLPGVFH VTARAIAGHA
     LSIFGDHQDV MACRPTGFAI LASSSVQEAM DMAGVAHLSA IKGRMPFMHF FDGFRTSHEI
     QKIEVINYED MAKLVDYEAL KEFKSRGLNP EHPVVRGSAQ NPDIYFQGKE AANSYYQKVP
     SIVEGYMQEI GKITGRQYKL FDYYGAADAE YVIVAMGSVC ETIEETIDYL LSKGEKVGVV
     KVRLYRPFSV EHFLAVMPGT VKKIAVMDRT KEHGSVGEPL YLDVVNVFYK KENKPLIVGG
     RYGLGSKDTT PSQIIAVFNN LKQDDPKDRF TVGILDDVTY TSLPEEPLVD TSAEGTICCK
     FWGLGSDGTV GANKSAIKII GDHTDLYAQG YFAYDSKKSG GSTISHLRFG KNPIKSTYLV
     INSDYTACHN SAYIYKYDVL KGLKKNGTFV LNCQWSQEEL EEKLPAKVKR FVAENNINFY
     IIDAVKIAQE IGLGGHINMI MQSAFFKLAN VIPVEDAVKY LKDSIEKSYG KKGDNIVDMN
     FAAVDRGIDA LVKVNVPADW AGVQDEAEVE QNEPDFIKNI LRLMVKNEGD SLPVSAFMER
     VDGSLPVGSS AYEKRGIAVM VPEWQPDNCI QCNQCSFVCP HAAIRPFLLN SEEAAKAPAT
     FITKAAKGKG LEELGLQYRM QVSTLDCTGC GNCVETCPAK EKALVLKSAD EQNSEQVANW
     GFAATVSIKD KLLDPKTLKG SQFKQPLFEF SGACPGCGET PYIKLITQLF GDRMMIANAT
     GCSSIYGASS PAIPYTTNSE GKGPSWANSL FEDNAEFGFG MYLGVKQTRD KLAGLMKQVV
     ETSDSDVLKE ACHEWLAGMN EAEASKAAAS KLLAVLEGID YSGNKAIEEI VEKKDYLVKK
     SQWILGGDGW AYDIGFGGLD HVLASGENVN VLVMDTEVYS NTGGQSSKAT PTGAVAKFAA
     SGKKIKKKDM GLMAMSYGYI YVAQIALGAN MSQALKAIAE AEAYDGPSLI IAYAPCINHG
     IKSGMGTSTA EMKKAVAAGY WHLYRYNPIL KDQGKNPFIL DSKEPQDSYK EFLTGEVRYA
     SLQQTFPDIA EKLFEAAEQD SKERLANYKR LAGE
//

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