(data stored in SCRATCH zone)

SWISSPROT: C8W1Z7_DESAS

ID   C8W1Z7_DESAS            Unreviewed;      1207 AA.
AC   C8W1Z7;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   SubName: Full=Pyruvate ferredoxin/flavodoxin oxidoreductase {ECO:0000313|EMBL:ACV61051.1};
GN   OrderedLocusNames=Dtox_0088 {ECO:0000313|EMBL:ACV61051.1};
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:ACV61051.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61051.1, 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; ACV61051.1; -; Genomic_DNA.
DR   RefSeq; WP_012813503.1; NC_013216.1.
DR   STRING; 485916.Dtox_0088; -.
DR   EnsemblBacteria; ACV61051; ACV61051; Dtox_0088.
DR   KEGG; dae:Dtox_0088; -.
DR   eggNOG; ENOG4105D95; Bacteria.
DR   eggNOG; COG0674; LUCA.
DR   eggNOG; COG1013; LUCA.
DR   eggNOG; COG1014; LUCA.
DR   HOGENOM; HOG000266425; -.
DR   KO; K03737; -.
DR   OMA; GANMNQT; -.
DR   OrthoDB; 10483at2; -.
DR   BioCyc; DACE485916:G1GFV-92-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; PF12838; Fer4_7; 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;
DR   PRODOM; C8W1Z7.
DR   SWISS-2DPAGE; C8W1Z7.
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:ACV61051.1};
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      736    767       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   REGION      999   1002       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   REGION     1028   1033       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       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       751    751       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       755    755       Iron-sulfur 1 (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       815    815       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       840    840       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL      1108   1108       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     817    817       Thiamine pyrophosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   BINDING     840    840       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       1033   1033       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
SQ   SEQUENCE   1207 AA;  133053 MW;  4BABF344B767A0AB CRC64;
     MAKASKTMDG NEAAAYISYP FTEVAAIYPI TPSTPMAESV DLWAAHGKKN FFGQTVRVVE
     FQSEAGASGG MHGSLAAGAL TTTYTASQGL LLMIPNMYKM AGELLPAVFH VTARAIATHA
     LSIFGDHQDV MSCRQTGVAL LASASVQEAM DLGCIAHLSA IKSRIPFLHF FDGFRTSHEV
     QKIEVLDYTE VSKLLDYEAI KEFRDRSLNP EHPSIRGTAQ NPDIYFQGRE ASNPLYDKVP
     DIVESYMREI SRITGRDYKP FDYYGAEDAE YVIVAMGSVC ETIDETIDYL RGKGEKVGTI
     RVRLYRPFSA QHFFNVLPPS VKSIAVLDRS KEPGSVGEPL YLDIVKSFYN KDKKPVLVGG
     RYGLGSKDTR PSQIIAVFNN LKSGTPKDRF TIGIHDDVTH TSLPEEDIIE TTPQGTINCK
     FWGLGSDGTV GANKTAIKII GDNTNLYAQG YFSYDSKKSG GTTVSHLRFG KQPIRSTYLV
     YNADYIACHN SSFIFHYDLL KGLKKNGTFV LNCHWKTNEL EEKLPSYIKR YLAQNHINFY
     IINAIDIASE IGLGARINMI MQAAFFKLAN VIPLENAVKY LKDSIVSSYG HKGQNIVDMN
     NKAVDKGISS LVKVEVPAGW ANADDENQPV KEEPFFTKNF QRPMARMEGD ELPVSAFKGR
     EDGTFPLSTT AYEKRGIAAR IPQWQPEKCI QCNQCSFICP HAVVRPFLLN EEEVKKAPSS
     FITKKATGKG LEGLQYRIQI TPLDCTGCGN CADVCPAPGK ALIMNDPEEE IAAQSDNWEF
     ARLLTGKSHL IDHRTVKGSQ FAKPLFEFNG ACPGCGETPY IKLLTQLFGD RMMIANATGC
     SSIYSASAPS FPYTTTAEGK GPAWGNSLFE DNAEYGYGML LGVSQIRERL ADLMRTALGE
     KSAGELNSDL TLEAAHGKAS DQVLRQISPE AAAVPLSAEL QEAFREWLAG MYDGEASKSA
     AAKILAALKD FGNAENQLIK EIIDKKDFLI KKSQWIIGGD GWAYDIDFGG LDHVLAAGED
     VNMLVLDTEV YSNTGGQSSK STPTAAVAKF AASGKKIKKK DLGMMMMNYG YVYVAQICMG
     ANMNQTVKAM VEAESYKGPS LIIAYSPCIN HGIRSGMGTS IAEEKKAVEA GYWHMYRYNP
     MLKEEGKNPF ILDSKEPNES YKDFIKGEIR YSSLLNAFPE HAEKLMEESA KQARERYEGY
     KKLAETK
//

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