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Database: UniProt
Entry: F0H027_9FIRM
LinkDB: F0H027_9FIRM
Original site: F0H027_9FIRM 
ID   F0H027_9FIRM            Unreviewed;      1177 AA.
AC   F0H027;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   10-OCT-2018, entry version 39.
DE   RecName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000256|PIRNR:PIRNR000159};
DE            EC=1.2.7.- {ECO:0000256|PIRNR:PIRNR000159};
GN   Name=nifJ {ECO:0000313|EMBL:EGC84195.1};
GN   ORFNames=HMPREF9246_0962 {ECO:0000313|EMBL:EGC84195.1};
OS   Anaerococcus hydrogenalis ACS-025-V-Sch4.
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Anaerococcus.
OX   NCBI_TaxID=879306 {ECO:0000313|EMBL:EGC84195.1, ECO:0000313|Proteomes:UP000005277};
RN   [1] {ECO:0000313|EMBL:EGC84195.1, ECO:0000313|Proteomes:UP000005277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-025-V-Sch4 {ECO:0000313|EMBL:EGC84195.1,
RC   ECO:0000313|Proteomes:UP000005277};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JAN-2011) 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   -!- 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 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:EGC84195.1}.
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DR   EMBL; AEXN01000014; EGC84195.1; -; Genomic_DNA.
DR   RefSeq; WP_004816963.1; NZ_AEXN01000014.1.
DR   EnsemblBacteria; EGC84195; EGC84195; HMPREF9246_0962.
DR   OrthoDB; POG091H02IV; -.
DR   Proteomes; UP000005277; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005277};
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   ECO:0000313|EMBL:EGC84195.1}; Pyruvate {ECO:0000313|EMBL:EGC84195.1};
KW   Transport {ECO:0000256|PIRNR:PIRNR000159}.
FT   DOMAIN      682    711       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   DOMAIN      738    769       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   REGION      970    973       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   REGION      999   1004       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   COILED     1157   1177       {ECO:0000256|SAM:Coils}.
FT   METAL       691    691       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       694    694       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       697    697       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       701    701       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       815    815       Iron-sulfur 3 (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       843    843       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL      1079   1079       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   BINDING      33     33       Pyruvate. {ECO:0000256|PIRSR:PIRSR000159-
FT                                1}.
FT   BINDING      66     66       Thiamine pyrophosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   BINDING     116    116       Pyruvate. {ECO:0000256|PIRSR:PIRSR000159-
FT                                1}.
FT   BINDING     820    820       Thiamine pyrophosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   BINDING     843    843       Thiamine pyrophosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   SITE         33     33       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE         66     66       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE        116    116       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE       1004   1004       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
SQ   SEQUENCE   1177 AA;  131187 MW;  98DFD32C8A791F29 CRC64;
     MTIKRRKVTM DGNTAAAHVS YAFSEVSAIY PITPSSPMPE FIDKWAANER LNLFGNPVSV
     TEMQHEAGAA GAVHGSLAAG ALTSTYTASQ GLLLMIPDMY KIAGERLPAV FHVAARSLST
     SAINMYGDHQ DVMAARATGF AMLAEGSVQE IMDLSPVAHL AAIKGRVPFV NFFDGFRTSH
     EIQKIDVWDY DQFEDMVDWK AIDDFKNDSL NPHRPTMRGV FEKSGYFQRA EAQNKAYDAI
     PEIVLSYMEK VNEKIGTNYS LFNYVGADDA TDIIVAMGSG TDTIQQTVEE LNKEGRKVGL
     VKVHLYRPFS TKHLLEAIPE TVERIAVLDR TKEKGSAGEP LYLDVLEAFS DSDRNPKIIA
     GRYGLGQKDT RPAHFKSVFD NLAKDKPKNH FTVGINDDVT HTSLEVDDSF VINDGKTTRC
     IFWGNGGDGT VGANKSAIKI IGDNTDMFAQ GYFDYDAKKS NGLTMSHLRF SPNPIHAAYF
     IDEADFVSCS PQAYVRQYDL VKNLKEGGIF LLNTIWSEDE LEEHIPNYLL KEITDKNIKF
     YTVNASKIAQ EVGLGHRTNM VIQTAFFILS EVLPIDDAIK YLKDSIEKSY GMKGQDIVDM
     NNKAVDRASE ELQEIKVKEE WKNLKDDREG ENENEPDFIK NMVRPIINLK EDDLPVSTYL
     PYDDGQYMAG TSRYEKRGIA LFVPEWNIDN CIQCNQCSYI CPHATIRPFL LDEEQKAKAP
     EGFETKKAIG KGLEGYEFRI QVSPYDCMGC GNCVDVCPAP KKALAMKPID EQIEKQADNW
     EFAHGEVGYR DDEIAPTNVK NSQFSQPLLE FSGACAGCGE TPYAKLITQL YGDHQIISNA
     TGCSSIWGSS VPSMPYCTNK NGEGPAWASS LFEDAAEYGY GMLLATKSNK FLLETLMKKF
     LELKVSTPLN DAFNEWLENN DDFEQSKKAA IKIESLIANE TDNEEANKII ERIKNLKDYL
     VKKSVWIYGG DGWAYDIGFS GVDHVLASGD DINIIVFDTE VYSNTGGQSS KATPLAAVAK
     FAASGKKVRK KDLGLMMTTY GYVYVAQVAM GANQAQTLKA IKEAESYHGP SLIIAYAPCI
     NHGLKAGMGK TQRREKEAVA SGYWHLWRFN PLLKEEGKNP FSLDSKDPTE SFQEFLQGEV
     RYASLKKAFP EDADRLYSEA EEAAKERLES YKKMENK
//
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