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Database: UniProt
Entry: J5UFJ6_9FIRM
LinkDB: J5UFJ6_9FIRM
Original site: J5UFJ6_9FIRM 
ID   J5UFJ6_9FIRM            Unreviewed;      1167 AA.
AC   J5UFJ6;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   12-SEP-2018, entry version 29.
DE   RecName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000256|PIRNR:PIRNR000159};
DE            EC=1.2.7.- {ECO:0000256|PIRNR:PIRNR000159};
GN   Name=nifJ_1 {ECO:0000313|EMBL:EJU22119.1};
GN   ORFNames=HMPREF1143_0753 {ECO:0000313|EMBL:EJU22119.1};
OS   Peptoanaerobacter stomatis.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Peptostreptococcaceae; Peptoanaerobacter.
OX   NCBI_TaxID=796937 {ECO:0000313|EMBL:EJU22119.1, ECO:0000313|Proteomes:UP000005244};
RN   [1] {ECO:0000313|EMBL:EJU22119.1, ECO:0000313|Proteomes:UP000005244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OBRC8 {ECO:0000313|EMBL:EJU22119.1,
RC   ECO:0000313|Proteomes:UP000005244};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JUL-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:EJU22119.1}.
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DR   EMBL; ALNK01000023; EJU22119.1; -; Genomic_DNA.
DR   RefSeq; WP_009531099.1; NZ_ALNK01000023.1.
DR   EnsemblBacteria; EJU22119; EJU22119; HMPREF1143_0753.
DR   PATRIC; fig|796941.3.peg.1293; -.
DR   OrthoDB; POG091H02IV; -.
DR   Proteomes; UP000005244; 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:UP000005244};
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:EJU22119.1}; Pyruvate {ECO:0000313|EMBL:EJU22119.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005244};
KW   Transport {ECO:0000256|PIRNR:PIRNR000159}.
FT   DOMAIN      678    707       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   DOMAIN      734    765       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   REGION      959    962       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   REGION      988    993       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   METAL       687    687       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       690    690       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       693    693       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       697    697       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       743    743       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       746    746       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       749    749       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   METAL       753    753       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      1068   1068       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000256|PIRSR:PIRSR000159-50}.
FT   BINDING      30     30       Pyruvate. {ECO:0000256|PIRSR:PIRSR000159-
FT                                1}.
FT   BINDING      63     63       Thiamine pyrophosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000159-1}.
FT   BINDING     113    113       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         30     30       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE         63     63       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE        113    113       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
FT   SITE        993    993       Important for catalytic activity.
FT                                {ECO:0000256|PIRSR:PIRSR000159-2}.
SQ   SEQUENCE   1167 AA;  129807 MW;  5887EF19E9D99145 CRC64;
     MKKMITLNGN TAAATVAYAF SEVAPIYPIT PSSDMSELID AWAANNKENI FGEQVQVTEL
     QSEAGAAGAM HGALSAGVLA TSFTSSQGLL LMIPNMYKMS GELLPGVIHV AARALSTHAL
     SIFGDHQDVM ACRQTGFAMM ASGSVQEILD LGAISHLTAI KTRIPFLHFF DGFRTSHEFQ
     KVESVDYDIY KQLVDKQAIL NFRNKSMNPE HPYTKGTAQN PDVYFQGAEA SNKRYDTVVP
     TVIEYMEKLG ELTGRKYKPF DYVGAKDAKH IIIAMGSVNE TIEETISYLI EQGEKVGLVK
     VRLYRPFSKE ALLSVIPKTV EVISVLDRTK EKGSPFEPLH YDILGAYSGE ENKPVIVGGR
     YGLGSKNTTP SQIKAVFDNM KADKPKDRFT IGIIDDITHT NLEIKDIITT EPKDTIKCKF
     WGFGSDGTVG ANKSAIKIIG DGTDMYAQAY FAYDSKKSGG VTISHLRFGS KPIQSTYLIT
     KPDFISCSMQ SYVDNYHLLE GIKEGGTFLL NTIWNIDELS KNLPAHMKRE LYEKKINFYT
     INATHIAEEI GLGTRTNMIM QSAFFKLSNV IPIEEAVERL KESIKKTYGK KGDAIVNMNY
     LAVDKGKDDL VKIEIPEDWK DAQDKPVEKD YPKYVKEILI PLNSQKGDNK PVSAFMEREE
     GSMPNGTTKY EKRAVAVNVP KWNKDNCIQC NQCSFVCPHA VIRPFLLNEE ENANKPEGFQ
     TIKANGKGLD NLQYKIQVSV LDCTGCGNCA NVCPAKEKAL TMVPLGEELE ESKNWDYAMT
     LSPKEELMED NTVKGSQFKQ PLLEFHGACA GCGETPYATL VTQLFGDRML IANASGCSSI
     WGGSYPSTGF TTNHEGHGPA WASSLFEDNA EYGYGMALAV KKLRNTIKLH MEKYMKANPN
     SECEEVFNKW IDNMKDPKIT KSLKNQIVEL TKNSADKDLK EINDLKDYLV KQSIWSFGGD
     GWAYDIGYGG LDHVMASGED FNILVFDTEV YSNTGGQSSK STPRAAVAKF AASGKKVRKK
     DLGAMLMTYG YVYVAQVAMG ANMNQLIKAL KEAESYDGPS IVICYAPCIN HGIHSGMGTT
     INQEKRAVDC GYWHLYRYNP LLIEEGKNPF TLDSKEPKAS FQEFLDSEVR YTSLKKTFPE
     IAQELYDMAK EDSVFRYKRY KKMAENN
//
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