ID B9CZV4_CAMRE Unreviewed; 1193 AA.
AC B9CZV4;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE SubName: Full=Pyruvate synthase {ECO:0000313|EMBL:EEF14806.1};
DE EC=1.2.7.1 {ECO:0000313|EMBL:EEF14806.1};
GN Name=nifJ {ECO:0000313|EMBL:EEF14806.1};
GN ORFNames=CAMRE0001_0800 {ECO:0000313|EMBL:EEF14806.1};
OS Campylobacter rectus RM3267.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=553218 {ECO:0000313|EMBL:EEF14806.1, ECO:0000313|Proteomes:UP000003082};
RN [1] {ECO:0000313|EMBL:EEF14806.1, ECO:0000313|Proteomes:UP000003082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM3267 {ECO:0000313|EMBL:EEF14806.1,
RC ECO:0000313|Proteomes:UP000003082};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00009032,
CC ECO:0000256|PIRNR:PIRNR000159}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEF14806.1}.
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DR EMBL; ACFU01000004; EEF14806.1; -; Genomic_DNA.
DR RefSeq; WP_004318812.1; NZ_ACFU01000004.1.
DR AlphaFoldDB; B9CZV4; -.
DR STRING; 553218.CAMRE0001_0800; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1013; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG1143; Bacteria.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000003082; 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:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR CDD; cd03377; TPP_PFOR_PNO; 1.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR Gene3D; 4.10.780.10; Pyruvate-flavodoxin oxidoreductase, EKR domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR037112; Pyrv-flavodox_OxR_EKR_sf.
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_TPP-bd.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR NCBIfam; TIGR02176; pyruv_ox_red; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
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; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 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|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR000159-50};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR000159};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000159-50};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000159-
KW 50};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000159-50};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000159}; Pyruvate {ECO:0000313|EMBL:EEF14806.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT DOMAIN 682..711
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 740..771
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 31
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 64
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 114
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 691
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 694
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 697
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 701
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 749
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 752
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 755
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 759
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 818
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 821
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 823
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 846
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 846
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 968..971
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 997..1002
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 1077
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT SITE 31
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 64
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 114
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 1002
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ SEQUENCE 1193 AA; 130951 MW; FDE0BCDE5E0B77B1 CRC64;
MAKIMKTMDG NEAAAYASYA FTEVAGIYPI TPSSPMADYT DMWAAQGKKN LFGMPVKVVE
MQSEGGAAGT VHGSLQVGAL TTTYTASQGL LLKIPNMYKI AGQLLPGVIH VSARSLAAQA
LSIFGDHQDI YACRQTGFAM LASGSVQEVM DIAGVAHLAA IKGRVPFLHF FDGFRTSHEI
QKVEVLDYEH FDRLLDREAV RKFRDEALSP ESPKTRGTAQ NDDIYFQTRE LSNRYYDAVP
DIVAEYLKEI SKITGRDYKP FNYYGDPQAT RVVVAMGSVT QTLEEVVDHL RAKGEKVGVI
KVHLYRPFSL KYLFDVMPET VEKIAVLDRT KEPGSLGEPL YLDVKAAFYG RKNQPVIVGG
RYGLSSKDVG PAQMLAVFEN LNLEGPKNGF TVGIEDDVTF TSLKVGEKIS LSDASVKECL
FYGLGADGTV GANKNSIKII GDKTELYAQA YFAYDSKKSG GYTRSHLRFG KNPIRSTYLV
SNPHFVACSV AAYLEIYDVI DGIREGGTFL LNSIWDAEQT IAKLPNKVKK ILAEKRVNFY
IINATKLARE IGLKNRTNTI MQSAFFKLAD IIPFADAQKY MKEYAHKAYA KKGEAIVEMN
YKAIDMGADG LVKVAVDPSW ANLTDDAANE EKYVGDEFIE KIVKPINAAR GDSLPVSAFV
GFEDGHFKSG TTAYEKRGIG VMVPKWIEEN CIQCNQCAFV CPHAVIRPFL IDENELAAAP
QTVQDHVLDA KGKEVKGLKY KIQVSPLDCT GCELCAQNCP SKEKSLVMVP LAEEMEKNEQ
ENADYLFKKV TYKDDLMSKE SVKGVGFAQP LFEFHGACPG CGETPYLGLV TRLFGDRMIV
ANATGCSSIY GGSAPSTPYT TNKDGKGVAW ANSLFEDNAE FGMGMNVAVE TLRHRIEDVM
LRTKDAAPNA LAALYSDWIA HKNDGEKTTQ IAKILTPLLE QNLSVPGVKE ILELKRYLVK
KSQWIIGGDG WAYDIGFGGL DHVLASGENV NVLVLDTEVY SNTGGQSSKS SRAGSIAQFT
ASGKPMQKKD LGYIAMTYGN IFVAQINSNA SQANTIKAIA AAEAYDGPSL VIAYSPCIAH
GIKGGMALSG DQGELATKCG YWPTYVYDPR LIKEGKNPLK MTSKEPDWSL YEEFLLNEVR
YNSLKKTNPE HADELLAKNK ADAQRRYRQL KRLSLADFSD EVESSAETAE SAE
//
