ID G2E0Z9_9GAMM Unreviewed; 1646 AA.
AC G2E0Z9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein {ECO:0000313|EMBL:EGV31340.1};
GN ORFNames=ThidrDRAFT_1962 {ECO:0000313|EMBL:EGV31340.1};
OS Thiorhodococcus drewsii AZ1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodococcus.
OX NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV31340.1, ECO:0000313|Proteomes:UP000004200};
RN [1] {ECO:0000313|EMBL:EGV31340.1, ECO:0000313|Proteomes:UP000004200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ1 {ECO:0000313|EMBL:EGV31340.1,
RC ECO:0000313|Proteomes:UP000004200};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA Frigaard N.-U., Bryant D.A., Woyke T.J.;
RT "The draft genome of Thiorhodococcus drewsii AZ1.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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:EGV31340.1}.
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DR EMBL; AFWT01000012; EGV31340.1; -; Genomic_DNA.
DR RefSeq; WP_007040676.1; NZ_AFWT01000012.1.
DR STRING; 765913.ThidrDRAFT_1962; -.
DR PATRIC; fig|765913.3.peg.1993; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1013; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG1141; Bacteria.
DR eggNOG; COG1145; Bacteria.
DR eggNOG; COG1146; Bacteria.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000004200; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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 InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
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 PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF13370; Fer4_13; 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 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 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:EGV31340.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 778..808
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 915..944
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1646 AA; 181971 MW; 83726BC78E81E123 CRC64;
MFGKKDEKQF KYPGTRMAMD GNTAVVMCER EASDAAGAYP ITPSTQMGEY WAEEVASGHL
NVSGNPLIFV EPESEHAAAA VTAGMSMTGL RATNFSSAQG VAFMHESLYA AVGKRLPYVL
NIGSRAITKA SLNVHCAHDD YHCIDDTGFF QVFGKSAQEA ADLNLIARKI AELTLTPAAV
GQDGFLTTHL IEPLMVPERA LIEAFLGRPD DVIECPTPAQ RLVYGPTRRR VPLVWDVDSP
FTSGTVQNQD AYMQAVAGQR PYFFDHIEQI ADQVMDEFYE LTGRRYHRAT PYRCEDADYL
LIGQGSMVTQ AEAVADYLRE SRGLKVGVVN MTMFRPFPGD AIARLLQGKK GVAILERTDQ
PLAEDLPIMR ETRAALTKCL ENGMISKNEE MPYPLYPTYK SGDMPRLYSG CYGLGSRDLQ
PEGLIAAVEN MLPEAKRRKF FYLSVDFMRA AADPKDEIRI QALKDAYPNI GDMALRGSEN
PNLLPKGAVT VRMHSVGGWG AVTTGKNLAM TLYDLLGYDI RANPKYGSEK KGQPTTYFLS
AAPEPIRLNC EYTYVDVVLS PDPNVFTHSD PLSGLDRGGS FVIQSSLDNP EQVWASFPPA
ARKFIVEREI RVFYIDGFKI AREEASNPEL QFRMQGNAFQ GAFFAASPLM ERSGLDEKGL
FASIEEQLRS KFGGKGERVV QDNLRIVRRG FDEIFEITDK PLVSGQFLAR KEPGLPIMLK
TLPEGDGGVS DVHRFWEQTG SFYASGRGSD NLTDPHMALS LMPASTGVYR DMTQIRFAYP
KFVPENCTAC GSCFSVCPDS ALPGLVNKIS DVFATAIARV ERGMPTQYLR RETRTVEKRL
RALIEAAGET ADMRALMDQA VLETLAAFSG EPEQKEAAEK EFGLMMQALA DYQFAITKPY
WTNREKKQKG SGGLFSITVN PYTCKGCMEC IEVCNDGALI DEPQTEDRIK EMQARWGMWL
DLPTTDPDFI RIDDLDDKVG ALETLLLDKK NYQSMVSGDG SCMGCGEKTA LHLFTSTVTA
LMQPRVKRHL AEIDDLINRL ETHIRLKLAS SMDLSDTSAI GKALDSHKDN DLMLSDLSAE
LEDRRAQPVD PDWLKWVTAL LGKLRHLKSQ YTAAQPRAEM GIVNSTGCSS VWGATFPYNP
YPFPWSNNLF QDAPSMALGL FEGHMRKMGE GFKAIRQARQ ELDGTFNAAN PASNLTYFGW
KDFSDEEWKL CPPVVAIGGD GAMYDIGFQN LSRALMSGHP VKILVLDTQA YSNTGGQSCT
SGFIGQVADM APYGKQWKGK TEVRKEMGLI GMAHRTSFVL NSSASHLTHL LEGYIDGLNS
RRPALFNVYT SCQPEHGIGD DMSNKHARMA VESRAYPLFR FDPDAGTSFE ECCSIEGNPN
VDQDWISWSL KYINEKGEPA EMEVPFTFVD FAMSEGRFRK HFRKAPPETW NDSMVRMDEF
LNLDDSDRDG LYPYIWAVDA KNRLMRVLVS QELVLSCEER RHFWTQIRGI CGELNKVDVE
AVRNQAKAEM AQKLTSSLLA MAVGEGNGLA GLVGAAPVNG GGHNGNGAAH AGANGSGNNG
AGADADPVWV ETPECTACDE CITINPKIFK YNTDKKVEIL DPKGGPFKDI VKAAEKCGAN
CIHPGMPWNP AETGLDKLIK RAEKFQ
//
