ID A0A1Z9GX37_9PROT Unreviewed; 677 AA.
AC A0A1Z9GX37;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000313|EMBL:OUV98522.1};
DE Flags: Fragment;
GN ORFNames=CBD14_06820 {ECO:0000313|EMBL:OUV98522.1};
OS Proteobacteria bacterium TMED154.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1986844 {ECO:0000313|EMBL:OUV98522.1, ECO:0000313|Proteomes:UP000196632};
RN [1] {ECO:0000313|EMBL:OUV98522.1, ECO:0000313|Proteomes:UP000196632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED154 {ECO:0000313|EMBL:OUV98522.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-2017) 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:OUV98522.1}.
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DR EMBL; NHHD01000085; OUV98522.1; -; Genomic_DNA.
DR Proteomes; UP000196632; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-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 Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 2.10.240.10; Dihydroorotate dehydrogenase, electron transfer subunit; 1.
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; IPR037117; Dihydroorotate_DH_ele_sf.
DR InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
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; PF10418; DHODB_Fe-S_bind; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01558; POR; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; 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:OUV98522.1}.
FT DOMAIN 504..533
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT COILED 564..591
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 677
FT /evidence="ECO:0000313|EMBL:OUV98522.1"
SQ SEQUENCE 677 AA; 74875 MW; FB1808AF02543F75 CRC64;
MPRFVVQAME EYTXLTGXEY HPVQXVWTED ADWIXLGMGS VTDDAEAVAS HLRXXGKRVG
VVSVKLLHPF PEXDVIRALQ GKKAVTVLER SGTTALTQLV NQALYRSXEN HXTERHPGIP
GLSELPSVST AIFGLGGHXL QPRHLVAAFE NMISXXNVPL YYLGSKFFSD XTSPEMNXXQ
EQLKXAYPET VSMALETGEN XKLLPKEAIR VRFHSVGGYG XIASGKLLTD ILAAXLGLHS
KSAPKYGSEK SGAPTNFYLT LSPEPIKITN AQLEEVEIVI SPDHKVFEHT NPLNGLVEGG
TFXMQSGQNP REVWQELPEH ARXTLRDRDI HFLIVDAFGV ARRHAPSPDL QVRMMGVVFI
GALCAXDERI RQGTSGEDLL EKIQQQVNKK FGAKGPEVVR SNMLVLKEGM ESTQEVDYRL
PEFTDIIPSE EETEEIGLEL SAEMGIHGHS ADYAGLGDTG YFNATVAQPF KDGSIDESPV
LPGIGLFMPS GSASWKDKGL FRLSVPEFQP ELCTGCLECT LVCPDAAIPN TLHEIQDLLN
TSLETLKLSQ RQREHLQRFL LPLVQGIREE LRNSESNIAF AEAAAKALDQ MEDLKPQFRK
QLSEMLIRLS SFPLARTRTF YDATEQKNPG NGVMYSVMID ATGMCGACMV PIHKEDKLLR
KHACVDGPEF DAHSIDW
//
