ID A0A0S8DZB3_9BACT Unreviewed; 551 AA.
AC A0A0S8DZB3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000313|EMBL:KPK40781.1};
DE Flags: Fragment;
GN ORFNames=AMJ65_10370 {ECO:0000313|EMBL:KPK40781.1};
OS Phycisphaerae bacterium SG8_4.
OC Bacteria; Planctomycetota; Phycisphaerae.
OX NCBI_TaxID=1703409 {ECO:0000313|EMBL:KPK40781.1, ECO:0000313|Proteomes:UP000051853};
RN [1] {ECO:0000313|EMBL:KPK40781.1, ECO:0000313|Proteomes:UP000051853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_4 {ECO:0000313|EMBL:KPK40781.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- SIMILARITY: Belongs to the pyruvate:ferredoxin/flavodoxin
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009032}.
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:KPK40781.1}.
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DR EMBL; LJTR01000171; KPK40781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8DZB3; -.
DR PATRIC; fig|1703409.3.peg.4413; -.
DR Proteomes; UP000051853; Unassembled WGS sequence.
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:0022900; P:electron transport chain; IEA:InterPro.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR033412; PFOR_II.
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; 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; PF17147; PFOR_II; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:KPK40781.1}.
FT DOMAIN 18..247
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 269..351
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT DOMAIN 433..550
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT NON_TER 551
FT /evidence="ECO:0000313|EMBL:KPK40781.1"
SQ SEQUENCE 551 AA; 60068 MW; E038D261F6B7FAF1 CRC64;
MKRKMVIIEG NTAAAYVAHA TNEVIAIYPI TPSSPMGEIS DAKTAKGEVN IWGTVPSVTE
MQSEAGAAGA VHGALATGAL TTTFTASQGL LLMIPNMYKI AGELLPTVFH ISARSLACQA
LSIFGDHSDV MTCRETGFAM LCSNSIQEVM DFALIAQQAT LASQVPFLHF FDGFRTSHEV
QKVEELTLDD MRAMIDDELV ARHKARALTP DRPMISGTAQ NPDVYFQGRE TVNKYYLAVP
KIVQETMDKF AKIVGRQYRL FDYVGAPDAD KVIVVMGSAA DTAHETLEYM VSKGEKVGVV
KVRLFQPFSI EDFIAAIPPT TTKIAVLDRT KEPGSIGEPL YLNVRTAVGE AMGKGEAPFK
GYPVIVGGRY GLGSKDLTPA MVKAVFDNLD ADKPKYEFTV GITEDVTGTS LEVDESYDVP
DEGFFSGLFY GLGSDGTVGA NRNSIKIIGD LTDNYAQAYF VYDSKKAGAV TVSHLRFGDK
LIRRPYLVSK ADFVACHNPA FLEQFDMLTP ARDGSTFLLT SSHGPQEVWD TLPQEVQKQI
IDKKLKFYAI D
//
