ID A0A1S2LKE3_9BACI Unreviewed; 767 AA.
AC A0A1S2LKE3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Pyruvate synthase {ECO:0000313|EMBL:OIJ12784.1};
GN ORFNames=BKP35_09390 {ECO:0000313|EMBL:OIJ12784.1};
OS Anaerobacillus arseniciselenatis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX NCBI_TaxID=85682 {ECO:0000313|EMBL:OIJ12784.1, ECO:0000313|Proteomes:UP000180098};
RN [1] {ECO:0000313|EMBL:OIJ12784.1, ECO:0000313|Proteomes:UP000180098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15340 {ECO:0000313|EMBL:OIJ12784.1,
RC ECO:0000313|Proteomes:UP000180098};
RA Bassil N.M., Lloyd J.R.;
RT "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT Anaerobacillus genus.";
RL Submitted (OCT-2016) 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:OIJ12784.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MLQQ01000018; OIJ12784.1; -; Genomic_DNA.
DR RefSeq; WP_071313091.1; NZ_MLQQ01000018.1.
DR AlphaFoldDB; A0A1S2LKE3; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000180098; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; 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; -; 3.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
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; PF17147; PFOR_II; 1.
DR Pfam; PF01855; POR_N; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
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:ARBA00022485};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:OIJ12784.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000180098};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 33..259
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 281..385
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT DOMAIN 549..655
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 767 AA; 85382 MW; 4A511C839C21FAA3 CRC64;
MAKLENKLNN NDINTKYEQT TTFESGNEMA AMAAAQINYH VMGYFPITPS TEVAQYLDLM
KSQGLHDIEL IAADGEHGSA GICFGASATG ARVFNATSAN GFLYMLEQMP VQSGLRFPMV
MNLVTRAVSG PLDIRGDHSD LYYALNTGWV ILTARTPQAV YDMNIMALKL AEHKDVRLPV
IVAYDGFFTS HQKRKVDYFK DRKTVQNFVG EMPTEYPRAC VKDQPVTIGA HMNGDDLINN
NFQQSEALYR AGQVFEEIQK EYAEISGRGY ETLDLYGMED ADVALFLLNS AAESAKDVVD
KLRKQGIKAG VISPNIIRPF PAKEIREALK NVKSVLVGER ADSYGGNGPN LTHEVKSALQ
EDKENETIVL SRVFGVGGKD FYADDAEKFF EMAIDAMERG VAERPFDYYG HVPGNPENKL
EPVIEPMKGE DFNSGLIKVT QDEETNKLNV KVPPLRALTA KPKRFGSGHG ACPGCGIFPG
LELFFKGIEG DAVILFQTGC GYVVTTAYPH SSHKQTFIHN LFQSGAATLS GTLEAFFEMK
RRGEIDISDD FTFVMITGDG GMDIGMGSAI GTALRNHKMI ILEYDNEGYM NTGSQMSYST
PLGHMTSTTT IGKTKQGKAF HHKDTAQIMA ATNIPYVFTG TEAYPQDLIK KAAKAQWYAQ
NVGMAYGKIL ITCPLNWKSE DRLGEEIMRK AVESCFFPLY EIEQGETTIT YDPEAKKKRV
ELSEWLKMMG KTKHLLKESN APMLKDFEEE VERRWKRLKT KHETPFV
//
