ID A6TMI9_ALKMQ Unreviewed; 573 AA.
AC A6TMI9;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein {ECO:0000313|EMBL:ABR47407.1};
GN OrderedLocusNames=Amet_1199 {ECO:0000313|EMBL:ABR47407.1};
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR47407.1, ECO:0000313|Proteomes:UP000001572};
RN [1] {ECO:0000313|Proteomes:UP000001572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
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DR EMBL; CP000724; ABR47407.1; -; Genomic_DNA.
DR RefSeq; WP_012062448.1; NC_009633.1.
DR AlphaFoldDB; A6TMI9; -.
DR STRING; 293826.Amet_1199; -.
DR KEGG; amt:Amet_1199; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR HOGENOM; CLU_017038_1_0_9; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000001572; Chromosome.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; 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; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
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; IPR009014; Transketo_C/PFOR_II.
DR NCBIfam; TIGR03710; OAFO_sf; 1.
DR PANTHER; PTHR32154:SF20; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORA; 1.
DR PANTHER; PTHR32154; 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 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:ABR47407.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001572}.
FT DOMAIN 14..171
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 209..450
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 476..562
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT REGION 416..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 62657 MW; 8E374A8AF4F00983 CRC64;
MPESYTLLIG GIQGEGVVST GLNLMRSLSS LGFYTYGSRR FSSRIKGGNT SFKISISTKK
QLCTQDSVDS LFALDLETIS LYENQLKEGG ILLYDADLAP SFSKNSSLTY VPVPITQIAK
ESGALLMKNT CTIGFIGQLL GISEDDLIPS IKERYDKKGK QVVEKNLKVL SNSFGYKSDV
IDQHKHSLGS KPVPTSRPLM IGNEAIALGA LMAGCRFIPA YPITPASEIM EYLGSVLPQY
GGVMIQVEDE ISAVTMAIGA SYAGVRSMTA SSGPGLSLML EGISLAGMTE VPIVVVACQR
VGPSTGLPTK HEQSDLFTLY YGGHGEYPSI ILAPSTVEEC FYDTIRAFNL AEEYQCPVIV
LSDLSLSLSP QTVDPLDYDQ VVIQRGAMVT MDTLNHTETN DFKRFAFTEN GISPRSIPGM
KNGSHHVTGV EHSENGIPND NEKNRKKMME KRMGKTAPLS LGSEIKIIHN NRRSTLFLTM
GSNFGIVKEA VESCGNQVDY GAITMIRPLP RKQLLEVFEK YDRVVIVENN YEGQLAAIIK
QEIGYHHKID QFLKYDGSPF TLESLRDKIG GEA
//
