ID Q1LHV8_CUPMC Unreviewed; 1197 AA.
AC Q1LHV8;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000313|EMBL:ABF10268.1};
DE EC=1.2.7.8 {ECO:0000313|EMBL:ABF10268.1};
GN Name=porG {ECO:0000313|EMBL:ABF10268.1};
GN OrderedLocusNames=Rmet_3396 {ECO:0000313|EMBL:ABF10268.1};
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF10268.1, ECO:0000313|Proteomes:UP000002429};
RN [1] {ECO:0000313|Proteomes:UP000002429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC {ECO:0000313|Proteomes:UP000002429};
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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DR EMBL; CP000352; ABF10268.1; -; Genomic_DNA.
DR RefSeq; WP_011517831.1; NC_007973.1.
DR AlphaFoldDB; Q1LHV8; -.
DR STRING; 266264.Rmet_3396; -.
DR KEGG; rme:Rmet_3396; -.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG4231; Bacteria.
DR HOGENOM; CLU_009166_1_0_4; -.
DR Proteomes; UP000002429; Chromosome.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02008; TPP_IOR_alpha; 1.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR046667; DUF6537.
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 PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR Pfam; PF20169; DUF6537; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABF10268.1}; Pyruvate {ECO:0000313|EMBL:ABF10268.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002429}.
FT DOMAIN 481..628
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 754..940
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 976..1181
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1197 AA; 130759 MW; 41355A27330EB475 CRC64;
MNAPLTPPVS DAIRRALENV SLEDKYTLER GRIYISGTQA LVRLPMLQQE RDRASGLNTA
GFISGYRGSP LGALDQSLWK AKKHLAAHNV VFQAGLNEDL AATSVWGSQQ VNMYPDAKFD
GVFGMWYGKG PGVDRTGDVF KHANSAGSSR HGGVLVLAGD DHSAKSSTLA HQSEHIFKAC
GLPVLYPSNV QEYLDYGLHG WAMSRYSGLW VAMKCVTDVV ESSASVELDP HRVRIVLPDD
FALPQGGLNI RWPDPPLEQE ARLLDYKWYA GLAYVRANKI DRIEIDSPHA RFGIMTAGKA
YLDTRQALSD LGLDDETCAR IGIRLYKVGC VWPLEAHGAR AFAEGLHEIL VVEEKRQIME
YALKEELYNW RDDVRPKVYG KFDEKDNAGG EWSIPQNNWL LPAHYELSPA IIAKAIATRL
EKFDLPSDIR ARIEARLALI QAKEKALATP RVTAERKPWF CSGCPHNTST NVPEGSRALA
GIGCHYMTVW MDRNTSTFSQ MGGEGVAWIG QAPFAGDNHV FANLGDGTYF HSGLLAIRAS
ISAGVNITYK ILYNDAVAMT GGQPVDGQLS VQDIAFQVAA EGARKIVIVT DQPEKYNSAI
KLPEGLTVHP REELDNIQRE LREVPGCTIL IYDQTCATEK RRRRKRGTFP DPARRAFIND
AVCEGCGDCS VKSNCLSVEP LETELGTKRQ INQSSCNKDF SCVNGFCPSF VTAEGAQVRK
PQATGMSMGG LPALPEPVLP TMRRSYGILV TGVGGTGVVT IGGLLGMAAH LENKGVTVLD
MAGLAQKGGA VLSHVQIAAK PDDLHATRIA MGEADLVIGC DAIVSATDEV ISKTQTGRTR
AVVNTAQTPT AAFIKDPKWQ FPGLSAEQDI RNAVGEACDF INASALAVAL LGDAIYTNPL
VLGYAWQKGW IPLSLEALVR AIELNGVSVD KNKAAFDWGR HMAHDPDHVL SLTGKLKTQT
EGADVVKLPT SSGALLEKLI TNRVDLLTKY QNAAYAEQYR DAVNRVRAAE SALVGAGKPL
PLTEAAARNL AKLMAYKDEY EVARLYTDPI FLDKLRAQFE GEPGRDYQLN FWLAPPTTAK
RDDKGHLVKR RFGPSTMTLF RMLAKLKGLR GGPLDIFGKT EERRTERALI GEYRSLLDEL
SKGLSAANHD TAVALANVPD DIRGFGHVKE NNLKAARGRW EKLLAQFRNP QAGQQAA
//
