ID J9S4U3_9ACTN Unreviewed; 1191 AA.
AC J9S4U3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase, alpha and beta subunits {ECO:0000313|EMBL:AFR47910.1};
GN ORFNames=KTR9_1270 {ECO:0000313|EMBL:AFR47910.1};
OS Gordonia sp. KTR9.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR47910.1, ECO:0000313|Proteomes:UP000003281};
RN [1] {ECO:0000313|EMBL:AFR47910.1, ECO:0000313|Proteomes:UP000003281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTR9 {ECO:0000313|EMBL:AFR47910.1,
RC ECO:0000313|Proteomes:UP000003281};
RX PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA Indest K.J., Eltis L.D.;
RT "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL Appl. Environ. Microbiol. 78:7798-7800(2012).
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DR EMBL; CP002907; AFR47910.1; -; Genomic_DNA.
DR RefSeq; WP_014925852.1; NC_018581.1.
DR AlphaFoldDB; J9S4U3; -.
DR STRING; 337191.KTR9_1270; -.
DR KEGG; gor:KTR9_1270; -.
DR PATRIC; fig|337191.3.peg.1499; -.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG4231; Bacteria.
DR HOGENOM; CLU_009166_1_0_11; -.
DR Proteomes; UP000003281; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
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; -; 2.
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 Pyruvate {ECO:0000313|EMBL:AFR47910.1}.
FT DOMAIN 484..634
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 758..944
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 987..1182
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1191 AA; 128497 MW; 10FE969F6D035FEC CRC64;
MTLADDRARF EHVPTPDQRP TEAAVAGFSL DDRYTRDAGD IYLTGIQALV RMVRDRARVD
RRSGLQTASF ISGYEGSPLA GYDLELARRR EYLAPYDIIH RPGLNEELAA TSVMGSQLAA
QVTAGSVLSP SADGLPRDGV VGYWYGKAPG LDRATDALRH ANLIGTHSAG GAVALVGDDP
GAKSSTVPCA SEMALADLYI PILYPADSQD ILDLGVHAAI MSRTSGLWTS LKISAHVADG
ASTAHVDPDR IVPVFGELGT SPHVPSGRLL GANLMELEQN QLTTRLPRAQ EYARLNGLNR
IVVSSPDDRI GIVAAGKTYL DLREALRLLH IDDDDLRRLG IRILKLGMVY PIEREILNRF
MFDTATGDLD EVIVIEEKRD FIETMMRDIL FRHPRAPRIV GKVHEDGSTL FSRFGELDVD
AVTRGLADRL ARHGVDAAQI WLDRKAARRT RIELPLAVRT PYFCSGCPHN SSTKVAENTL
VGAGIGCHAM VLLMDPRQVG DIAGVTQMGG EGAQWIGMAP FVPADHFVQN VGDGTFMHSG
SLALRAAVAS GENITYKLLY NGTVAMTGGQ DPVGAMTLPR LTSLLLDEGV ARIVITSDDP
KHARTLGLPE QIQIRHRDDL LEVQTELAAV PGVTVLVHDQ HCAAEKRRKR KRGTVPTPTR
RVMINERICE GCGDCGEKSN CLSVHPVQTE FGRKTTIDQS SCNLDFSCLQ GDCPSFVTVT
PGADRIRTRA ADLAESALPA PAVPTLRDTF SLRITGVGGT GVVTVSQVLA TAAVLDGHSA
RTVDMTGLAQ KGGAVVSDIK VAPRPLEQAA KVASEDCDLY LVCDPLVGTD PVNLKVAAPE
KTVAVVSTTQ VPTGLMVIDT SVGFPSDSAV HSAIDDRVTR AVYLDSGALS TALFGDEQYA
NMVMAGAAYQ AGALAIPASS IERAIALNGV AVDANVQAFR RGRQIVSDPD SVTATIDGLH
GRGVAEIEPS GHALEVVAGL GSIDDELRRT IAIRYDELTA HSDERYARTY LDAVGRVHRT
APDAALTGAV ARNLYKLMAY KDEYEVARLT QDPSFAARIA DEFGADAEVA VRLHPPTLRS
MGMRQKLALG SWADTPLKAL ATMKRLRGTR LDPFGRSEIR RTERELIVEY RELVDAVVDA
FASRRIGEAQ VPAAIELVEL PDMVRGYESI KMRNVERYRA ELGRQRAALE V
//
