ID R4MKC9_MYCTX Unreviewed; 653 AA.
AC R4MKC9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Oxidoreductase alpha subunit {ECO:0000313|EMBL:AGL27907.1};
GN ORFNames=J113_17060 {ECO:0000313|EMBL:AGL27907.1};
OS Mycobacterium tuberculosis CAS/NITR204.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1310114 {ECO:0000313|EMBL:AGL27907.1, ECO:0000313|Proteomes:UP000013548};
RN [1] {ECO:0000313|EMBL:AGL27907.1, ECO:0000313|Proteomes:UP000013548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAS/NITR204 {ECO:0000313|EMBL:AGL27907.1,
RC ECO:0000313|Proteomes:UP000013548};
RX PubMed=23788533;
RA Narayanan S., Deshpande U.;
RT "Whole-Genome Sequences of Four Clinical Isolates of Mycobacterium
RT tuberculosis from Tamil Nadu, South India.";
RL Genome Announc. 1:e00186-13(2013).
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DR EMBL; CP005386; AGL27907.1; -; Genomic_DNA.
DR AlphaFoldDB; R4MKC9; -.
DR SMR; R4MKC9; -.
DR KEGG; mtuc:J113_17060; -.
DR PATRIC; fig|1310114.3.peg.3602; -.
DR HOGENOM; CLU_017038_1_0_11; -.
DR BioCyc; MTUB1310114:G13A2-2477-MONOMER; -.
DR Proteomes; UP000013548; 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 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}.
FT DOMAIN 38..225
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 269..486
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 526..612
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 653 AA; 69182 MW; B15D0DF492C2DBC5 CRC64;
MDPNGSGAGP ESHDAAFHAA PDRQRLENVV IRFAGDSGDG MQLTGDRFTS EAALFGNDLA
TQPNYPAEIR APAGTLPGVS SFQIQIADYD ILTAGDRPDV LVAMNPAALK ANIGDLPLGG
MVIVNSDEFT KRNLTKVGYV TNPLESGELS DYVVHTVAMT TLTLGAVEAI GASKKDGQRA
KNMFALGLLS WMYGRELEHS EAFIREKFAR KPEIAEANVL ALKAGWNYGE TTEAFGTTYE
IPPATLPPGE YRQISGNTAL AYGIVVAGQL AGLPVVLGSY PITPASDILH ELSKHKNFNV
VTFQAEDEIG GICAALGAAY GGALGVTSTS GPGISLKSEA LGLGVMTELP LLVIDVQRGG
PSTGLPTKTE QADLLQALYG RNGESPVAVL APRSPADCFE TALEAVRIAV SYHTPVILLS
DGAIANGSEP WRIPDVNALP PIKHTFAKPG EPFQPYARDR ETLARQFAIP GTPGLEHRIG
GLEAANGSGD ISYEPTNHDL MVRLRQAKID GIHVPDLEVD DPTGDAELLL IGWGSSYGPI
GEACRRARRR GTKVAHAHLR YLNPFPANLG EVLRRYPKVV APELNLGQLA QVLRGKYLVD
VQSVTKVKGV SFLADEIGRF IRAALAGRLA ELEQDKTLVA RLSAATAGAG ANG
//
