ID A0JSG9_ARTS2 Unreviewed; 582 AA.
AC A0JSG9;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Pyruvate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:ABK01989.1};
GN OrderedLocusNames=Arth_0590 {ECO:0000313|EMBL:ABK01989.1};
OS Arthrobacter sp. (strain FB24).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=290399 {ECO:0000313|EMBL:ABK01989.1, ECO:0000313|Proteomes:UP000000754};
RN [1] {ECO:0000313|Proteomes:UP000000754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB24 {ECO:0000313|Proteomes:UP000000754};
RX PubMed=24501649; DOI=10.4056/sigs.4438185;
RA Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL Stand. Genomic Sci. 9:106-116(2013).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP000454; ABK01989.1; -; Genomic_DNA.
DR RefSeq; WP_011690457.1; NC_008541.1.
DR AlphaFoldDB; A0JSG9; -.
DR STRING; 290399.Arth_0590; -.
DR KEGG; art:Arth_0590; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_11; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000000754; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR047211; POXB-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Pyruvate {ECO:0000313|EMBL:ABK01989.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000754};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 385..530
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 582 AA; 61648 MW; EFF99FA096E5C805 CRC64;
MAKELASQLI EQLQAAGVQR IYGIVGDSLN PIVDAVRKTG GSQQGGIDWI HVRHEEAAAF
AAAAEAQLTG RLAVCAGSCG PGNLHLINGL YDANRSGAPV LAIASHIPSK QIGSGYFQET
HPDRLFNECS VYSELVSTAE QAPRVMHSAI QHAVGLGGVA VVTLPGDIAG LEATGRTPLP
ATFRRATLTP DAASVRELAD AINAAEKIAI FAGAGTQGAH DEVVALAELI GAPIGHSLRG
KDFMQYDNPY DIGMTGLLGY GAAAEGIEDA DLLILLGTDF PYDQFLPGTR TAQVDRAAHK
LGRRTDVDIA VHGDVLPTLG ALKPLLARKK NRRFLNQMLK KHDRLMNKAV GAYTRKVEKK
QPIHPEYAAS ILDQVAAENA IFTADTGMCN VWTARYINPL GTRRLIGSYL HGSMANALPH
AIGAQLAYPG RQVISVSGDG GLSMLLGELI TVAAHRLPVN VVVFNNSTLG MVKLEMLVDG
LPDFGVDVPD ADYAAVARAL GFHAVRVTDP ARIEDAYREA FAHPGPSLVE LITDPKALSI
PPKITGSQVL GFATAMSKVV LNRGAGEAVS MARSNLRNIP RR
//
