ID N1V192_9MICC Unreviewed; 582 AA.
AC N1V192;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:EMY33832.1};
GN ORFNames=D477_012725 {ECO:0000313|EMBL:EMY33832.1};
OS Arthrobacter crystallopoietes BAB-32.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1246476 {ECO:0000313|EMBL:EMY33832.1, ECO:0000313|Proteomes:UP000010729};
RN [1] {ECO:0000313|EMBL:EMY33832.1, ECO:0000313|Proteomes:UP000010729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-32 {ECO:0000313|EMBL:EMY33832.1,
RC ECO:0000313|Proteomes:UP000010729};
RX PubMed=23833141;
RA Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Desai S.M., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of Arthrobacter crystallopoietes Strain BAB-32,
RT Revealing Genes for Bioremediation.";
RL Genome Announc. 1:e00452-13(2013).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMY33832.1}.
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DR EMBL; ANPE02000150; EMY33832.1; -; Genomic_DNA.
DR RefSeq; WP_005269591.1; NZ_ANPE02000150.1.
DR AlphaFoldDB; N1V192; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000010729; Unassembled WGS sequence.
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:EMY33832.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010729};
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..531
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 582 AA; 61740 MW; 58525C8E77109073 CRC64;
MAQELASQLI DQLVSAGVRR IYGIVGDSLN PIVDAVRKTG GSAKGGIDWI HVRHEEAAAF
AAAADAQLTG ELAVCAGSCG PGNLHLINGL YDANRSGSPV LAIASHIPSK QIGTGYFQET
HPDRLFTECS VYSEMVSTAE QAPRVMHSAI QHAWGRRGVA VVSLPGDIAS LDAVAPTPVC
TPFLPASVVP DPRSVEQLAK AINDAGKVAI FAGAGVAGAH DEVVALAELI GAPIGHSLRG
KDFIQYDNPY DIGMTGLLGY GAAAEGIEDA DLLLLLGTDF PYDQFLPETR TAQVDRAAEH
LGRRTDVDLA VHGDVLPTLT ALMPLLKRKK SRRFLDQMLK KHDKLMNKAV GAYTRKADKL
KPIHPEYAAS VLDQTAAADA IFTADTGMCN VWTARYINPL GTRRLIGSYL HGSMANALPH
AIGAQFAHPR RQVISVSGDG GLAMLLGEML TAVTYKLPLN IVLFNNSTLG MVKLEMLVDG
LPDFGVDVPD TNYAAIASAM GFHAVRITEP SELEGAYRAA FAHRGPSLVE VITDPKALSL
PPKITGEQVF GFATAMSKLV LNKGAGEAVS MARSNLRNIP RS
//