ID A0A1I5QGS0_9SPHN Unreviewed; 596 AA.
AC A0A1I5QGS0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Pyruvate dehydrogenase (Quinone) {ECO:0000313|EMBL:SFP45241.1};
GN ORFNames=SAMN04488241_10219 {ECO:0000313|EMBL:SFP45241.1};
OS Sphingomonas rubra.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=634430 {ECO:0000313|EMBL:SFP45241.1, ECO:0000313|Proteomes:UP000199586};
RN [1] {ECO:0000313|EMBL:SFP45241.1, ECO:0000313|Proteomes:UP000199586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9113 {ECO:0000313|EMBL:SFP45241.1,
RC ECO:0000313|Proteomes:UP000199586};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; FOXP01000002; SFP45241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5QGS0; -.
DR STRING; 634430.SAMN04488241_10219; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000199586; 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:SFP45241.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199586};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..330
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..545
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 596 AA; 64371 MW; E92AD834E1DEFDFA CRC64;
MTRLTSDFFV ERLKTWGVTR IYGYSGDGIN GVLGALQRAE GTEGEIEFVQ VRHEEMAAFM
ATAHAKFTGE LGVCLSTGGP GATHLITGLY DAKSDHMPVL AIAGQAETTV RGASYQQELN
LDRMFADVAD FVQEAAAPAQ LRHLVDRGLR VAKARNGVTV LILPKDVQDE AWEEPKRAHG
FTRSGPGYSA PRVLPHDADL RRAAEVLNAG RKVAILIGAG AREAADEVVA VAERLGAGVA
KALLGKDVLP DDLPFVTGAI GLLGTKPSSD MMDDCDTLLM IGTGFPWAEF LPADGQARAV
QIDIAPEMLG LRYPAEVNLH GDAGETLRAL LPLLDHQQDR GWQDGIAAAM DDWRETLKGR
ALADASPVNP QRVVHEMSPR LPADAIVTSD SGSCANWYAR DWQMKRGQRG SLSGGLASMG
AAVPYAIAAK FAHPTRPVVA LVGDGAMQMN NMAELITIQK YWRRWADPRL VVCVFNNEDL
NEVTWEQRIM EGNPRFATTQ SLPDVPYARF AEMVGLTGIF VDDPAALGDA WDRALSADRP
VVLEVKTDPN VAPLPPHVTM EQAKAFMTSM AKGDRGAMQV VADTARQIIG GVRERL
//
