ID J7QTH7_METSZ Unreviewed; 595 AA.
AC J7QTH7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Thiamine pyrophosphate enzyme TPP binding domain protein {ECO:0000313|EMBL:CCJ08923.1};
GN OrderedLocusNames=BN69_3472 {ECO:0000313|EMBL:CCJ08923.1};
OS Methylocystis sp. (strain SC2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylocystaceae; Methylocystis.
OX NCBI_TaxID=187303 {ECO:0000313|EMBL:CCJ08923.1, ECO:0000313|Proteomes:UP000005263};
RN [1] {ECO:0000313|EMBL:CCJ08923.1, ECO:0000313|Proteomes:UP000005263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:CCJ08923.1,
RC ECO:0000313|Proteomes:UP000005263};
RX PubMed=23045511; DOI=10.1128/JB.01446-12;
RA Dam B., Dam S., Kube M., Reinhardt R., Liesack W.;
RT "Complete Genome Sequence of Methylocystis sp. Strain SC2, an Aerobic
RT Methanotroph with High-Affinity Methane Oxidation Potential.";
RL J. Bacteriol. 194:6008-6009(2012).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; HE956757; CCJ08923.1; -; Genomic_DNA.
DR RefSeq; WP_014892949.1; NC_018485.1.
DR AlphaFoldDB; J7QTH7; -.
DR STRING; 187303.BN69_3472; -.
DR KEGG; msc:BN69_3472; -.
DR PATRIC; fig|187303.17.peg.3748; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_5; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000005263; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 387..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 595 AA; 65126 MW; A7BB3D0CC0F18702 CRC64;
MSGTVGDFFV RRLHEWGVRR IFGYPGDGIN GVLGALQRAK GKIEFIQVRH EEMAAFMASA
HAKFTGELGV CLSTGGPGAA HLITGLYDAK CDHMPVLAIS GQAPRTARGS HYQQELNLDR
MFSDVAAFVQ EAETPSQVRM LTDRAIRIAK AEHAVSVIIF PADLQDLEYE EPPREHGSVR
TGVGYSRPVI VPRHKDLLRA AEVLNAGRKV AVLIGAGALG ASKQVVEVAE KLKAGVAKAL
LGKAALPDAL PWVTGSIGLL GTKPSYDLMM ECDTLLMIGS GFPYSEFLPR EGQARGVQID
IDPSMLSIRF PMEVNLHGDA AATLEALLPL IEEKSHFGWR DRIEKDVRDW WELMEQRAMA
PARPINPQLV AWDLSPRLPD GAIITSDSGS CANWYARDLK IRPGMMCSLS GGLASMGAAV
PYAIAAKLAH PERPVISLVG DGAMQMNNMA ELITVAKYWR EWSNPSWICC VFNNEDLNQV
TWEQRVMEGN PKFEATQNIP DVPYHRFAEL IGLKGIFVDD PDRLAAAWEE ALSCDRPVVL
EVKTDPEVPP LPAHISFEQA RNFATTLFKG DPEQSRLIQG TARQVLASVL PGGEE
//
