ID N1MME8_9SPHN Unreviewed; 594 AA.
AC N1MME8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=COG0028: Thiamine pyrophosphate-requiring enzymes {ECO:0000313|EMBL:CCW17914.1};
GN ORFNames=EBBID32_22630 {ECO:0000313|EMBL:CCW17914.1};
OS Sphingobium indicum BiD32.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1301087 {ECO:0000313|EMBL:CCW17914.1, ECO:0000313|Proteomes:UP000013201};
RN [1] {ECO:0000313|EMBL:CCW17914.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW17914.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Le V.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW17914.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW17914.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Nielsen J.L., Zhou N.A., Kjeldal H.;
RT "Bisphenol A degrading Sphingobium sp. strain BiD32.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:CCW17914.1}.
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DR EMBL; CAVK010000108; CCW17914.1; -; Genomic_DNA.
DR RefSeq; WP_006956693.1; NZ_CAVK010000108.1.
DR AlphaFoldDB; N1MME8; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000013201; 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; cd07035; TPP_PYR_POX_like; 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; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000013201};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 24..136
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 212..347
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 425..568
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 594 AA; 64764 MW; 1F18CD8624C31E69 CRC64;
MSYDDPKPAA AASASDKSGT PVYKRVLDLF EAEGINTLFG IPDPNFVHMF LEAERRGWTV
VAPHHEAAAG FMAEAASRIT GKPAVAVGTL GPGIANMAPA IQCALVEHSP VIFLSGQRAR
VTEQRVRRGR IQFVKQMPLF ENSVKYAASI EYADQTDEVI RESIRKAMGG TPGPVYIEYP
SHIILEELDL PAPLVPERYR LVNQGADIDR VHEAAKLIRE AKNPILLVGH GVHTSRTGAA
VRELAELMNC PVIQTSGGTS YIKGLEDRTF QYVFSKASIE AVTESDLVLA LGTELGEPVH
FGKWRYWQKN EAIRKWIYVE QDASAIGVNR PIDVPLVGDL RGVVPQLVTA LKDTPRAPAP
MLAAFMRDGQ AELEELAAES RTKSDGTGEL AIHPARLAVE ATEAFPKDGI MIRDGGAGVI
FQWTYSQCKP HDVIWNQNFG HIGTGIPYAT GAMLADKAAT GVSRPAMLLT SDSSFLFHIG
ELEVAARCKL PLVCVVGVDN AWGLEVGVYK RTFGQGTEET GTHWSKDVRF DKIGEGFGCH
GEYVTKAEDI KPAIERAYAS GKVGVVHVVI DPKANSEEMP KYAEFRTWYA EGTQ
//
