ID A0A3T0MXS3_9RHOB Unreviewed; 540 AA.
AC A0A3T0MXS3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:AZV76557.1};
GN ORFNames=EBB79_00710 {ECO:0000313|EMBL:AZV76557.1};
OS Parasedimentitalea marina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Parasedimentitalea.
OX NCBI_TaxID=2483033 {ECO:0000313|EMBL:AZV76557.1, ECO:0000313|Proteomes:UP000283063};
RN [1] {ECO:0000313|EMBL:AZV76557.1, ECO:0000313|Proteomes:UP000283063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W43 {ECO:0000313|EMBL:AZV76557.1,
RC ECO:0000313|Proteomes:UP000283063};
RA Cao J.;
RT "Parasedimentitalea marina sp. nov., a psychrophilic bacterium isolated
RT from deep seawater of the New Britain Trench.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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}.
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DR EMBL; CP033219; AZV76557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3T0MXS3; -.
DR KEGG; sedi:EBB79_00710; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000283063; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd00568; TPP_enzymes; 1.
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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 540 AA; 57639 MW; 28EFD27451A36F0D CRC64;
MSTKKHVYQT IADAVSDHGV ETMFGLMGDA NLFMVDSFVR DCGGRFVPAA HEGSSVLMAL
AYAHVAGKVG VASVTHGPAL TNCITALTEG VRGHIPMVLL AGDTPVANPR HLQGIDQREL
VKASGAGFEQ LRAPDTVGRD VARAFYRAQV ERRPIVLNMP ADFMWEEANH KTQVLDVFTA
PGGVAEGDTL DEAIGMIASA RRPLILAGGG AVAARDQLIR LADRLEAPLA TTLKAKGLFQ
GHPYNIDIFG TLSTPAAYDL IAKSDCIVCF GTALHDFTTD RGKLMKDKRI VQVDVEPTAI
GGGVHPDAAL VADAGLTAET ILYWLDEAEI AASGFTRELD VDTLTMHPTG SDKTAEGCVN
YVHALEQLET ALPKDRVLVT DGGRFMTEVW CRISAPNPQS FVVTANFGSI GLGLQEAVGA
GLAAPERPVV MFTGDGGFMM GGINEFNTAV RLGLDLIVIV ANDSAYGAEH IQFLDRKMDP
SLTEFHWPSF AGIATSLGGQ GFEVRSSEEL EVALAALTTR KGPVLIELRL DPHDVPRMRI
//
