ID A0A291P2I0_9GAMM Unreviewed; 544 AA.
AC A0A291P2I0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Thiamine pyrophosphate-requiring enzyme {ECO:0000313|EMBL:ATJ81075.1};
GN ORFNames=BEI_0088 {ECO:0000313|EMBL:ATJ81075.1};
OS Halomonas beimenensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=475662 {ECO:0000313|EMBL:ATJ81075.1, ECO:0000313|Proteomes:UP000219993};
RN [1] {ECO:0000313|EMBL:ATJ81075.1, ECO:0000313|Proteomes:UP000219993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTU-111 {ECO:0000313|EMBL:ATJ81075.1,
RC ECO:0000313|Proteomes:UP000219993};
RX PubMed=29026163;
RA Chen Y.H., Lin S.S., Shyu Y.T.;
RT "Revealing the Saline Adaptation Strategies of the Halophilic Bacterium
RT Halomonas beimenensis through High-throughput Omics and Transposon
RT Mutagenesis Approaches.";
RL Sci. Rep. 7:13037-13037(2017).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP021435; ATJ81075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291P2I0; -.
DR KEGG; hbe:BEI_0088; -.
DR OrthoDB; 8664451at2; -.
DR Proteomes; UP000219993; 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 GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF142; ACETOLACTATE SYNTHASE; 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:UP000219993};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 385..525
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 544 AA; 57378 MW; 14A56DEC3C658B56 CRC64;
MTTITVGEAV ARTLEAYAVS AVYGVISIHN LPIADAIGQR ERVRFVPSRG EAGAVTMADG
HTRVGGLGVA LTSTGAGAGN AVGAMLEALN AGTPLLHITG QVEKAYLDRD AGFIHETRDQ
MGFLQACSKR AYRACTPEQV VPLLHRAIQE AMTLPRGPVS LEIPIDIQAS SVEWVETAPA
EPAAPARVGE AEIDALAERV LAAERPVLWI GGGCLEAGDA VRRLADAGIP VVSSTHARGV
LPDSHPRSLR AFHSAPAVEE LFGRSDLMLV AGSRLRSNET RTYSVALPRP LVQIDVDPAA
AHRNYSADAF LCGECGDVLA RLADRLEGKR SPDAEVDRDV AQAVEAAEQA LRGQVGEYAK
LSDAIRAALP EDGIFVRDIT VSGSTWGSRL LPIERPLTNI HSLAGAIGQG LATGIGCAVG
AAGRKVVTVV GDGGLMLMVG EMATLAQERA DMTLVVMNDG GYGVMRGIQD KYFEGRQYYN
DLHTPDFQAM ADALGLPRWK VSRGDDFQAV LAEAVGQDGP AVVEVDMASV GELKFAGPPQ
KTLY
//
