ID A0A329QSZ2_9ACTN Unreviewed; 589 AA.
AC A0A329QSZ2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Thiamine pyrophosphate-binding protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DPM12_12510 {ECO:0000313|EMBL:RAW13818.1};
OS Phytoactinopolyspora halophila.
OC Bacteria; Actinomycetota; Actinomycetes; Jiangellales; Jiangellaceae;
OC Phytoactinopolyspora.
OX NCBI_TaxID=1981511 {ECO:0000313|EMBL:RAW13818.1, ECO:0000313|Proteomes:UP000250462};
RN [1] {ECO:0000313|EMBL:RAW13818.1, ECO:0000313|Proteomes:UP000250462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 96934 {ECO:0000313|EMBL:RAW13818.1,
RC ECO:0000313|Proteomes:UP000250462};
RA Tang S.-K.;
RT "Phytoactinopolyspora halophila sp. nov., a novel halophilic actinomycete
RT isolated from a saline soil in China.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RAW13818.1}.
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DR EMBL; QMIG01000011; RAW13818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329QSZ2; -.
DR Proteomes; UP000250462; 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; 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: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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000250462};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 31..135
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 234..366
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 446..557
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 62069 MW; 102E938D9FA38F52 CRC64;
MTHISKPAPA SPHQTKGRDM CAEHSPTEHR TVADALVQFL ARAGVTHLFG VAGSTIMPLL
DAVEDDGRIR YVAARYELSA AEMAAGYARA SARLGVVATH VGPGATSCIT AMAGAHRDGV
PLLLITGNEE SDTLARMPYH DWQLLPVMSQ LCAFSYRVTR PDELPHVLRR ALGEALRGGT
GTVHIDLPED IALMPVTDDD LASWSAAIDP VLAQIADAPQ APLSRPAPNS GEVHRAVDLL
ARAHAPVVLL GETSRRGAAA ERILDQCDGL GIPYATTFGA RGGIGSRPGY AGTIGRFGSR
DTTALVGDAD VVLALGAELT DVDTVRWSIP RPDTDVICVH PEPGVIDRRL APTLGVVADV
EEFLHAFGPA YRERAVSVAG SWIDRARLVN RANGPLGDVS GAEATLDAQL VTRMIDAAPD
SWIVTMDPGF GPLTLSASAD FGGSPFIYAH GLGAMGFAVP NAIGATMTGG IDGALAVIGD
GSFFMSLSSL ESIASLDVPV VVLVLDDGGF GSQRKKQQEG YGRNVGVDYD NPDIPQIASA
MRIDATWVES VADIDRLCAD LPARTRGQVL AVRRAQVQHG TWYEGGTRR
//
