ID K9AK10_9MICO Unreviewed; 574 AA.
AC K9AK10;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Thiamine pyrophosphate TPP-binding domain-containing protein {ECO:0000313|EMBL:EKU47639.1};
GN ORFNames=C272_07847 {ECO:0000313|EMBL:EKU47639.1};
OS Brevibacterium casei S18.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=1229781 {ECO:0000313|EMBL:EKU47639.1, ECO:0000313|Proteomes:UP000009879};
RN [1] {ECO:0000313|EMBL:EKU47639.1, ECO:0000313|Proteomes:UP000009879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S18 {ECO:0000313|EMBL:EKU47639.1,
RC ECO:0000313|Proteomes:UP000009879};
RA Sharma R., Singh A., Jangir P.K.;
RT "Genome Sequence of Brevibacterium casei S18.";
RL Submitted (SEP-2012) 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:EKU47639.1}.
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DR EMBL; AMSP01000005; EKU47639.1; -; Genomic_DNA.
DR AlphaFoldDB; K9AK10; -.
DR PATRIC; fig|1229781.4.peg.1574; -.
DR eggNOG; COG0028; Bacteria.
DR Proteomes; UP000009879; 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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000009879};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 2..111
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 187..316
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 378..526
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 574 AA; 61921 MW; DD7A19A24DB423D3 CRC64;
MADDLWGMLI DAGVERVYGI VGDALNPTID SLSRHPQIEF IHVRHEEWGA FAASADAQLS
AGPVVVCGTA GPGVTHLLNG LLDALHEQAP VIAIAGDVET SIIDTDAVEE ISPYDLFRTA
SLYTGRVVSP EQSRAVFQQA ITIATEDLGP TVIALPGDVA SAKSPLDAPP KYTPSRRSVL
TPRDEDVRAV ADLINSREKI FLFGGNGTEH AADLVQELSD KVSAPVGYTL KGKNWLEAGN
PNAVGMTGLL GYGAANDCIK HADVMVMLGA DFPFPGFLDR GHAKVVLVDN LASHLGRRVA
LEMGVPADVR AFLEKLLPLV ERKSDDEFLR TAQKTTEGWT KRLRHYVDGG EKRSPIRPEY
LASLLDELID EDAIVTADTG TSVIWVAHQM SFGGDRIQLG SYSWASMADA SPYAFGATKA
VPGRQVIAFC GDGGFSMLGL GDLLTERQHR SPIVHVVLNN EELDFVNIEQ QEAGFRPWGT
GFPAANYAAI AEGFGVKGIR CEDPARLRDQ LTEALAHRDG PVVVDVVVDK RALALPSTVD
AELVGKFTLS VFKRALHGEI PELWEEAKDN IRLL
//