ID G0J6M4_CYCMS Unreviewed; 546 AA.
AC G0J6M4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Thiamine pyrophosphate TPP-binding domain-containing protein {ECO:0000313|EMBL:AEL28539.1};
GN OrderedLocusNames=Cycma_4854 {ECO:0000313|EMBL:AEL28539.1};
OS Cyclobacterium marinum (strain ATCC 25205 / DSM 745 / LMG 13164 / NCIMB
OS 1802) (Flectobacillus marinus).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=880070 {ECO:0000313|EMBL:AEL28539.1, ECO:0000313|Proteomes:UP000001635};
RN [1] {ECO:0000313|Proteomes:UP000001635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25205 / DSM 745 / LMG 13164 / NCIMB 1802
RC {ECO:0000313|Proteomes:UP000001635};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Cyclobacterium marinum DSM 745.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP002955; AEL28539.1; -; Genomic_DNA.
DR RefSeq; WP_014022819.1; NC_015914.1.
DR AlphaFoldDB; G0J6M4; -.
DR STRING; 880070.Cycma_4854; -.
DR KEGG; cmr:Cycma_4854; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_2_10; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000001635; 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 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:SF129; 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:UP000001635};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 186..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 378..523
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 546 AA; 60765 MW; 49DF26EB1E22AAD0 CRC64;
MKASDLFVKA LEKEGVEYIF GLPGEENLDI LESLTRSKIK LILTRHEQGA GFMAATYGRL
TGKPGVCMST LGPGATNLFT PGAYAQLGAM PMLMITGQKP IKKSKQARFQ IIDVVDMMRP
ITKYTKQIVD GNVIASNVRE AFRKATEERP GAVHLELPED IAQENVEDHV FEVVDYMLPK
SDDEAIRAAA KMIGNAKMPL LLIGAGANRK VTCQALASFV DTTGIYFFTT QMGKGVIDER
HPKYLGTAAL SSHDFVHAAI DESDLIINVG HDVIEKPPFF MKQGGKKVIH VNFSPAEVDP
VYFPQLNVVG DITDSVEKLA KAIKPSESWN FDFYKKVKTE VSEHLGKYFE DERFPTLPQR
LVNLLRNKLG EKDVITLDNG VYKIWFARNY TCYHPNTLLL DNALATMGAG LPSAMCVNLL
YPDKKVVAIC GDGGFMMNSQ ELETAVRLGL NMVVIILNDE SYGMIKWKQE DMGFKDFGLD
FKNPDFVQYA NSYGAHGYRP ESDKDLQEIL DKSLNSSGVH VIDLKVDYSL NHPILNVMLK
EKTSKL
//
