ID I0I905_CALAS Unreviewed; 581 AA.
AC I0I905;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Putative TPP binding protein {ECO:0000313|EMBL:BAM01743.1};
GN OrderedLocusNames=CLDAP_37030 {ECO:0000313|EMBL:BAM01743.1};
OS Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS STL-6-O1).
OC Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC Caldilinea.
OX NCBI_TaxID=926550 {ECO:0000313|EMBL:BAM01743.1, ECO:0000313|Proteomes:UP000007880};
RN [1] {ECO:0000313|EMBL:BAM01743.1, ECO:0000313|Proteomes:UP000007880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1
RC {ECO:0000313|Proteomes:UP000007880};
RA Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA Hanada S., Yamazaki S., Fujita N.;
RT "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT 102666).";
RL Submitted (FEB-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}.
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DR EMBL; AP012337; BAM01743.1; -; Genomic_DNA.
DR RefSeq; WP_014434966.1; NC_017079.1.
DR AlphaFoldDB; I0I905; -.
DR STRING; 926550.CLDAP_37030; -.
DR KEGG; cap:CLDAP_37030; -.
DR PATRIC; fig|926550.5.peg.3986; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_3_0; -.
DR OMA; DIGSHYI; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000007880; 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; cd02004; TPP_BZL_OCoD_HPCL; 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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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 Reference proteome {ECO:0000313|Proteomes:UP000007880};
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 222..350
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 419..567
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 581 AA; 62004 MW; EE3F20EA003E66F5 CRC64;
MHSGDRVAEV LKAQGVELLF TLVGGHISPI LVGAKQRGIR VIDTRHEATA VFAADAVARL
TGRPGVAAVT AGPGVTNTIT ALKNAQMAQS PVVVIGGAAP TALQGRGALQ DIDQMAVVRP
VVKWAKQVKR VKALIPTLEE AFHVAQSGVP GPVFVECPVD LLYDEATVRS WYGADRGGKS
LADKALKQYL RFHVNRLFSG ADAVHPGPRI EAAPPAPDPA AVQKVAERLL AAQRPLLLIG
SQAMLDAGRA HELAGALEAI AAPVYLSGMA RGLLGRDHPL QMRHKRREAL READFVLLAG
VPCDFRLDYG NHIRRSAVYV SINRSREDLT KNRRPTLALL ADPALTLRML AATLSTLRPQ
AWNKQAWDEW TAHLRARDDA RNAEIAAQAL APTGKVNPLH LCMEIDRQIT PNSILIGDGG
DFVATASYVI QPPGPLRWLD PGAFGTLGVG AGFALGAKLV HPTADVWVLY GDGSFGYSVA
EFDTFVRHGL PVIAVIGNDA SWSQIAREQV ELLGDPVATE LAHSDYERAV EGFGAAGVRL
DDPELAAEAI EQARETAAAG KPTVLNVLLG KTDFRKGSIS M
//