ID A0A2A5X2A0_9GAMM Unreviewed; 553 AA.
AC A0A2A5X2A0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:PDH42534.1};
GN ORFNames=CNF00_02260 {ECO:0000313|EMBL:PDH42534.1};
OS Candidatus Thioglobus sp. MED-G25.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus.
OX NCBI_TaxID=1986229 {ECO:0000313|EMBL:PDH42534.1, ECO:0000313|Proteomes:UP000219647};
RN [1] {ECO:0000313|EMBL:PDH42534.1, ECO:0000313|Proteomes:UP000219647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED-G25 {ECO:0000313|EMBL:PDH42534.1};
RA Haro-Moreno J.M., Lopez-Perez M., De La Torre J., Picazo A., Camacho A.,
RA Rodriguez-Valera F.;
RT "Fine stratification of microbial communities through a metagenomic profile
RT of the photic zone.";
RL Submitted (AUG-2017) 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:PDH42534.1}.
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DR EMBL; NTKC01000004; PDH42534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5X2A0; -.
DR Proteomes; UP000219647; 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 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 387..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 553 AA; 59974 MW; 1C2F906AD02A20BA CRC64;
MEINRTGGQL LIEALRQQGT DHVFCVPGES FLSALDGLHG MESIRTVICR QEGGAAMMAD
AYGKLTHRPG VCFVSRGPGA SNAASGIHIA SQDSTPLVMF VGQIERSTIG REAFQEIDYR
AMFGYAAKRV EQIEDVDRIP EVVSRAFHTA VNGRAGPVVV ALPEDMLRDT TTAQPVALFR
RIEPAPGAAA VAEFEERLKA ARKPIMIVGG RGWRPDTKEK IQQFSEDWDL RLVAGFRFQD
CVDNDHDHYI GELGLGTNPV LTDAIQAADL LIVLGVRLGE LTTAGYTLID IPVPRQQLVH
IYPGMEELGS VYYPTLAINA SVNQFANVLP DLGGRPADPP WSALRKQGRQ AYLDWTKPVF
SPGRVNLSEV ICSLNDFLPD DAIIANGAGN YTAWVHRFYR YRTLGSQLAP TAGSMGYGLP
AAVAAKLVQP HRPAIVFAGD GCFMMTGQEL ATAVQYQLSV VIVVVNNGMF GTIRMHQERR
FPGRVIGTEL VNPDFCALAQ AYGAHAERVE ETAAFLPALR RALDISGPAL IELIVDPEAI
TPARTLSDLT AGG
//
