ID D4CJV4_9FIRM Unreviewed; 733 AA.
AC D4CJV4;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Thiamine pyrophosphate enzyme, C-terminal TPP binding domain protein {ECO:0000313|EMBL:EFE92730.1};
GN ORFNames=GCWU000341_00622 {ECO:0000313|EMBL:EFE92730.1};
OS Oribacterium sp. oral taxon 078 str. F0262.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Oribacterium.
OX NCBI_TaxID=608534 {ECO:0000313|EMBL:EFE92730.1, ECO:0000313|Proteomes:UP000004602};
RN [1] {ECO:0000313|EMBL:EFE92730.1, ECO:0000313|Proteomes:UP000004602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0262 {ECO:0000313|EMBL:EFE92730.1,
RC ECO:0000313|Proteomes:UP000004602};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) 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:EFE92730.1}.
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DR EMBL; ACIQ02000009; EFE92730.1; -; Genomic_DNA.
DR RefSeq; WP_009214114.1; NZ_GG729933.1.
DR AlphaFoldDB; D4CJV4; -.
DR STRING; 608534.GCWU000341_00622; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_1_3_9; -.
DR Proteomes; UP000004602; 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:SF142; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..108
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 265..400
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 500..683
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 733 AA; 81524 MW; 8543327D55B178FB CRC64;
MRQRLADYIS ETLVANGITQ NFSVTGGGAM HLNDAFGHQR GMHTLYQHHE QACAMAAESY
ARIYNRPALV CVTSGPGGTN AITGVLGAWL DSIPMLVISG QVRRDNTAHW SGRRLRAMGD
QEFEITRAVS CMTKYAELLL DPYRVRYALE KCIYLSQTGR PGPCWLDIPV DVQGCYIETE
ELRGFFRESY ERGEDGWGNA EGKRHSHPET ASSMQRYFTS EEEREEVLRG LSALENPQRL
PEDRGAAREE LPIPPGEELR EAASHILDKL KESRRPVFYT GNGIRIAGAE ADFLKLKDRL
QIPVVVGWNA PDIIPTEDPL YAGRPGGRGD RPGNLCVQNA DCILSIGSRL NIRQVGYRFQ
SWAREAYVML CDIDGEELWK PSLHVDFRVR SDAGDLIRAL LSELDRRKLR RLFSGGEGIL
RRDALMLSHT ESAERIASGG ESERLDWLET TAFYRENYPT VLPEYLRIEG EDGEGANVYA
LVKILSELSE DGQITVVGNG SPCVAGGQAW LVKKDGRFIS QDGVASMGYD LPAAIGACAA
SHGEDAEKWR ENALKNPYWK GRKEQYPDYG KRDILLLTGD GSLQMNLQEL QTIIHHRLPI
KIFVINNGGY HSIRQTQRSF FGEPLVGIGV DSGLGGKSDL SFPDLEKLAK AYGYPFLRIS
DNSGLKEGLR ELLSMEGPAL CEIIVSRSQQ FLPKSSAKKL PDGSLLSPPL EDMAPFLPEE
ELSKLMLIKT ADS
//