ID A0A2S7K529_9PROT Unreviewed; 542 AA.
AC A0A2S7K529;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Thiamine pyrophosphate-requiring protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CW354_10995 {ECO:0000313|EMBL:PQA87599.1};
OS Marinicaulis flavus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC Parvularculaceae; Marinicaulis.
OX NCBI_TaxID=2058213 {ECO:0000313|EMBL:PQA87599.1, ECO:0000313|Proteomes:UP000239504};
RN [1] {ECO:0000313|EMBL:PQA87599.1, ECO:0000313|Proteomes:UP000239504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY-3-19 {ECO:0000313|EMBL:PQA87599.1,
RC ECO:0000313|Proteomes:UP000239504};
RA Hurst M.R.H.;
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:PQA87599.1}.
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DR EMBL; PJCH01000006; PQA87599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7K529; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000239504; 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; 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:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000239504};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..101
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 184..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 383..530
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 542 AA; 58686 MW; 582D3A464BC2BD75 CRC64;
MKMSAAIAQI LKREGVDVIF GYPRNAVLEE AASAGIRPVI VRQERTGLHM ADALSRLTRG
KRMGVFAMQH GPGTENAYGG VAQAYSESVP VLVLPQGYAR RLAYVPDNYN ASLSMRDVTK
HAEPITDAAE IENVMRRAFT QLRNGRLRPV LVEMPSDLLN AQTAEPVGYR PVPRTRSGPD
PDAVREAART LVGAERPVIY AGQGVHWAEA YDELQALAEL LAAPVSTSLE GKSAFNERHP
LALGAGGAAT PGQLRRFLDD ADVILGIGCS FSETAFGVRM PEGKRVIHAT LDAADLNKSV
ICELALTGDA KLTLAMLRDA CAGLIEGKRE ISRTAEKIAA VEKEWMRDWL PLLTSDETPL
SPYRVLWDLQ SAVDVGETII THDAGSPRDQ LSPFWKTTKP MTYIGWGKST QLGYGLGLAM
GAKIACPDKL CVNVWGDAAI GFTGMDFETA VREKLPILSI LLNNSAMAIE LDQMPVATER
FRSTDISGDY AAFARALGGY GERVSEPEEI KPAIARAIAA IENGQPALLE FITCKETRAS
RL
//
