ID A0A2U2CCU1_9RHOB Unreviewed; 550 AA.
AC A0A2U2CCU1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:PWE29669.1};
GN ORFNames=C4N9_07970 {ECO:0000313|EMBL:PWE29669.1};
OS Pararhodobacter marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pararhodobacter.
OX NCBI_TaxID=2184063 {ECO:0000313|EMBL:PWE29669.1, ECO:0000313|Proteomes:UP000244940};
RN [1] {ECO:0000313|EMBL:PWE29669.1, ECO:0000313|Proteomes:UP000244940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIC4N-9 {ECO:0000313|EMBL:PWE29669.1,
RC ECO:0000313|Proteomes:UP000244940};
RA Lai Q.Sr., Liu X., Shao Z.;
RT "Pararhodobacter marina sp. nov., isolated from deep-sea water of the
RT Indian Ocean.";
RL Submitted (MAY-2018) 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:PWE29669.1}.
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DR EMBL; QEYD01000004; PWE29669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2CCU1; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000244940; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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: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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000244940};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 402..526
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 550 AA; 58042 MW; 259052819BDEB7B6 CRC64;
MTETVGYQIA RALADIGVKT VFGVISIHNM PILDGIATQD RIRFVPARGE AGAMGMADAY
SRVTGELGVV ITSTGTAAGN AAGAQAEALT AGSRVLHITT QIDREFMDRD RAAIHDVPKQ
PEMLRGVSKA VFRIWDEKSA TGTLEAAVRA ALTPPTGPVS LEIPVDVQRL DAMDGHPAVA
PVVALPGNDE TRLDALAEMV KQAKRPMIWL GGGARGAQAE ATELVARGFG AVTSTQGRAV
VPEENPATLG AFNMTPEAQA IYAQSDLMIV VGSRLRGNET LNNKMALPRP LVQIDADATQ
YGRNYPVDLF LCGDAAKTLR GLLDRLPAKL DVDPQQAYDI AVARAKAEGV LRERLGPYQV
IADHLMSVIP AGKHPWVRDV TISNSTFGNR YVQIGAPNLG VHALGGGIGQ GVAMGIGAAV
ASPDARTVTL LGDGGTMLGL AELITAVDED LDMTFLLMND QAYGVIENIQ DAQYDGRRHY
SKLKTPNFAK LCDAIDLPHT KVDDITAFEA VFNESMTRKG PHVVEVDMTA IGPYAVAFAG
PPAGAAGGKS
//
