ID A0A0M2LSF7_9MICO Unreviewed; 564 AA.
AC A0A0M2LSF7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Thiamine pyrophosphate-binding protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=XM48_07765 {ECO:0000313|EMBL:KKI20405.1};
OS Leucobacter sp. Ag1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1642040 {ECO:0000313|EMBL:KKI20405.1, ECO:0000313|Proteomes:UP000033836};
RN [1] {ECO:0000313|EMBL:KKI20405.1, ECO:0000313|Proteomes:UP000033836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI20405.1,
RC ECO:0000313|Proteomes:UP000033836};
RA Pei D., Kukutla P., Yu W., Xu J.;
RT "Draft Genome Sequences of Leucobacter sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) 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}.
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:KKI20405.1}.
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DR EMBL; LAYO01000092; KKI20405.1; -; Genomic_DNA.
DR RefSeq; WP_046455239.1; NZ_LAYO01000092.1.
DR AlphaFoldDB; A0A0M2LSF7; -.
DR STRING; 1642040.XM48_07765; -.
DR PATRIC; fig|1642040.3.peg.539; -.
DR OrthoDB; 3203527at2; -.
DR Proteomes; UP000033836; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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 PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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 Reference proteome {ECO:0000313|Proteomes:UP000033836}.
FT DOMAIN 13..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 219..353
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
SQ SEQUENCE 564 AA; 57232 MW; 065210AECF485D51 CRC64;
MSQFASVAPA APTVSAALAG ALARHTAQGF ARIARVNATL VTDLEQHGIG VTMVGHEVAT
IASADAFARA TGTLAVAVTT TGPGFTNALT ALAETTRARV PLIVLAADAP TTGNRPWDVD
QEMLAAALGV RTLTVTPDNI DAIVDRAVDS ALRTRRPVVL SVAIDVIGAP ASLTDSRGID
LSDPAVIRSL SAATLPSAAA VPAAIPHPPT GVNPVERTSA VQALTVAMRP VIIAGRGAWL
SGAATELGLM ADALGAITAT TALARGIFPA QHFDVGVVGG LGQDAAMRLI SEADAVLVVG
ASLNSFTTAG GTLFGPHTTV VRIDVDDVPA PEADHEIVQH RLRGDASAVL RELRETLALS
RPAPSGWRER VPGLEPGGAL RVRDTGFVEH PTGICADGLL DPRSVATRLA ELLPLDRYVA
TDGGSAIAWS GRYWSVASPA RSIMVGSAFR AIGLGCASIA GVAAAAPGST AVLSTGSDPG
LQALDDVETA IRTAQRCVIV VWNDGSSAAD FAALANALGA QGVSVTELAH LDALAAWSAA
GGTGTILLDC RVSPTVPSYV PRTH
//
