ID B8IRB3_METNO Unreviewed; 581 AA.
AC B8IRB3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=Thiamine pyrophosphate protein central region {ECO:0000313|EMBL:ACL58653.1};
GN OrderedLocusNames=Mnod_3747 {ECO:0000313|EMBL:ACL58653.1};
OS Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL58653.1, ECO:0000313|Proteomes:UP000008207};
RN [1] {ECO:0000313|EMBL:ACL58653.1, ECO:0000313|Proteomes:UP000008207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC {ECO:0000313|Proteomes:UP000008207};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP001349; ACL58653.1; -; Genomic_DNA.
DR RefSeq; WP_015930309.1; NC_011894.1.
DR AlphaFoldDB; B8IRB3; -.
DR STRING; 460265.Mnod_3747; -.
DR KEGG; mno:Mnod_3747; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_5; -.
DR OMA; GGSPMVW; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000008207; Chromosome.
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:0044281; P:small molecule 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:SF169; 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:UP000008207};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 16..130
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 207..345
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 415..560
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 581 AA; 61200 MW; 45ED7E6019E09284 CRC64;
MTIAARSASP DAGGNMTGAD ALAAALQRHG VREVFGQSIP SALFLAAPHY GIRQIGYRTE
NAGAAMADAF ARISGRVGVV AAQNGPAATL LVPGLAEALK ASIPVVAIVQ DVNRRFTDKN
AFQELDHVAL FSGVAKWVRR IGDPSRIDDY VDMAFTAAST GRPGPAVLLV PLDILDERAE
IDAVAPRRAA SLGAYPLDRT VADPARIAEA ASLIAAAQRP VVIAGGGVHS SGASAELAAL
QALGLPVGTT VMGKGAVDET NPLSLGVVGY FMAPRSRSSH LREVVTGADV VLLVGNRANQ
NGTDSWSLYP REARYVHIDV DGGEIGRNYE ALRLAGDAKL TLAALTEALR ATGLPGSQDR
RAALEAQIAD ARARHAEDMR RLVDMEAVPV RPERIMAEID AVVTPETIMV ADASYASIWI
ANFLTARKPG QRFLTPRGIA GLGWGLPFAL GAKTARPDAP VICVTGDGGF GHVWSELETA
RRMRLPVVLI VLNNQILGYQ KHAELSLFGN FTDVCHFEAV DHAAIARACG CTGVRIERPG
ELSGALRDAL AADSVTVIDV VTDQRAYPPI TSFEGKDALA Y
//