ID D9TC43_MICAI Unreviewed; 530 AA.
AC D9TC43;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Thiamine pyrophosphate TPP-binding domain-containing protein {ECO:0000313|EMBL:ADL44591.1};
GN OrderedLocusNames=Micau_1028 {ECO:0000313|EMBL:ADL44591.1};
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL44591.1, ECO:0000313|Proteomes:UP000001908};
RN [1] {ECO:0000313|EMBL:ADL44591.1, ECO:0000313|Proteomes:UP000001908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC {ECO:0000313|Proteomes:UP000001908};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP002162; ADL44591.1; -; Genomic_DNA.
DR RefSeq; WP_013284230.1; NC_014391.1.
DR AlphaFoldDB; D9TC43; -.
DR STRING; 644283.Micau_1028; -.
DR KEGG; mau:Micau_1028; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_11; -.
DR OrthoDB; 2443624at2; -.
DR Proteomes; UP000001908; 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 CDD; cd02002; TPP_BFDC; 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:SF133; BENZOYLFORMATE DECARBOXYLASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000001908};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..103
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 381..518
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 328..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..347
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 55744 MW; 03587F017CC69710 CRC64;
MATVREATYD LLRALGLTTV FGNPGSTEEP FLQHFPDDFH YVHALQEASA VAMADGYAQG
TGRPAHVNLH TAPGTGNGMG NLVTAWHNRT PLIVSAGQQT REMLLIEPRL ASPRAVELAQ
PYVKWAHEPA RAQDIPAAFM RAYASAVQPP AGPVFLSLPM DDWDRPADPP PQVRTVATRI
APDPDRLRSF AGALAAARAP ALVLGAAVDR SDAWPDAVAL AEHLAAPVWA APAPERAVFP
ERHPHFRGVL PYAIGPLSEA LRGHDVVLVV GAPVFRYYPH VPGDYLPGDA RLLHVTDDPD
EAARAPVGES LLGDAGLTMA ALCELLPPTD RAAPSPRPQP ALPEPADPPS ADTLFAALAA
AWPADGVLVQ ESPSNLAALR RRLPIERPRS YLTMASGGLG FGLPAAVGMA LAERDTGRGR
PVVAVVGDGS FHYSVQALWT AARLRLPLAV VVPVNQQYAI LKAFAELKHT PGVPALDLPG
LDVTAVAHGY GCAGEVTTPD GLGAALAAAL GADRPTVLPV PISTDVPRIL
//
