ID Q2H848_CHAGB Unreviewed; 591 AA.
AC Q2H848;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAQ91671.1};
GN ORFNames=CHGG_03606 {ECO:0000313|EMBL:EAQ91671.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ91671.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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DR EMBL; CH408030; EAQ91671.1; -; Genomic_DNA.
DR RefSeq; XP_001230122.1; XM_001230121.1.
DR AlphaFoldDB; Q2H848; -.
DR STRING; 306901.Q2H848; -.
DR GeneID; 4389451; -.
DR VEuPathDB; FungiDB:CHGG_03606; -.
DR eggNOG; KOG1185; Eukaryota.
DR HOGENOM; CLU_013748_4_0_1; -.
DR InParanoid; Q2H848; -.
DR OMA; DMCFPGD; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF164; PYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001056}.
FT DOMAIN 210..315
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 418..585
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 50..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 64510 MW; 087E9C99A90A0493 CRC64;
MYTTSFAFFE ALWDAGVEYV FVNLGSDHPS IIEAMVKGSR EKKGQFPRII TCPNERGGHV
HGKRLRAPEQ QTASRDRARR RRDPRAWGSR AQRERGTRAT CSCSRASRPS RRKGELRGSR
TGVHPLDSRT VPDLEADRRA VLPLCGRARK TGVNVKQMVN RALQFARSGP QGPVYLCGSR
EVMEMEMEPY EIRQEEWEPV ELGGLPAGAV RRIAEALAGA KEPLLVTGYG GRNQAMPAAL
VELANTVKGL RVLDTGGSDM CFPADHPAWL GLRYGVEAAV TTADAIVVLD CDVPWITTQC
KPKADAKIFH IDVDPLKQVM PLYYIAAQHR YRADGLTSVE QITALLQKDE GLKAQLSSAE
SDKRWAAMEE SYKKHLETIA VRSKPLENGE FGTSHLCAKL KELCPEDTIW AIEAVTNTLF
VHESLQPKLP GQWINCGGGG LGWSGGGALG IKLATDHEAK LKGEKGKFVV QIVGDGSYLF
SVPGSVYWIA KRYNIPILTI VLNNKGWNAP RKSLLLVHPE GLGSQASNEE INISFDPSPD
YAGIAKAAAG GDIHAAKVDK AADLERVLKE AIEVVQGGQT AVLDCKVSMG C
//
