ID A0A0A0HUK5_PARBD Unreviewed; 1286 AA.
AC A0A0A0HUK5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KGM92262.1};
GN ORFNames=PADG_11446 {ECO:0000313|EMBL:KGM92262.1};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:KGM92262.1, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:KGM92262.1, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:KGM92262.1,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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}.
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DR EMBL; KN275959; KGM92262.1; -; Genomic_DNA.
DR RefSeq; XP_010758918.1; XM_010760616.1.
DR STRING; 502780.A0A0A0HUK5; -.
DR GeneID; 22587343; -.
DR KEGG; pbn:PADG_11446; -.
DR VEuPathDB; FungiDB:PADG_11446; -.
DR eggNOG; KOG1125; Eukaryota.
DR eggNOG; KOG1185; Eukaryota.
DR HOGENOM; CLU_006523_0_0_1; -.
DR InParanoid; A0A0A0HUK5; -.
DR OMA; RRFERIW; -.
DR OrthoDB; 2020042at2759; -.
DR Proteomes; UP000001628; 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 CDD; cd02004; TPP_BZL_OCoD_HPCL; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR045025; HACL1-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR PANTHER; PTHR43710:SF2; 2-HYDROXYACYL-COA LYASE 1; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13432; TPR_16; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT REPEAT 361..394
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 514..547
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 686..799
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 877..1007
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 1086..1260
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1286 AA; 140905 MW; 6FE67331F23E4880 CRC64;
MSFLGGPECS TAGNPLTQFT KHVQDDKSLQ RDRLVGRGPG GLQEGMRSRS MMGGQDKMMD
EFLQQGDQMP QGPAQPFAME QMRRELENFQ TAPQRTGSPG WAAEFDPGEQ ARMEAAFKPA
IARHFPGPEF SSADFVRFQQ QNRNGMQVTS GPATSHTPMM SAYQPQMMGF GGMNPGYVGM
MGPPYPMGMQ HHPHPPQQST QDDKGKGRMI ELDDQNWEAQ FAEIAASGQK DEDAEANAAI
EAELDEVDRS VHTEADEFRR FERIWKGIQA ETAAHRQMAD EDLSFDPMHL GEFGEWDHFD
GDLNVRIRDP QMGDYLFEEE NPFKSANNPF EEGIRIMKDG GNLSLAALAF EAAVQKDPKH
IKAWTLLGSA QAQNEKESPA IRALEQALKL DPNNLDALMG LAVSYTNEGY DSTAYRTLER
WLSVKYPQLV DPNSLSADTD LSFTDRHILH ERVTDLFIQA AQLSPQGEHM DPDVQVGLGV
LFYGAEEYHK AVDCFSAALA STESGSSNQS DQVHLLWNRL GATLANSGRS EEAIEAYEKA
LTINPNFVRA RYNLGVSCIN IGCFPEAVQH LLGALSMHKV VEEEGRERAR DIVGDSIDDA
QLEHMIHISQ NQSTNLYDTL RRVFSQMGRR DLSDLVVSGM DVSVFRSENP SLLSFTIIQK
GLPYSREVHT CEKSQLAVSE DMPPLTGAQI VARSLYDLGV SVIFGIVGIP VVEIAEEAIN
LGIRFIAFRN EQACSYAASV FGYMSGKPGV CLVVGGPGVL HAMAGIGNST VNTFPLLVLA
GSAETHMVTK GGFQEMDAIT LLTPHTKLAI RPFSPESVTN AIRNAYRTCW YGRPGTSFID
LPADLIQGKA PEGFSLPPRE RIVVPSPPKP SGDPVVISKV ARLLKSARAP LVVVGKGSAY
ARAESSILEF VEKTGIPFLP TPMGKGVIPD SHPLNTSSAR SAALKNADVV ILLGARLNWI
LHFGETPRWS RSVKFIQVDI NVEEIGRNAG DAELGIVGDI SLVIQQLLSS LSNWKYKPSS
PTSPNSYPSI LAASASKNEN ASQEKALLPT KPNGFLTYQR SYHIIKTVLN TLSPPEQGNI
VYVSEGANTM DISRSSFPLE QPRQRLDAGT YATMGVGLGY IVAAHAAYNL PSSPGEKIPP
KQKKIVALEG DSAFGFSAME VETLARHRIP ALIFVMNNSG IYHGDTQTKD EWKTLQDETL
TSTNVAKGGL RSTSLLYETR YEHLAAMCGG RGYFVRTEEE LEKATREGFL EGERVTIVNV
IVEPGIGQSI QFGWQVAKEK GTEAKL
//
