ID A0A2S7PBA1_9HELO Unreviewed; 602 AA.
AC A0A2S7PBA1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=2-hydroxyphytanoyl-lyase protein {ECO:0000313|EMBL:PQE11581.1};
GN ORFNames=CJF32_00004753 {ECO:0000313|EMBL:PQE11581.1};
OS Rutstroemia sp. NJR-2017a WRK4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070412 {ECO:0000313|EMBL:PQE11581.1, ECO:0000313|Proteomes:UP000238813};
RN [1] {ECO:0000313|EMBL:PQE11581.1, ECO:0000313|Proteomes:UP000238813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a WRK4 {ECO:0000313|EMBL:PQE11581.1,
RC ECO:0000313|Proteomes:UP000238813};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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, ECO:0000256|RuleBase:RU362132}.
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:PQE11581.1}.
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DR EMBL; NJPR01000123; PQE11581.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7PBA1; -.
DR STRING; 2070412.A0A2S7PBA1; -.
DR InParanoid; A0A2S7PBA1; -.
DR OrthoDB; 2020042at2759; -.
DR Proteomes; UP000238813; 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; 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 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 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 Lyase {ECO:0000313|EMBL:PQE11581.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000238813};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..565
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 580..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 63747 MW; 503FFABBE7364924 CRC64;
MPSPTGAQLI AKALHELGVK VIFGLVGIPV VQIAEEAIAL GIRFIAFRNE QAASYAATAY
GYLTGRPGVC LVVGGPGVLH AMAGVGNSSA NAFPMLLLAG SSETHLVTKG AFQELDAISL
LAPHTKIAIR STLDSIAPSI TNAYRTSWYG RPGTGFVDLP ADVIQGEGEY IPTKMVSTAP
KPAADPERIK AVTQLLKSAK APLIILGKGA AYAQAESLIR KLIDQTQIPF LPTPMGKGIL
PDSHPLNTST ARSAALLGAD VILILGARLN WILHYGEAPK YNPSVKIIQV DISADEIGKN
NGDASLGLVG DINIVTSQLL ASLQNWHYDT SSSPYIKTLQ ASTHKNEAKA ASAAQNAKIP
LTYQHTFSLI KETIHSISPS SDGRVVYVSE GANTMDISRS AFPVSHPRLR LDAGTHATMG
VGLGYAIAAH CAYNLPSPEA SSGPSLLGKK IVCLEGDSAL GFSLAEIETM ARYKMDILIF
VLNNGGVYHG DSDSARTWRE LQGKSKDGSA KGGLRSTSLG WEVAYEKVAE MCGGRGYFVR
TPEELRTATR EGFLATGEGP TVVNVVIEAG EGKALEFTWQ KSDSKKKDAN TKESTKKDVA
KL
//