ID A0A068SF87_9FUNG Unreviewed; 577 AA.
AC A0A068SF87;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=2-hydroxyacyl-lyase 1 {ECO:0000313|EMBL:CDH60487.1};
GN ORFNames=LCOR_11272.1 {ECO:0000313|EMBL:CDH60487.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH60487.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH60487.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) 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:CDH60487.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CBTN010000094; CDH60487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068SF87; -.
DR STRING; 1263082.A0A068SF87; -.
DR VEuPathDB; FungiDB:LCOR_11272.1; -.
DR OrthoDB; 2020042at2759; -.
DR Proteomes; UP000027586; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:CDH60487.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 12..126
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 206..335
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 402..553
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 577 AA; 62302 MW; 0982E5F642C2127E CRC64;
MSPPLNTKPA SSGAELIATT LKHQGVKVIF GIVGIPVIEV AEACIAAGIR FLAFRNEQSA
AYAASAYGYL SGQPGVCLTV GGPGVIHALA GLANAKVNCW PMVLLAGSSD TDQVDMGAFQ
ELDQVEACRP YCKYAARPMS VDKIPTTIEK ALRTAYYGRP GATYVDLPAD FIQYPIQDAN
KMNTIVQSVP VIPSTAPRSV ADDTSLQQAA QWLRQAKSPL IVVGKGAAYA RAESEIRQLV
ERTQIPFLPT PMGKGVVSDT HPLCVSAARS KALKNADVVL LLGARLNWIL HYGHSPRWTN
GVKFIQVDVM PEEIGNNAAH TLPLAGDIQA TVAQLLARHP LPRLPSTNQY VSDLKNKVKQ
NVEKSLAARK QGSDTAVLNY KTAYTVIKDI LPENDVVYIS EGANTMDIAR SFFDVHEPRR
RLDAGTFATM GVGMGYAIAA QAYYPNKRVV SIVGDSAFGF SAMELETAVR SKLPMIILVI
NNNGIYHGLD ADDFEQSRRD GNLPSTALLP DTRYDQLSVA FGGKGWLVKN RVELAKALKE
AMTVKDNACV INVMIAPGGR TKLEFGWMSK ADTKSKL
//
