ID A0A0C7MQQ6_9SACH Unreviewed; 552 AA.
AC A0A0C7MQQ6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=LALA0S05e01266g1_1 {ECO:0000313|EMBL:CEP62251.1};
GN ORFNames=LALA0_S05e01266g {ECO:0000313|EMBL:CEP62251.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP62251.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP62251.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP62251.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) 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}.
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DR EMBL; LN736364; CEP62251.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7MQQ6; -.
DR STRING; 1245769.A0A0C7MQQ6; -.
DR HOGENOM; CLU_013748_3_3_1; -.
DR OrthoDB; 2020042at2759; -.
DR Proteomes; UP000054304; Unassembled WGS sequence.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000054304};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 379..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 552 AA; 59480 MW; 2AB1697B668F958F CRC64;
MSSFPEYLSD ALSSYGVDVI FGIVGIPVVE LADTVISKGK IKFYGFRNEQ AASYAASAYG
FLTGKPAVLL TVGGPGVIHA LAGVYNSISN KWPLLVIAGS SEDTNRGGFQ ELDQVSLLTP
YIKFTARLDS SNVDETLYNA LRQASLGTPG VSYLDIPGNV FAQKCLEIRP RSPRPLRAVK
FQPPDADLKA VAKTLRSSKN ILCVIGKGAT DSAGEVRAFV QKFQIPFLPT PMAKGVVPDS
SNLNVSSARS LALRSADVVL VLGARLNWIL HFGEAPKWKK SAIFIQVDTT AEDLGHNNRL
GLTYSLCGDI GHTLRKLTLS LGSFSSSGVT ADIRKNIVAN QGKLRAKEEA VTAKLNYNQV
YALIRRHIVD RNTFIVSEGA NTMDVARISF PTDYPKQRLD AGTNATMGVG LGYAIAAKLA
HPSKKVICIQ GDSAFGFSGM ELETAARYRL GLVVIVMNNS GIYHGASEVG DTKSHQPRNM
VSTSLTTDCR YDLVADGLGC RGFLVKSLPE LNTALEMAFK LAEEGLPALL NVIIEPGRQG
KLEFGWQNRS KL
//
