ID   L5LI36_MYODS            Unreviewed;       639 AA.
AC   L5LI36;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=2-hydroxyacyl-CoA lyase 1 {ECO:0000313|EMBL:ELK25318.1};
GN   ORFNames=MDA_GLEAN10020718 {ECO:0000313|EMBL:ELK25318.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK25318.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxyoctadecanoyl-CoA = formyl-CoA + heptadecanal;
CC         Xref=Rhea:RHEA:55196, ChEBI:CHEBI:57376, ChEBI:CHEBI:74116,
CC         ChEBI:CHEBI:138631; Evidence={ECO:0000256|ARBA:ARBA00000194};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55197;
CC         Evidence={ECO:0000256|ARBA:ARBA00000194};
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; KB112110; ELK25318.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5LI36; -.
DR   Proteomes; UP000010556; 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; 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:ELK25318.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          89..189
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          265..393
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          462..618
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   639 AA;  69108 MW;  04A0186F23DA9B37 CRC64;
     MSESNLGDAS EEQVSGAAVL ARALKAQVRG TTLRGRAPTG AGEGRAVLGA GIAAGAGGVI
     GNEGGRSGGN RVAGVRAFTR PRSCPPPQDV KYMFGIVGIP VTEIAIAAQQ LGIRYVGMRN
     EQAACYAASA VGYLTGRPGV CLVVSGPGLV HALGGMANAN MNCWPLIVIG GSSERCQETM
     GAFQEFPQVE ACRLYSKFSV RPSSIEAIPS IIEKAVRSSI YGRPGACYID IPADFVNLQV
     NVNSIKYVEC CMPPPISMAE TSAVQMAASV IRNAKQPLLI IGKGAAYAHA EEGIRKLVEQ
     CKLPFLPTPM GKGVIPDNHP NCVAAARSRA LQFADVIILF GARLNWILHF GLPPRYQPDV
     KFIQIDICAE ELGNNVRPAV TLLGDINAVT KQLLEQFDKT PWQYPPESKW WNTLKEKMKS
     NEAASKELAS KKSLPMNYYT VFYHVQEQLP RDCMVVSEGA NTMDIGRTVL QNYLPRHRLD
     AGTFGTMGVG LGFAIAAAIV AKDRNPGQRV ICVEGDSAFG FSGMEVETIC RYNLPIVLLV
     VNNNGIYQGI DTDSWKEMLK FGDATALAPP MCLLPNAHYE QVMTAFGGNG YFVQTREELQ
     ESLRKSLADA TKPSLINIMI EPQSMRKAQD FHWLTRSNM
//