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Database: UniProt
Entry: R7VRT3_COLLI
LinkDB: R7VRT3_COLLI
Original site: R7VRT3_COLLI 
ID   R7VRT3_COLLI            Unreviewed;       351 AA.
AC   R7VRT3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=2-hydroxyacyl-CoA lyase 2 {ECO:0000256|ARBA:ARBA00018936};
DE   AltName: Full=Acetolactate synthase-like protein {ECO:0000256|ARBA:ARBA00032551};
DE   AltName: Full=IlvB-like protein {ECO:0000256|ARBA:ARBA00030510};
DE   Flags: Fragment;
GN   ORFNames=A306_15139 {ECO:0000313|EMBL:EMC77639.1};
OS   Columba livia (Rock dove).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX   NCBI_TaxID=8932 {ECO:0000313|EMBL:EMC77639.1};
RN   [1] {ECO:0000313|EMBL:EMC77639.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Blood {ECO:0000313|EMBL:EMC77639.1};
RX   PubMed=23371554; DOI=10.1126/science.1230422;
RA   Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA   Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA   Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT   "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL   Science 339:1063-1067(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-hydroxyhexadecanoyl-CoA = formyl-CoA + pentadecanal;
CC         Xref=Rhea:RHEA:55212, ChEBI:CHEBI:17302, ChEBI:CHEBI:57376,
CC         ChEBI:CHEBI:138654; Evidence={ECO:0000256|ARBA:ARBA00000244};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55213;
CC         Evidence={ECO:0000256|ARBA:ARBA00000244};
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}.
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DR   EMBL; KB376119; EMC77639.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7VRT3; -.
DR   eggNOG; KOG1185; Eukaryota.
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   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
FT   DOMAIN          34..166
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          228..321
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EMC77639.1"
FT   NON_TER         351
FT                   /evidence="ECO:0000313|EMBL:EMC77639.1"
SQ   SEQUENCE   351 AA;  38256 MW;  0E79CF31497BBFB7 CRC64;
     YLRNYIRNLF AGAWEPQDLS PLPIHVPQAT QEEVQRCAEL LSRARKPLVL LGSQAMLPPT
     TPAQLCSALE SLGIPCYLGG ASRGLLPPES PILLRQNRRD ALRDADLVLL AGAVCDFRLS
     YGRLFNRGAA IVAVNRDREQ LLKNSDVFWK PRLAVQGDVA SFVVRLAQSL SGFSCPREWG
     EQLREAERRR EKEIRDKATV PAPPHLNPLD LLLCLDQLLP QNCILVADGG DFVATAAYIL
     RPRQPLAWLD PGPFGTLGVG GGFALGAKLC RPDAEVWVLY GDGSLGYSLM EFDTFVRHKT
     PVIALVGNDA CWSQIAREQV ALLGSNVACG LAYLGNGTFG TSWHLLAPGL G
//
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