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Database: UniProt
Entry: F6YL86_CIOIN
LinkDB: F6YL86_CIOIN
Original site: F6YL86_CIOIN 
ID   F6YL86_CIOIN            Unreviewed;       589 AA.
AC   F6YL86;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 2.
DT   24-JAN-2024, entry version 57.
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};
GN   Name=LOC100178631 {ECO:0000313|Ensembl:ENSCINP00000013826.3};
OS   Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000013826.3, ECO:0000313|Proteomes:UP000008144};
RN   [1] {ECO:0000313|Proteomes:UP000008144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12481130; DOI=10.1126/science.1080049;
RA   Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA   Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA   Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA   Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA   Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA   Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA   Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA   Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA   Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA   Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA   Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA   Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA   Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA   Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA   Satoh N., Rokhsar D.S.;
RT   "The draft genome of Ciona intestinalis: insights into chordate and
RT   vertebrate origins.";
RL   Science 298:2157-2167(2002).
RN   [2] {ECO:0000313|Ensembl:ENSCINP00000013826.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; EAAA01001588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F6YL86; -.
DR   STRING; 7719.ENSCINP00000013826; -.
DR   Ensembl; ENSCINT00000013826.3; ENSCINP00000013826.3; ENSCING00000006732.3.
DR   GeneTree; ENSGT00940000156802; -.
DR   HOGENOM; CLU_013748_3_3_1; -.
DR   InParanoid; F6YL86; -.
DR   OMA; YMGMIGM; -.
DR   TreeFam; TF105690; -.
DR   Proteomes; UP000008144; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0001561; P:fatty acid alpha-oxidation; IBA:GO_Central.
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:UP000008144};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          14..124
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          202..331
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          401..568
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   589 AA;  64419 MW;  2815E3551A448A63 CRC64;
     HIKPNMSDEN VMVTGAEVYA RALKIQGVEY VFGIVGVPIM EVAMAIQQVG LKFIGMRNEQ
     SAAYAAGAIG YLTGRPGACL VVSGPGLIHA LGGMANAMEN CWPMIVLGGS SDEDQQAMGA
     FQEYPQVEAC RLYSKFAARP TSITIIPEII EKAVRTSIYG RPGACYVDIP GNFVNASVKL
     GDCRFRSECP PPPRSLADPT SISSAANLML AAKRPLIIIG KGAAYARAED EVRRFVEDHN
     LPFLPTPMGK GVIPDDHELC VSAARSRALL NCDVIVLLGA RLNWQLHFGR QPRFNKDVKV
     IQVDICAEEL HNNVQSTVAL LGNIPNVIQQ LIEHSKKTHR GVPWRLSKDS DWWKFLQEKI
     DSNAVSTKAL AEDKSVPLNY YAVFDVLTKH LPKDCIIISE GANTMDISRT MILNYLPRHR
     LDAGTFGTMG VGLGFAVAAS LYSLDIAKKT GMPPQKVVCI QGDSAFGFSG MELETVCRYN
     LPLVFVVVNN NGIYSGGNKD FWEAIKMSGD IAVQNSAPPT FLTPESKYEK LIEAFGGEGH
     SCVTADQLDE SFKRCMSRSS EQASLINVMI DTTSARKEQE FTWLTRSKM
//
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