ID   A0A3B4GCN9_9CICH        Unreviewed;       568 AA.
AC   A0A3B4GCN9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=2-hydroxyacyl-CoA lyase 1 {ECO:0000313|Ensembl:ENSPNYP00000019373.1, ECO:0000313|RefSeq:XP_005738507.1};
GN   Name=hacl1 {ECO:0000313|RefSeq:XP_005738507.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000019373.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000019373.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_005738507.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_005738507.1; XM_005738450.1.
DR   AlphaFoldDB; A0A3B4GCN9; -.
DR   Ensembl; ENSPNYT00000019858.1; ENSPNYP00000019373.1; ENSPNYG00000014606.1.
DR   GeneID; 102214808; -.
DR   CTD; 26061; -.
DR   GeneTree; ENSGT00940000156802; -.
DR   OrthoDB; 1966690at2759; -.
DR   Proteomes; UP000261460; Unplaced.
DR   Proteomes; UP000695023; Unplaced.
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|RefSeq:XP_005738507.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000695023};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          5..118
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          193..322
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          391..547
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   568 AA;  61007 MW;  4012C7B318A05FFC CRC64;
     MDEVTGAQLI AESLKAQKVD YMFGIVGVPI IEVAMAAQAA GIRYVGMRNE QAACYAASAV
     GYITGRPGAC LVVSGPGLIH ALGGMANANM NCWPVVVIGG SSDRNQETAG AFQEFPQVEA
     CRLYSKFSAR PSSLEAIPSV IEKAVRTSIY GRPGACYVDI AGDMVNAKVE RSKVREVSCC
     PPPPVSLADQ GSVTEAISVL KAAKTPLVII GKGAAYGRAE AVLRELIEMS GLPFLPTPMG
     KGVLPDDHAN CVAAARSRAL LQADVILLFG ARLNWMLHFG LSPRFNPNVK IIQVDLCAEE
     MGNNVRPAVA LLGDISAVAT QLLLCVRRDG WKYPSNAEWW STLKSKIAAN AKISKALALQ
     STVPLNYYTV FHHISQLLPH DCIIVSEGAN TMDIGRTMLN NYLPRHRLDA GTFGTMGVGL
     GFAIAAAAVE ASQNTSRRVV CVEGDSAFGF SGMEVETMCR YSLPVVVIVV NNNGIYSGVD
     SETWKAMKQM GELTSVAPPV SLLPDARYDE VMKAFGGRGL LVRTVEELRS ALQLSLSDWE
     RPSLINVLID PSSDRKQQEF PWLTRSNL
//