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Database: UniProt
Entry: A0A091I193_CALAN
LinkDB: A0A091I193_CALAN
Original site: A0A091I193_CALAN 
ID   A0A091I193_CALAN        Unreviewed;       578 AA.
AC   A0A091I193;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=2-hydroxyacyl-CoA lyase 1 {ECO:0000313|EMBL:KFP01208.1};
GN   ORFNames=N300_01088 {ECO:0000313|EMBL:KFP01208.1};
OS   Calypte anna (Anna's hummingbird) (Archilochus anna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC   Trochilidae; Calypte.
OX   NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP01208.1, ECO:0000313|Proteomes:UP000054308};
RN   [1] {ECO:0000313|EMBL:KFP01208.1, ECO:0000313|Proteomes:UP000054308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP01208.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL218015; KFP01208.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091I193; -.
DR   STRING; 9244.A0A091I193; -.
DR   Proteomes; UP000054308; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:KFP01208.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        27..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        58..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        420..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..131
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          203..332
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          401..557
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   578 AA;  63483 MW;  2AA96EC528094D17 CRC64;
     MASGSGAEAV SGAQLIAESL KAQNIEYMFG IVGIPVTEIA VAAQAVGIKY VGMRNEQAVM
     FFVFTFLFFL SHFVLFSSRP GVCLVVSGPG FLHALGGMAN ATINCWPLIV IGGSSDRNQE
     TMGAFQEFPQ VEAGRLYNKL SVRPSSLEVI PFFLRRTSIY GRPGACYIDI PGDFVNLQVN
     KSSVKYMECC LPPPVSTAEQ SAVSKALCII AHSKQPLLII GKGAAYSHAE NNIRKLVDLC
     GLPFLPTPMA KGVVPDDHPN CVAAARSTAL QHADVIILLG ARLNWILHFG LPPRFRQDVK
     VIQIDICAEE LGNNVRPAAT LFGDINAVTQ QLLEEFGKRP LKYPSNSEWW KQLREKIVSN
     EERSKGLALQ KTLPMNYYTV FHHIRELIPK DCIIVSEGAN TMDIGRTMLP NYYPRQRLDA
     GTFGTMGVGL GFAIAAAMVA KDRTPEKRII CIEGDSAFGF SGMEVETICR HNLPILIIVV
     NNNGIYTGLD ADAWKEMLKF GDPATCVPPV SLLPNSHYEK IMSAFGGKGY FVKTPEELQN
     ALRASLADKQ TPSLVNVMID PQSERKKQEF HWLTRSNL
//
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