ID A0A091M769_CATAU Unreviewed; 543 AA.
AC A0A091M769;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=2-hydroxyacyl-CoA lyase 1 {ECO:0000313|EMBL:KFP54366.1};
DE Flags: Fragment;
GN ORFNames=N323_05083 {ECO:0000313|EMBL:KFP54366.1};
OS Cathartes aura (Turkey vulture) (Vultur aura).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae; Cathartes.
OX NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP54366.1, ECO:0000313|Proteomes:UP000053745};
RN [1] {ECO:0000313|EMBL:KFP54366.1, ECO:0000313|Proteomes:UP000053745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP54366.1};
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; KL318094; KFP54366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091M769; -.
DR Proteomes; UP000053745; 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:KFP54366.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053745};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..101
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 168..297
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 366..522
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP54366.1"
FT NON_TER 543
FT /evidence="ECO:0000313|EMBL:KFP54366.1"
SQ SEQUENCE 543 AA; 59365 MW; F658E24DC40254AA CRC64;
NIEYMFGIVG IPVTEIAIAA QAVGIKYVGM RNEQAACYAA SAVGYLTGRP GVCLVVSGPG
FLHALGGMAN ATMNCWPLIV IGGSSDRNQE TMGAFQEFPQ VEAGRLYNKL SVRPSSLEAV
RTSIYGRPGS CYIDIPGDFV NLQVNKSSVK HVECCLPPAI STAEHSAVSK AASIIARSKQ
PLLIIGKGAA YSHAENNIRK LVDLCGLPFL PTPMAKGVVP DNHPNCVAAA RSTALQDADV
IILLGARLNW ILHFGLPPRF RQDVKVIQID ICAEELGNNV RPAAILLGDI NAVTKQLLEE
FSKRPLKYPS NSEWWKKLRE KIMTNEERSK GLALQKSLPM NYYTVFHHIR EQIPKDCILV
SEGANTMDIG RTMLPNYYPR QRLDAGTFGT MGVGLGFAIA AAMVAKDRTP EKQVICIEGD
SAFGFSGMEV ETICRYNLPI LIIIVNNNGI YTGLDADTWK EMLKFGDPAT CVPPVSLLPN
SHYEEIMSAF GGKGYFVKTP EELQSALKAS MTDKQTPALI NVMIDPQSER KKQEFPWLTR
SNL
//