GenomeNet

Database: UniProt
Entry: A0A091QIY4_9GRUI
LinkDB: A0A091QIY4_9GRUI
Original site: A0A091QIY4_9GRUI 
ID   A0A091QIY4_9GRUI        Unreviewed;       473 AA.
AC   A0A091QIY4;
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:KFQ27153.1};
DE   Flags: Fragment;
GN   ORFNames=N332_09986 {ECO:0000313|EMBL:KFQ27153.1};
OS   Mesitornis unicolor (brown roatelo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX   NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ27153.1, ECO:0000313|Proteomes:UP000053369};
RN   [1] {ECO:0000313|EMBL:KFQ27153.1, ECO:0000313|Proteomes:UP000053369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ27153.1};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KK798634; KFQ27153.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091QIY4; -.
DR   Proteomes; UP000053369; 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:KFQ27153.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053369};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..101
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          171..300
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          369..452
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ27153.1"
FT   NON_TER         473
FT                   /evidence="ECO:0000313|EMBL:KFQ27153.1"
SQ   SEQUENCE   473 AA;  51505 MW;  1D95B45A70E86606 CRC64;
     NIEYMFGIVG IPVTEIAIAA QAVGIKYVGM RNEQAACYAA SAVGYLTGRP GVCLVVSGPG
     FLHALGGMAN ATINCWPLIV IGGSSDRNQE TMGAFQEFPQ VEAGRLYNKL SVRPSSLEAI
     PAVRSSIYGR PGSCYIDIPG DFVNLQVNKS SVKYMECCLP PPISTAEHSA ISKAASIIAH
     SKQPLLIIGK GAAYSHAENN IRKLVDLCGL PFLPTPMAKG VVPDNHPNCV AAARSTALQH
     ADVIILLGAR LNWILHFGLP PRFRPDVKVI QIDICAEELG NNVRPAAVLL GDISAVTQQL
     LEEFSRRPLK YPSNSEWWKR LREKIMNNEE RSKGLALQKS LPMNYYTVFH HIKELIPKDC
     ILVSEGANTM DIGRTMLPNY YPRQRLDAGT FGTMGVGLGF AIAAAMVARD RTPEKRVICI
     EGDSAFGFSG MEVETICRYN LPILIIVVNN NGIYTGLDAD AWKEMLKFGD PTT
//
DBGET integrated database retrieval system