ID J9IYV8_9SPIT Unreviewed; 562 AA.
AC J9IYV8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=2-hydroxyacyl-CoA lyase 1 {ECO:0000313|EMBL:EJY87672.1};
GN ORFNames=OXYTRI_00284 {ECO:0000313|EMBL:EJY87672.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY87672.1};
RN [1] {ECO:0000313|EMBL:EJY87672.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY87672.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJY87672.1}.
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DR EMBL; AMCR01001063; EJY87672.1; -; Genomic_DNA.
DR AlphaFoldDB; J9IYV8; -.
DR EnsemblProtists; EJY87672; EJY87672; OXYTRI_00284.
DR OrthoDB; 1966690at2759; -.
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; 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 Lyase {ECO:0000313|EMBL:EJY87672.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 387..534
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 562 AA; 61801 MW; E45E427D73EA714D CRC64;
MITGYEVLAK ALALQDLKYA FGIVGIPVYE IGMALQANDV YYIGFRNEQA AAYAGSAIGY
ITQKPGIVLA VSGPGMTNCI SAMANAMVNK WPMIVIAGAS DASMDGKGAF QEFDQLALAK
PCTKYAARPA NIKHIPLIVQ KAVRMSMYGT PGAVYIDMPA DLIYAKIEEK YINYLPVVNI
LPQPQVQDYL IGATLDLLKS AKQPLIIVGK GVAYGQAENE MREFINKTNI PFLATPMGKG
VVKDTDIHSV GPARTFVLQN ADVIFLVGAR LNWILHFGEA PRFNKNVKII QLDNDPHEFN
TNVESSVCLF GDAKLTLGQL NHAVKEEILP ESSGWWKTLR EKVDKNRVVA DKLNADRNIP
MNYYSVLKMI EDTIHSQKDD YIIVSEGSNT MDIGRTILTN DQARQRLDAG TFGTMGVGFG
FAIAAQALYP KKKIVMVVGD SAFGFSGMEV ETAARYNIPL KVIIVNNNGI LYGNESIDKS
DPKSIPVYAL SINANYEMIS QAFGGKGAQV KDHADLQKNL TEMLNDDNLW VLNVMIDPNG
GRRPQEFAWL TRDEPKEEKA KL
//
