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Database: UniProt
Entry: A0A0V1H980_9BILA
LinkDB: A0A0V1H980_9BILA
Original site: A0A0V1H980_9BILA 
ID   A0A0V1H980_9BILA        Unreviewed;       605 AA.
AC   A0A0V1H980;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=2-hydroxyacyl-CoA lyase 2 {ECO:0000256|ARBA:ARBA00018936};
DE   AltName: Full=IlvB-like protein {ECO:0000256|ARBA:ARBA00030510};
DE   Flags: Fragment;
GN   Name=ilvbl {ECO:0000313|EMBL:KRZ06934.1};
GN   ORFNames=T11_9215 {ECO:0000313|EMBL:KRZ06934.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ06934.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ06934.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ06934.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-hydroxyhexadecanoyl-CoA = formyl-CoA + pentadecanal;
CC         Xref=Rhea:RHEA:55212, ChEBI:CHEBI:17302, ChEBI:CHEBI:57376,
CC         ChEBI:CHEBI:138654; Evidence={ECO:0000256|ARBA:ARBA00000244};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55213;
CC         Evidence={ECO:0000256|ARBA:ARBA00000244};
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   -!- 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:KRZ06934.1}.
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DR   EMBL; JYDP01000110; KRZ06934.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1H980; -.
DR   Proteomes; UP000055024; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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; 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; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          62..167
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          263..390
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          463..563
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ06934.1"
SQ   SEQUENCE   605 AA;  66670 MW;  43E6B7F0031042CD CRC64;
     LKYFQSMDDT FKLDWTSVSV ALLVCLAIIV VQYTWMTVCR RFKVLQKCQS RLTNHGGEIV
     AREHNVNFVF TLCGGHISPI LAACENLNIR IIDTRHEATA VFAADAMSRL SGKIGVACVT
     AGPGVANTIV ALKNAQMAES SVLLLAGASP TLLKGRGPLQ DMDQIALVKS ICKCAVTVTR
     VKDISKKLRP VFVELPVEVL YPFDIVKKQM GIKENCKGFR DRIINFYLRW ALCQLFQDAE
     LEFDCSPLTP HLTEAKIADV ELIKQMLARS SRPLMLLGSQ LMANFENIHQ LKGAIELIGI
     PCYCGGMSRG VLSDNSELLF RHKRRKALKQ ADFILLVGAV CDFRLNYGKS LNPMADVVVV
     NRGKNQIKMN AGWFWKLSHG ICADPSDFLI KLSQANVNDS LKESRFSGWM EILRDQENLQ
     ELEIIKLTEQ NSIDQNLLNS ILLLKKVDSA APDDTIFVFD GDPGPFGTLG IGAGFAIAAK
     LCHPNLPVWI IYGDGAVGYS LLEFDTFTRH QLPVVAVVGN DARWSQIHRT QTSIFGTAVG
     CVLEYSSYEQ VAAAFHFKGI KIDGTNGITV EGILNEVPQL NAHGIGVLLN CYISPSGFRD
     GSISL
//
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