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
//