ID G3HM53_CRIGR Unreviewed; 632 AA.
AC G3HM53;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=2-hydroxyacyl-CoA lyase 2 {ECO:0000256|ARBA:ARBA00018936};
DE AltName: Full=Acetolactate synthase-like protein {ECO:0000256|ARBA:ARBA00032551};
DE AltName: Full=IlvB-like protein {ECO:0000256|ARBA:ARBA00030510};
GN Name=Ilvbl {ECO:0000313|Ensembl:ENSCGRP00001002738.1,
GN ECO:0000313|RefSeq:XP_027275283.1};
GN ORFNames=I79_011801 {ECO:0000313|EMBL:EGV95477.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV95477.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
RN [2] {ECO:0000313|EMBL:EGV95477.1}
RP NUCLEOTIDE SEQUENCE.
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan C.H., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary CHO-K1 cell line.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSCGRP00001002738.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [4] {ECO:0000313|RefSeq:XP_027275283.1}
RP IDENTIFICATION.
RC STRAIN=17A/GY {ECO:0000313|RefSeq:XP_027275283.1};
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_027275283.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR EMBL; JH000504; EGV95477.1; -; Genomic_DNA.
DR RefSeq; XP_003504767.2; XM_003504719.3.
DR RefSeq; XP_027275283.1; XM_027419482.2.
DR STRING; 10029.G3HM53; -.
DR PaxDb; 10029-XP_007621636-1; -.
DR Ensembl; ENSCGRT00001003749.1; ENSCGRP00001002738.1; ENSCGRG00001003112.1.
DR GeneID; 100752439; -.
DR CTD; 10994; -.
DR eggNOG; KOG1185; Eukaryota.
DR GeneTree; ENSGT00940000158035; -.
DR OMA; QETDMIG; -.
DR OrthoDB; 1328249at2759; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR Proteomes; UP000694386; Unplaced.
DR Proteomes; UP001108280; Chromosome 5.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
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 GO; GO:0001561; P:fatty acid alpha-oxidation; IEA:Ensembl.
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; 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 Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lyase {ECO:0000313|RefSeq:XP_027275283.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..168
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 273..403
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 467..615
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 632 AA; 68001 MW; 5975310174B99FD4 CRC64;
METPTAAAPA GGFFPSFLLL AFGTLVAAVL GTVHRLGLFY QLMHKVDKTS IRHGGESVAA
VLRAHGVRFV FTLVGGHISP LLVACEKLGI RVVDTRHEVT AVFAADAVAR LTGTVGVAAV
TAGPGLTNTV TAVKNAQVAQ SPVLLLGGAA STLLQKRGAL QAIDQMSLFR PLCKFCASVR
TVRDIVPTLR AAVAAAQSGT PGPVFVELPL DVLYPYFMVE KEMVPAKLPK GLMGRVVFWY
LQNCLTNLFA GAWEPRPEGP LPLNIPQASP QQVQRCVEIL SRAKRPLLVL GSQALLPPTP
ATKLRAAVET LGVPCFLGGM SRGLLGRNHP LHIRQNRSAA LKKADVVVLA GAVCDFRLSY
GRVLNRKSKI IIVNRNRDDM LLNSDVFWKP QEAVQGDVGS FMLKLVEGLQ GQMWASDWAE
ELRNADRQKE QTYRDKAGMP VSQHLNPVRV LQQVEEALPD NALLVVDGGD FVATAAYLVQ
PRGPLRWLDP GAFGTLGVGA GFALGAKLCQ PDAEVWCLFG DGAFGYSLIE FDTFVRHKIP
VMALIGNDAG WTQISREQVP RLGSDVACGL AYTDYHKAAI GLGAQGLMLS RDNEDQVVKV
LREGQQLCRA GHAVVVNILI GRTDFRDGSI SV
//
