ID F7C8Z1_MACMU Unreviewed; 660 AA.
AC F7C8Z1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 76.
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:ENSMMUP00000010154.4,
GN ECO:0000313|VGNC:VGNC:73739};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000010154.4, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000010154.4}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000010154.4};
RG Ensembl;
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 AlphaFoldDB; F7C8Z1; -.
DR SMR; F7C8Z1; -.
DR STRING; 9544.ENSMMUP00000010154; -.
DR Ensembl; ENSMMUT00000010824.4; ENSMMUP00000010154.4; ENSMMUG00000007729.4.
DR VEuPathDB; HostDB:ENSMMUG00000007729; -.
DR VGNC; VGNC:73739; ILVBL.
DR GeneTree; ENSGT00940000158035; -.
DR HOGENOM; CLU_013748_3_3_1; -.
DR InParanoid; F7C8Z1; -.
DR OMA; QETDMIG; -.
DR TreeFam; TF354221; -.
DR Proteomes; UP000006718; Chromosome 19.
DR Bgee; ENSMMUG00000007729; Expressed in ileum and 21 other cell types or tissues.
DR ExpressionAtlas; F7C8Z1; baseline.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
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 GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
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 Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 81..196
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 301..431
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 495..646
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 25..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 71303 MW; 00ABF9A19206C49C CRC64;
MKGEGRRGLC ARRPVEARLF RVAPERGSDC AHAHRAGLRG AAEPSGRPGQ GRAPGSRDTE
LAEFCRRQRH SLEVDKASVR HGGENVAAVL RAHGVRFIFT LVGGHISPLL VACEKLGIRV
VDTRHEVTAV FAADAMARLS GTVGVAAVTA GPGLTNTVTA VKNAQMAQSP VLLLGGAAST
LLQNRGALQA IDQLSLFRPL CKFCASVRRV RDIVPTLRAA MAAAQSGTPG PVFVELPIDV
LYPYFMVQKE MVPAKPRKGL VGRVVSWYLE NYLANLFAGA WEPQPEGPLP LDIPQASPQQ
VQRCVEILSR AKRPLMVLGS QALLTPKSAD KLRAAVETLG VPCFLGGMAR GLLGRNHSLH
IRENRSAALK KADVIVLAGT VCDFRLSYGR VLSHSSKIII VNRNREDMLL NSDVFWKPQE
AVQGDVGSFV LKLVEGLQGQ TWAPDWVEEL READRQKEQT FREKAAMPVA QHLNPVRVLQ
LVEETLPDNS ILVVDGGDFV GTAAHLVQPR GPLCWLDPGA FGTLGVGAGF ALGAKLCRPD
AEVWCLFGDG AFGYSLIEFD TFVRHKIPVM ALVGNDAGWT QISREQVPSL GSNVACSLAY
TEYHKAAMGL GARGLLLSRE NEDQVVKVLH DAQQQCRDGH PVVVNILIGR TDFRDGSIAV
//
