ID A0A0L9UW85_PHAAN Unreviewed; 563 AA.
AC A0A0L9UW85;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=2-hydroxyacyl-CoA lyase {ECO:0000313|EMBL:KAG2391396.1};
GN ORFNames=HKW66_Vig0128430 {ECO:0000313|EMBL:KAG2391396.1},
GN LR48_Vigan07g082400 {ECO:0000313|EMBL:KOM47120.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM47120.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
RN [2] {ECO:0000313|EMBL:KOM47120.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:KOM47120.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG2391396.1, ECO:0000313|Proteomes:UP000743370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG2391396.1};
RA Xiang H.;
RT "Vigna angularis (adzuki bean) Var. LongXiaoDou No. 4 denovo assembly.";
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
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; JABFOF010000007; KAG2391396.1; -; Genomic_DNA.
DR EMBL; CM003377; KOM47120.1; -; Genomic_DNA.
DR RefSeq; XP_017430348.1; XM_017574859.1.
DR AlphaFoldDB; A0A0L9UW85; -.
DR STRING; 3914.A0A0L9UW85; -.
DR EnsemblPlants; KOM47120; KOM47120; LR48_Vigan07g082400.
DR GeneID; 108338133; -.
DR Gramene; KOM47120; KOM47120; LR48_Vigan07g082400.
DR KEGG; var:108338133; -.
DR OMA; PGPYGCL; -.
DR OrthoDB; 1966690at2759; -.
DR Proteomes; UP000053144; Chromosome 7.
DR Proteomes; UP000743370; Unassembled WGS sequence.
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:KAG2391396.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 9..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 398..546
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 563 AA; 60410 MW; DB90B29D20E57E02 CRC64;
MEIDGNVLAA KSLVRFGVRH MFGVVGIPVT SLANRAVALG VRFIAFHNEQ SAGYAASAYG
YLTATPGVFL TVSGPGCVHG LAGLSNASIN TWPTVLISGS CDQADVGRGD FQELNQIEAT
KPFSKLSVRA SHISEIPARV AQVLEWAQSG RPGGCYLDLP TDVLHQKISE SEAEKLLTEV
EKNRAKPEPY SISNSKIEEA VSLLRRAERP LIVFGKGAAY ARAEHVLTKL VETTGIPFLP
TPMGKGLLPD THALAATAAR SLAIGKCDVA LVVGARLNWL LHFGEPPKWS KDVKFILVDV
SEEEIELRKP HLGLVGDAKQ VIEVLNKEIK DDPFCLGNTH PWVQAISNKA KDNVAKMEVQ
LRKDVVPFNF LTPMRIIRDA IADLGSPAPI VVSEGANTMD VGRSVLVQTE PRTRLDAGTW
GTMGVGLGYC IAAAVASPDR LVVAVEGDSG FGFSAIEVET LVRYQLPVVV IVFNNGGVYG
GDRRRPEEID GPHKGDPAPT DFVPNAGYHA LIEAFGGKGY LVGMPDELKF ALSESFSARK
PAVINVVIDP YAGSESGRMQ HKN
//
