ID K9MST3_MALDO Unreviewed; 388 AA.
AC K9MST3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=BIS3 biphenyl synthase {ECO:0000313|EMBL:AFX71922.1};
DE EC=2.3.1.177 {ECO:0000313|EMBL:AFX71922.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:AFX71922.1};
RN [1] {ECO:0007829|PDB:5W8Q, ECO:0007829|PDB:5WC4}
RP X-RAY CRYSTALLOGRAPHY (1.17 ANGSTROMS).
RX PubMed=29199980; DOI=10.1107/S2059798317016618;
RA Stewart C., Woods K., Macias G., Allan A.C., Hellens R.P., Noel J.P.;
RT "Molecular architectures of benzoic acid-specific type III polyketide
RT synthases.";
RL Acta Crystallogr. D Struct. Biol. 73:1007-1019(2017).
RN [2] {ECO:0000313|EMBL:AFX71922.1}
RP NUCLEOTIDE SEQUENCE.
RA Stewart C.Jr., Hellens R.P.;
RT "Malus domestica biphenyl synthases.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000256|ARBA:ARBA00005531,
CC ECO:0000256|RuleBase:RU003633}.
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DR EMBL; JQ582626; AFX71922.1; -; mRNA.
DR RefSeq; NP_001315968.1; NM_001329039.1.
DR PDB; 5W8Q; X-ray; 1.17 A; A/B=1-388.
DR PDB; 5WC4; X-ray; 1.20 A; A/B=1-388.
DR PDBsum; 5W8Q; -.
DR PDBsum; 5WC4; -.
DR AlphaFoldDB; K9MST3; -.
DR SMR; K9MST3; -.
DR GeneID; 103456250; -.
DR KEGG; mdm:103456250; -.
DR OrthoDB; 883077at2759; -.
DR BRENDA; 2.3.1.177; 3164.
DR GO; GO:0033815; F:biphenyl synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0019748; P:secondary metabolic process; IEA:UniProt.
DR CDD; cd00831; CHS_like; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR012328; Chalcone/stilbene_synt_C.
DR InterPro; IPR001099; Chalcone/stilbene_synt_N.
DR InterPro; IPR011141; Polyketide_synthase_type-III.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11877:SF108; CHALCONE SYNTHASE-LIKE; 1.
DR PANTHER; PTHR11877; HYDROXYMETHYLGLUTARYL-COA SYNTHASE; 1.
DR Pfam; PF02797; Chal_sti_synt_C; 1.
DR Pfam; PF00195; Chal_sti_synt_N; 1.
DR PIRSF; PIRSF000451; PKS_III; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5W8Q, ECO:0007829|PDB:5WC4};
KW Acyltransferase {ECO:0000256|RuleBase:RU003633,
KW ECO:0000313|EMBL:AFX71922.1};
KW Transferase {ECO:0000256|RuleBase:RU003633, ECO:0000313|EMBL:AFX71922.1}.
FT DOMAIN 11..223
FT /note="Chalcone/stilbene synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00195"
FT DOMAIN 233..383
FT /note="Chalcone/stilbene synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02797"
FT ACT_SITE 159
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000451-1"
SQ SEQUENCE 388 AA; 43022 MW; 4285AF3501423239 CRC64;
MAPLVKNEPQ HAKILAIGTA NPPNVYHQKD YPDFLFRVTK NEHRTDLREK FDRICEKSRT
KKRYLHLTEE MLKANPNIYT YGAPSLDVRQ DICNIEVPKL GQEAALKAIK EWGQPISRIT
HLIFCTASCV DMPGCDFQLI KLLGLDPSVT RTMIYEAGCY AGATVLRMAK DFAENNKGAR
VLVVCAEITT VFFHGLTDTH LDILVGQALF ADGASAVIVG ANPEPEIERP LFEIVACRQT
ILPNSEHGVV ANIREMGFNY YLSGDVPKFV GGNVVDFMTK TFEKVDGKKK DWNSLFFSVH
PGGPAIVDQV EEKLGLKEGK LRATRHVLSE YGNMGAPTVH FILDEMRNKS IEEGKTTTGE
GLEWGVVIGI GPGLTVETAV LRSESIRC
//
