UniProt: A0A3Q3W2M9

Database: UniProt
Entry: A0A3Q3W2M9_MOLML

LinkDB:  A0A3Q3W2M9_MOLML 
Original site:  A0A3Q3W2M9_MOLML

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Ontology (3)   
   GO (3)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (32)   
   InterPro (18)   
   Pfam (8)   
   PROSITE (3)   
   SMART (3)   
All databases (38)   

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ID   A0A3Q3W2M9_MOLML        Unreviewed;      2103 AA.
AC   A0A3Q3W2M9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMOP00000005872.1};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000005872.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000005872.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC         Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449; EC=2.3.1.39;
CC         Evidence={ECO:0000256|ARBA:ARBA00023404};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41793;
CC         Evidence={ECO:0000256|ARBA:ARBA00023404};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194}.
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DR   STRING; 94237.ENSMMOP00000005872; -.
DR   Ensembl; ENSMMOT00000005979.1; ENSMMOP00000005872.1; ENSMMOG00000004608.1.
DR   OMA; IINHCTG; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000261620; Unplaced.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05274; KR_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR45681:SF6; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..429
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2004..2079
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2103 AA;  233020 MW;  9D4E0394BF8A68CB CRC64;
     MEEAEDSIAV IGIGCNFPGG EGLENFWKVL VDGKNCSVPI PRERFDLAGW YDPDDTKAGK
     SCTANAALIE GFNQFDHKFF GISDSEVEQM DPQQKQLLQC VYRALENAGI PMEHASGTRT
     GVFFGLMNRD YETNAAHVHP SIINHWTSTG LAMSIAANRV SYIFNFTGPS LSIDCACSSS
     LVALHLACQS IKQGDCDMAM CGGVNCIIEP RVFVALSKAK MISPEGTSKP FSRTADGYGR
     GEGCGVLLLK PLKKAIQDHD HIWGIISKTA VNQDGHSVTP LTKPSMTQQE ELLRKIYSES
     DLANVQYIEA HGTGTPVGDP TEARSISNVI AKAKIPGSET LRIGSVKSNI GHTESAAGVA
     GLIKVLLMMK HETIVPSLFY SEETACVDAK AFNIKIPREA EKWEASCARI AGVNNFGFGG
     TNAHAIVKQH KQSRIEQKND GRKAKYFVMS ANSPKSLTLM MDDTIKNLET GNQLDLDALV
     YTSACRRSHQ KNKYRKALLV SSVVDLKEKL SATAGRNIKP AYSDPRLVFV FCGNGVTYHG
     MCTQLLKQEP VFKDKIKEIA QLFQRLTTLN ILDTLESEFE VDNLNNPPVV QPLLFAIQVG
     ITTLLRQWGV KPDAILGHSV GEVAAAHCSG LLSLEDAVKV IYFRSTLQNK VTGGKMLVIS
     NMAVSEVSAL LPHYSGRLCL AAFNSPQSCT LSGDADAVDS LHMELSTSAK NQNLFLRVLD
     VAAAYHSHMM DPILTEIRET IGSLQVYDLG TELFSTVTGK EVQQGDFCTG EYWARNIREP
     VALEQAVRSA TKGKKNTVFV EIGPRRALQR NIMESLGDDT TVFASVQPGK DHETVISVVS
     KVFEVGIHVN WNTFYKGHET MPIPIPKYQF DCSDRDAIIG AAQNNTLSSH PVLCQTSESN
     IFSCDLNSDS SFYLKEHKHN GVAIIPGAFY AEVGLAAFMA SARPKVPLSS LQLSVSFHSP
     FVLSQNSPEM RVQLEQTERE ARFMVLSPSA MYASGTVVSK KERLIEEHFI SLSSIYKRCK
     SVVSSQELYG YLSQGGFQYG DVFQNKADVH YGEDLKEAFV VVTVPGELQC QLHDYCIHPV
     ILDFLMQLVP VTVEHIFAGR PGFPAKIGSL TVFEPLQDEM IVYLRAVDLG TDHFEVCGCF
     TDEEGRVLVE VKHVIIKYLG SISHVVEEYF YHNDFSVIPD GTTSALPPKA LVFCDCIGIS
     KGLGQYLDSR SRFVSFTHAK DILRDGFPSL LANLKITDID KNFQEVLFLW GKENLTLLGA
     DVVLQNLASC CEIFRQIVLE LKRIHFPNSI RAVTYCSSDI TVEHVNPGFA LAGMTRSFAA
     EMPDLLFQLI DIDSTSAKDI AALFEVLKSC PCSKYPELVV KDGLILKPGI VRTPPEIIDC
     SEESFTTTMS EQCIFQTADA HKMTQLSAIH FEEETQPLSD TSVEIQPTEI CVHSSDYFPV
     SASHLKFGQT LYWNKYSSQN HKLLALDFCG TITAVGKDVG KLKVGDQVAS CYPVVAASRV
     RVPEDVCYSS KRFPFFQKTP CVSYFVVAWE LLHRALPRTK HKLGIISSVP DSVLMKVLEL
     TAYKYGWNVV VGTQHNGAFA DVNQVTVMVI LPPFDESLIA KICQIPGIQR IILICETKFQ
     SLHAQDIFQI VKESVYVQTI QMPVILQKAY LRAERPHIYQ WLKSLNLSRK FALESFTFQN
     QKSDSLKNQN SENQQSYFNS KKLAVVTLKK NGSNTLSNIP LLPTKKQLFR KRAVYIVAGG
     LSGLGFETVK FISQRGGKFI VILSRSKPTT DVQQDIYNVE KQCGNCITAM ECDVSMSESV
     NKVISAIGLK FPSCPIRGVF HSAVVLHDGL IETLDRSLYE KVLKPKVNGV LNLHHATKEF
     QLDYFVCYSS ISAFLGNASQ TNYAAANTFL DLFCQYRRRL GLPGQSINWG ALNLGLLLNK
     EHFIRFLEAK GIMVLDVSEI HKSLEQCLAL NRPQQVICRF HFRNIRYNIL SQNVALSNRL
     SKLVDEVFQK SKETDSQTKT TQSVSPKDYV VSLLSETISM DKSELKDDSP LSLLGIDSMQ
     AMTLQNLIFQ QRGVNVPLVK LLDPNATIST VSAILKQGDE CEYLSDDLEP FPVEDMNHLI
     TRL
//

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