ID H0YS83_TAEGU Unreviewed; 2056 AA.
AC H0YS83;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Mycocerosic acid synthase-like polyketide synthase {ECO:0000313|Ensembl:ENSTGUP00000001143.2};
GN Name=LOC100231542 {ECO:0000313|Ensembl:ENSTGUP00000001143.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000001143.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000001143.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000001143.2}
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; 59729.ENSTGUP00000032677; -.
DR Ensembl; ENSTGUT00000001155.2; ENSTGUP00000001143.2; ENSTGUG00000001111.2.
DR GeneTree; ENSGT00940000164060; -.
DR HOGENOM; CLU_000022_35_3_1; -.
DR TreeFam; TF300549; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000007754; Chromosome 2.
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; 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; IPR020807; PKS_DH.
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; 2.
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; SM00826; PKS_DH; 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; 2.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..382
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1956..2034
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2056 AA; 226993 MW; 16B6A2DAB0A2CEBF CRC64;
MEAERMDPQQ KLLIECTYKA LEDAGVPVES VSGTKTGVFI GLMNRDYEII TSRDVNEINH
YDGTGTAMSI AANRISFTFN LTGPSLTIDT ACSSFLFALH YALRAIKSGN ETEEVLDNEI
KIFTVSVYHQ GHLNMNICFC LTPGDCEAAI CGGVSCIIDP RTFVSLSKAK MISPDGISKP
FSKKADGYGR GEGCGVVFLK PLKKAKEDHS KIWGVINISA VNQNGRSTTP ITRPSQKEQE
NLLRSIYESR VDPAVVQYIE AHGTGTAAGD PTEAESLGNV ISKNRSSRVP ILKIGSVKGN
IGHTESAAGA AALIKVLLMM HHGKIVPSLH YSKEMSSIDT EKLNLAVATA VEPWEGSSEY
GRVGGINCFG FGGTNAHVVV RQVKQPEPLP AFKKPLELVL LSAASPKSLQ MTMADTAEQL
STRNSVTLPS LAYTSACRRS HASYRYRKAF VTNSLQHLQQ ELKLAASTEP AMSKVEPQLV
FVFCGNGVTL KEFSEALLSS EPVFRDKCKE IEDLFQQHAA ISLLPASNRN PKDLLNPELS
QPLLFALQVA VASLLKHWGI KPVAVVGHSV GEVAAAHIAG YLSLADAVKV IYHRSRLQAK
TASGRMLVVG NIPVEEIAAR LHPYSGKVCI AAFNSPISCT LSGSVEVVEA VQRELAEAFR
QRNIFLHVLN VPAAYHSPSM DVILEELEEQ IEPLERQKGE MEVISTLTGA AASENDFAQG
KFWAQHTRKP VAFTQAIQTA ARGRENVVFV EISPHRALQR SIKETLGKGT KVLSSLQTDA
EYQTLFTLVG NLFELGFNPN WQHFYDGYQS VPVAIPQYQF DHQKLMTCLD MHRQTNQRGV
SSSHPLIYSI NSDNVELGCL VSQDTAPYLY EHKNHGVALV PGAFYVELGL ASVMSRSEPK
VPLSTCQLSI SFSAPCVLTQ NSQVLSIKLS SQKAMTTFEV LSSSNSVYAA GQVAKGLEGV
VEESSISFQA IYRRCRSVIS KEELYEALSQ VGFQYGSIFR QLSDVHYCQE LKEAITSIKV
NEEIARDMYS YCIHPVLLDC FLQMTAVLTS RTLPSRAGFP SGIGSLVVLR PLEEEMMIYM
RMSKSTGNCL EVCGCFVDKH GSVLAELKRV AITFMKESSS RDNEFLFENK WKEVSLSQTI
AHLGFKPRVL VFADKFGIAE QLKKYLHPSS RYVMYEDWEC LVEGDTQNKM RAEVKDYDEI
LFLWGIQKLN EDSPRKAVDQ LAKCCEAYRQ VVVALKEKTS RCSIRVITYR TTERYVDHVN
CGFALYGMTR TCTVEVPEIT FQLIDLSSFT SLDISVLADV LVKYQGGDYP EVCISQGRIY
VSEIRRTPCV GADYIQPVRS LQKSQSFTLF TSDPYTAKDL SGELSTSAAT QLDKQSVEIQ
VDKICLHSED YFPISVSSCS FGNTLYWNSQ AGDKHRLLAL DFSGTVTATG SDVKKVKVGD
HVVSCYPSAA SSRVQIPGTV CLNARKFPFL QNVPCLSYFI TAWEIFTQRL PKGKHGRTLG
IITTEPSSVL CHVLSAAAEE MGWRTVLAKP TPNVFLCINL CSALVILPPV NRLSQEDLAH
MYLLKDVVIV CGSQQSECIQ NVSEIDNENI SFHILAVASL FRKAPLKEVQ KTVHAWISSM
DMKQFRHLSG SVFQQTENFE GLNSVMSYFT CTSVPLAVLG RQKDISVLSD IPLYEPQKQL
FKQNAVYVVA GGLTGLGFET VKFIAENGGG CIAILSRRIP SSEKQEELRA LQQQYKGSKV
VSVQCDVAST SDVEKAFQSI ANTFVGSPIK GVFQSAVALH DGRLEVLKLA DFHKVLSPKV
AGTLNLHWAT RDQELDYFVC YSSVTSFLGN ATQTNYAAAN SFLDVFCLYR RNCGLSGQAI
NWGALNLGIL LNQNYIQSIL RSKGIDILQV HEIHDYLRKT LLINNAQQAV VKLNFQALYN
HVFTQITSLK SRFISLISED FKIKIETFEE TEVPDAAFLK SEDYITSLVS DLTGVNTEEL
TMNTPLSSLG IDSMLAMTIQ NRVFQERKVD IPLVKLLDPH TTLSSLVVVL EERSDANGTV
ENKNAVIENA ENGSWL
//
