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Database: UniProt
Entry: A0A091VNS8_OPIHO
LinkDB: A0A091VNS8_OPIHO
Original site: A0A091VNS8_OPIHO 
ID   A0A091VNS8_OPIHO        Unreviewed;      1348 AA.
AC   A0A091VNS8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Phthioceranic/hydroxyphthioceranic acid synthase {ECO:0000313|EMBL:KFR04123.1};
DE   Flags: Fragment;
GN   ORFNames=N306_00674 {ECO:0000313|EMBL:KFR04123.1};
OS   Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC   Opisthocomus.
OX   NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR04123.1, ECO:0000313|Proteomes:UP000053605};
RN   [1] {ECO:0000313|EMBL:KFR04123.1, ECO:0000313|Proteomes:UP000053605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR04123.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KK734122; KFR04123.1; -; Genomic_DNA.
DR   STRING; 30419.A0A091VNS8; -.
DR   PhylomeDB; A0A091VNS8; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000053605; Unassembled WGS sequence.
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; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
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; 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; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 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; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053605};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..193
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFR04123.1"
FT   NON_TER         1348
FT                   /evidence="ECO:0000313|EMBL:KFR04123.1"
SQ   SEQUENCE   1348 AA;  150173 MW;  99F86F9D83BCF86D CRC64;
     RGEGCGVVFL KPLKKAKEDY SKIWGVISIS AVNQNGRSVT PITRPSQIEQ EKLLHSIYGT
     RVDPSVVQYI EAHGTGTAAG DPTEAESLCN VICKNRSTQV SILKIGSVKG NIGHTESAAG
     AAGLIKVLLM MHHGKIVPSL HYSKEVSSID TEKLNLAIPT AVEPWEESSE YGRVAGINCF
     GFGGTNAHIV VRQVKQLEPL PAFKRPLELV LLSAASAKSL QMTMADTADQ LRTRNSVTLP
     SLAYTSACRR SHAGYRYRKA FVTNSLQHLQ QEVMSAASTE LAMSKVEPQL VFVFCGNGVT
     LKEFSEALLS SELVFRDKCR EIEALFQKHA PISLLPARGH SPKDLLNPEL SQPLLFTLQV
     ALASLLKHWG IKPVAAVGHS IGEVAAAHFA GYLSLVDAVK LIYHRSWLQA KTASGRMLVV
     GNIPVQEIAE HLQPYSGKVC IAAFNSPVSC TLSGNSDSVD AVQRDLAQAF CQRNIFLHVL
     NVRAAYHSPS MDMILGQLEE NIQPLEKQKG EIEVISTLTG AAASEKDFAQ GKFWARHTRE
     PVAFTQAIKT AARDRENVVF VEISPHRALH RSIKETLGKD TKVFSSLQTD AEYQTLLTLV
     GNLFELGYNP NWQHFYNGYQ SIPEAIPRYQ FDRKKLMAYL DIHLQPNRRG ISSSHPLVYG
     INSDNIEFGC LLSQDTTSYL YEHKNNGVAL VPGAFYVELA LASVMNSSNP KVPLSACQMS
     ISFSAPCVLT QSSQVLSIKL SPQKAVTTFE ILSSSNAVYA AGQVTKRPEA VVEESTISFQ
     DIYQRCRSVI SREEVYEALS QVGFQYGSIF RQLSDVHYYK ELKEAITSIK VNKETIREMY
     NYCIHPVLLD CFLQMTAVMT SRTLESRAGF PSGIGSLVLL RPLEEDMMIY MRTSKSVGNF
     LEVCGCFMDR RGSVLAELKR VAITFMKQAS SRDNEFMFEN KWKEVSPSQM IGHLGAMPRV
     LVFADKFGIA KQLRKYLHPD SRYVMYEDWE TLMEGHTQNI MRTEVEDYDE ILFMWGIQKL
     NEDFPSKVVD QLAKCCEAYR QVIVALREKT SRCSVRVITY RTTERNVDHI NCGFALYGMT
     RTCVIEVPEI TFQLIDLSSS SSLDISVLAD VLVKYKDVDY PEVYIFRKAS LKELQKTLHM
     WISSMDMKKF RCLSDIPFYE SQKKLFKQNA VYVVVGGLTG LGFETVKFIA ENGGGGIAIL
     SRKIPSNEKQ EEMKALWQQH KGSKIVFVQC DVTLTTDVEK AFQAILNIFA GSPIKGVFQS
     AVVLHDGHLE VLTLADFQKV LSPKVAGTLN LHWATRGQDL DYFVCYSSIT SFLGNSTQAN
     YAAANSFLDI FCLYRRNCGL SGQSINWG
//
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