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
//