ID A0A166W3T6_9GAMM Unreviewed; 1457 AA.
AC A0A166W3T6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KZN35380.1};
GN ORFNames=N475_18735 {ECO:0000313|EMBL:KZN35380.1};
OS Pseudoalteromonas luteoviolacea DSM 6061.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1365250 {ECO:0000313|EMBL:KZN35380.1, ECO:0000313|Proteomes:UP000076643};
RN [1] {ECO:0000313|EMBL:KZN35380.1, ECO:0000313|Proteomes:UP000076643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6061 {ECO:0000313|EMBL:KZN35380.1,
RC ECO:0000313|Proteomes:UP000076643};
RA Vynne N.G., Mansson M., Gram L.;
RT "Comparative Genomic and Metabolomic Analysis of Twelve Strains of
RT Pseudoalteromonas luteoviolacea.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZN35380.1}.
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DR EMBL; AUYB01000112; KZN35380.1; -; Genomic_DNA.
DR RefSeq; WP_063365573.1; NZ_AUYB01000112.1.
DR STRING; 43657.S4054249_19840; -.
DR PATRIC; fig|1365250.3.peg.3346; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000076643; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
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; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 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 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; 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; IPR013968; PKS_KR.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 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; PF00550; PP-binding; 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; 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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000076643};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..430
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1379..1454
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1457 AA; 156072 MW; 5FE0EA5BCCD09971 CRC64;
MSENNYSELD IAIVGMAGRF PDANNVDELW QNVRDGKCAV QDLSDAQLRA AGVSEDDLAH
PDYVKRGIPF MGMAQFDAAF FGYTPKEAAQ LDPQQRVFLQ TCWHALEHAG MTTDRSSFTG
VFAGCGVPAY LLQNLLADSQ QDITSLLALT NGNDKDSLAT RVSYELDLTG PAVSVQTACS
TSLVAVHMAC RSLQNYECDS ALAGGVWLNL NNEQGYHAPA GGSLSPSGQL SAFGEQADGI
LIGSGSAAVV LKRVDDALEA GDHILAVIKG SAINNDGKEK VGYTAPSVTG QAGAIEAALE
FADIEPNSVG YIETHGTGTT LGDPIEIAAL SRAYDGCANQ QVAIGSIKAN IGHLDSAAGV
TGLIKAVQAL RHKTLPPSLH CEPLNSKIDF ANSPFYVNTE LKPWHSDSVR RAAVSSLGMG
GTNAHVILEE YVAPEVEYSQ ATPWYLLPLS GNSQAGLDAQ RQALAIKLQQ SPEQLPLIAA
QLQHSRTAHA IRHAVVVDGA EQAQQLLVRD VSGDKATNHK IGLMFSGQGS QYVTMAQPML
KYVPAFKAHF EEVTALFNDA LQDELRRVFI PNDEELLAAN QLLGQTRVTQ PALFVVAYAM
AKCYQSHGVN IEAMLGHSIG EYVAACLSGV MNLETAVKLV TARGEALQKM APGAMLSVMS
DAQSLAPYLN DQLDIAACNS PSNTVVAGTK EAIKALQGEL KAADISVTRL HVSHAFHSHL
TEPVLGEFAE VLEQAQLSAP NTPFVSNLTG TWITAEQAVS TQYWLDHIRQ AVNFVDGVNT
LAQQCDVLIE AGPGDTLQKL AKQSVSDSVI VLNSIAHARD LKAPIPPFVK SLGKLWQLGV
QIEWSEVSEV AQGVEIALPA YQFDKTEFWV DAKAVKASST RVTEHTGPEL LEPIWQQQLC
TVSSPVNLQD QKVVLLASDA PLTTQLSSAL TARGATVIQV WQGQTFSALE QNQYRLDCQD
ASQLNMLHEQ VDGFEQIVDC RLLDEHACGY QLLLPLAKWL LGQGQINWTV VASELFSVLG
DEAVSAEKAT ALGILRVIGM EQTAIRCQLR EVMQTHRDGS QLQFAAQLVA DMANDSQEIA
YRGRQRFVRT QQALPTITTQ EHEVSSSAVT FITGGLGGVG LVIAKLLAAQ GHALVLQTRS
ALPASEQWAA LIADKDSDAK LVGQLTALTA LQDAGVRIAV VQADVLDIAS LNVAISHAEQ
SLGSITQVIH AAGLPGGGML AQMSAEQAAQ SMAAKTQGTD NLLAAFKSHK LERMLLCSSL
ASVLGALGQS DYCAANSYLD AVALQPQPFL VQSVNWDAWA NIGMAAGHSV GEDFGIDEVA
AQTLLAGIGQ SQAPQLYAAS LSWQAREDKV AELTERLMQA KAPAPKGHKR PELDTEFEAP
ESELELQLAA IWSEFLGFDE IGVFDNLFEL GGDSLIAIQM LAKVKQQFAV EIEPATFFED
PNLDNLTFLI EEQLLNE
//
