ID A0A0F6AGB6_9GAMM Unreviewed; 1455 AA.
AC A0A0F6AGB6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KKE85213.1};
GN ORFNames=N479_05630 {ECO:0000313|EMBL:KKE85213.1};
OS Pseudoalteromonas luteoviolacea S4054.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1129367 {ECO:0000313|EMBL:KKE85213.1, ECO:0000313|Proteomes:UP000033434};
RN [1] {ECO:0000313|EMBL:KKE85213.1, ECO:0000313|Proteomes:UP000033434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4054 {ECO:0000313|EMBL:KKE85213.1,
RC ECO:0000313|Proteomes:UP000033434};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KKE85213.1}.
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DR EMBL; AUXW01000068; KKE85213.1; -; Genomic_DNA.
DR RefSeq; WP_046354582.1; NZ_AUXW01000068.1.
DR PATRIC; fig|1129367.4.peg.746; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000033434; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..430
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1377..1452
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1455 AA; 156087 MW; 02FDE503C2FA9E37 CRC64;
MSESNYSELD IAIVGMAGRF PDADDVDQLW QNVRDGHCAV KTFDDNSLKA AGVSDEDLAH
PDYIKRGIPF AGMAQFDAAF FGYTPKEAAQ LDPQQRVFLQ TCWHALEHAG ITTDTSNFTG
VFAGCGVTAY LLQNLLGDSQ QDITSLLALT NGNDKDSLAT RISYELDLTG PAVTVQTACS
TSLVAVHMAC RSLQNYECDS ALAGGVWLNL NNEQGYHAPT GGSLSPSGQL SAFGEQADGI
LIGSGSAAVV LKRVEDAIEA GDHILAVIKG SAINNDGKEK VGYTAPSVTG QASAIEAALE
FADIEPSSVG YIETHGTGTT LGDPIEIAAL SRAYGECDKQ QIAIGSIKAN IGHLDSAAGV
TGLIKAVQAL RHKTLPPSLH CEPLNSKIDF ANSPFYVNTT LTPWESDSVR RAAVSSLGMG
GTNAHVILEE YRANETQHSY TSPWHILPVS ANSQSALEAQ RQALVIKLQQ NPDDLALIAA
QSQHNRTAQA VRHALVVDNA EQAQQLLVRD VAGDKAGAVQ VALMFSGQGS QYVTMAKPLL
EHMPEFKAQF DDVIALFDST LQDELRRVFT PNDDELLAAN QLLGQTRVTQ PALFVVAYAM
AKCYQAHGIH IEAMLGHSIG EYVAACLSEV MSLDTAVKLV TARGEALQKM APGAMLSVMS
DAPSLQPYLN AQLDIAACNS PTNTVVAGAK EAIKALQTEL KAADISVTRL HVSHAFHSHL
TEPVLGEFAE VLNTVQLNAP QTPFVSNVTG TWISPEQATS TQYWLDHIRQ AVNFVDGVKT
LAAKCNVLVE AGPGDTLQKL AKQSIADDIT VLNSIAHARD LKAPIPPCVK TLAKLWQLGV
AIDWSVVSSN PHGLEMAFPA YQFDSTEYWI DATHSTAPVT TQAHSTGPEL LAPVWQQQLN
TISVLSQFNG EKVLVIATDA PILSQLTNEL RTKGAEVIVA WQGDEFVSLE QGQYRLDCQD
ANQLTALYEQ QSFTRIVDCR LLDESGCGYQ QLLPLAKWLL SQGTLQWTVV ASELFSVLGD
EQISADRATA LGITRVIGME QTAIDCQLRE ITTAQRDSAQ SHIAAQVVAD MANEAKEIAY
RGRQRFVLTE QVLPQTEIAA NTASSPVTFI TGGLGGVGLV LAKLLAAQGH ALMLQTRAEF
PDSEQWPALL VDEHTDSKLI GQIHALQALQ EAGARVAVVT ADVLDIASLN VAISHAEQSL
GRITQVIHAA GLPGGGMLAQ MTSEQAAHSM AAKIRGTDNL LAAFKSHQLE RMILCSSLAS
VLGALGQSDY CAANSYLDAV AMQPQPFLVQ SVNWDAWANI GMAAGHSVGE DFGIDELAAK
TLLDGISQSQ APQIYAASLS WQARADKVAE LTEKLMQAKS AAPKGHKRPD LDTEFEAPES
ELELQLAAIW SEFLGFDEIG IFDNLFELGG DSLIAIQMLA KVKQQFAVEI EPATFFEDPN
LDNLTFLIEE QLLSE
//
