ID A0A066RSZ3_9GAMM Unreviewed; 1465 AA.
AC A0A066RSZ3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KDM90807.1};
GN ORFNames=EA58_15590 {ECO:0000313|EMBL:KDM90807.1};
OS Photobacterium galatheae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=1654360 {ECO:0000313|EMBL:KDM90807.1, ECO:0000313|Proteomes:UP000027192};
RN [1] {ECO:0000313|EMBL:KDM90807.1, ECO:0000313|Proteomes:UP000027192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2753 {ECO:0000313|EMBL:KDM90807.1,
RC ECO:0000313|Proteomes:UP000027192};
RA Machado H.R., Gram L.;
RT "Draft genome sequence of Photobacterium halotolerans S2753: a solonamide,
RT ngercheumicin and holomycin producer.";
RL Submitted (APR-2014) 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:KDM90807.1}.
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DR EMBL; JMIB01000028; KDM90807.1; -; Genomic_DNA.
DR RefSeq; WP_036754422.1; NZ_JMIB01000028.1.
DR STRING; 1654360.EA58_15590; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000027192; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 1.10.287.1960; -; 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; 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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 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 SMART; SM00823; PKS_PP; 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; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 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 3..411
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1381..1456
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1465 AA; 158392 MW; D4ADD3CA672D33AF CRC64;
MSSSKVAVIG YGLRVPEAQD ADAFWEIISK GMDVVTRASS NVGATASDRV HAYGLLEGFE
QFDAEYFEYS PREAEDIDPQ QRLLLHCAVE ALESAGVSPK KIPYDIGVWA ASGLSGYLLH
TLDHSRSGMD ATSQLMGGDG HYAATRISYK LGLTGPAMAV GSACSSSLLA IHSAAQAILN
GETDLALAGG MDIEFPQPMS YLFQDGGILS SDGVCRPFDS AANGTVFGSG GGLVLLADLD
TALKEGWPIL AEIAGSAANN DGSDKASFSA PKPSRQADVI SQALTVAELS PEDVGFIECH
GTGTLLGDQS ELEALASVFG HESGIVLGSA KANFGHLRVG AGVIGFIKAC ETIAHGEMAP
MANLSHPVNA VAEHGFIVEP AAKALNFDQR KAAGVSSFGF GGTNVHVVLK QNSTRVFKDS
QGSTDAAVIL PVSSTSPDSC ISNGIALSDF IERQEGIDLG SVSHTLCQGR EHGKYRLAAI
AADVASAVRG LHAAPDASVE GWVAEKNAVV FLFSGQGTSL MNLARGLWNW EPVFTEKLVE
LATYAGLDRT ALAQAISGQA SLPLGIEHAL HVAVQMAIVA QLRARGVTEA YTAGYSLGEY
AAAAVGGAVD EKAVIEVLLK RGEVLAQAPQ GHMFMVASSP EEIKRFAPRT FTAARIGETR
TLISCHPDSA NEVRESLSAA GIVFIELDMG LPYHSPLLAD AAEQFNLICQ SAEPNVESHW
IPTLNSSRSN DRAYWSRHLE STIDFRVVGK KLSTLTQSER ILLIDFSDDG FLSRATSESI
SLNETIPLSL SGKKSDTRKA YLRVLSQLWV SGCDIHIGTS ETATPELSQS MMRLPARRWE
CQPYLKASQS SMNESVSVKK GHRKVQREAS IEKWVYQPSW TLKMRSPELG EISEQRWLVF
TRNNPLSQSL VSRLESAGVD CVCLPIEQFT FQDDAAIQGI IGQLNLEQTP FDRIVHLWCS
DETSTPTDLE PRLSFLNAEL EQGFYTLLFA LQEITERQGA HPLQLDIVAH GIHPLDSAES
VPERALLLGA SIVLPQDYPF ITGRSIDISD LTADRLVDDV FDELSTMQVD HAVALFRQQR
WVRTYERDVL PDLPKDEMPL RLRKQGVYLI TGGLGGIGMT LAEFLVKQCQ ARLVLTGLES
IPSDDSSDDP LICQRKEQIK KLEALGGQVL AVKCDAADPG DTARLLDEID TRFGGLNGVI
HAAGVFETQR AFKSIAETGR EDCIRRLLPK VQGTLVLAAH LKGRKLDFVI TQSSLSSQLG
GLGFYAYTAG NAFMDAFTER QRNQDIPWMT VNWDGWIFRE RGDDAPHQSV VSPSFASPDF
GVVAEIAVRP SEGAEIYARL MHTKHPRQVL ISTANFNERI SQWVNSSHHE KTEVVLKNAQ
SWDDPVARKV ADAWGEILGV DELQPESNFF AVGGDSLLGV SLAHRLSVEF NVVLSAITLF
ENATIDQMVS VIKKASHHSG KEIES
//
