UniProt: H0IYL3

Database: UniProt
Entry: H0IYL3_9GAMM

LinkDB:  H0IYL3_9GAMM 
Original site:  H0IYL3_9GAMM

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Ontology (4)   
   GO (4)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (43)   
   InterPro (23)   
   Pfam (10)   
   PROSITE (3)   
   SMART (7)   
Literature (1)   
   PubMed (1)   
All databases (51)   

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ID   H0IYL3_9GAMM            Unreviewed;      2453 AA.
AC   H0IYL3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:EHK62226.1};
GN   ORFNames=MOY_02269 {ECO:0000313|EMBL:EHK62226.1};
OS   Halomonas sp. GFAJ-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1118153 {ECO:0000313|EMBL:EHK62226.1, ECO:0000313|Proteomes:UP000004512};
RN   [1] {ECO:0000313|EMBL:EHK62226.1, ECO:0000313|Proteomes:UP000004512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK62226.1,
RC   ECO:0000313|Proteomes:UP000004512};
RX   PubMed=22408239; DOI=10.1128/JB.06664-11;
RA   Phung le T., Silver S., Trimble W.L., Gilbert J.A.;
RT   "Draft Genome of Halomonas Species Strain GFAJ-1 (ATCC BAA-2256).";
RL   J. Bacteriol. 194:1835-1836(2012).
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:EHK62226.1}.
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DR   EMBL; AHBC01000006; EHK62226.1; -; Genomic_DNA.
DR   RefSeq; WP_009096070.1; NZ_CP016490.1.
DR   STRING; 1118153.MOY_02269; -.
DR   KEGG; hag:BB497_09770; -.
DR   PATRIC; fig|1118153.6.peg.450; -.
DR   eggNOG; COG0604; Bacteria.
DR   eggNOG; COG3321; Bacteria.
DR   OrthoDB; 9778690at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000004512; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase 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; cd05195; enoyl_red; 1.
DR   CDD; cd08955; KR_2_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; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
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; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR020843; PKS_ER.
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:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 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; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
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.
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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004512};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..422
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2336..2413
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2453 AA;  265421 MW;  30458278220E0998 CRC64;
     MTKRVAIIGA AHRFPGTTPE TFWQDLQAEK DLVTQVAPDR WSHDAYWHPD KRHPGTSVTF
     SAGSLGDISG FDAAFFGISP REAANMDPQQ RMLLELAWEA MESAGIVPSS LRGSQCGVFL
     GVASLDYSYR MADDMGAIDA STATGNTSSI ASNRLSYVFD LHGPSMSLDT ACSSSMVAFH
     QACQSIRSGE TTMALAGGIS LHLHPYGFII FSKASMLSPT GRCQVFDDAG DGYVRSEGAG
     LFLLKDYDLA VSDGDNILAV VAGSAVNTDG HKSGLTVPNP SAQIDLMRRA YEQAGISPDE
     IDYLEAHGTG TAVGDPIETR AIGEALGKHR KTPLLIGSVK SNVGHLETAS GVAGLAKALY
     SLQHREVPAT IGIRKLNSRI KFDEWNISVV TKAQPLKPQG RLVIGVNSFG FGGANAHVIL
     ESAPEKNTVP SHTSADALPI RLSARSQEGL VANAQALAAY LRDSEHSFYD IAHTLYHHRE
     QHTFGALYFA HTPTDAADAL SQFAEGEEAT AGQENSVTTL ERLADACGPV FVYDGNGCQW
     ETMGHDLLES DAVFSSAIDR VDTLFQQYGD FSLRDELAGR NQLDGAESRF ARTEIAQPAL
     FALQVALTEW LSAQGITPAA VFGHSVGEVA AAWASGALSL EDAVKVIYYR SYYQGKTRGL
     GEMSAVAMSA DEIAPWLEKP EYQRISLAGI NSPKGITLAG DRDQLSALEA ALSDQNIFAK
     RLPLDYAFHS PAMDSIEADV VEALADISPQ TTQIPYISTV TGTTSEGSAL GAHYWWLNIR
     EPVLFDNAAT VLMEQGFNVF VEVGAHPILR RYLNESLRQQ ERDGLVVGTI ERHKPGHEGL
     NRCLSQLLLS GLSLDSRRFF PVEGQRVLLP RYAWQRTHYW VQGTNDGQNL LLRYYQHPLL
     GYPLAQQEHT WESQLDTKRQ PWLADHVVGE GAVFPGAGFV ELTLAAALQQ KDTPLLDIEE
     LEIRAPLLLD GPNGRTMRLT LNPDDGRLAI HSREPATGTE WQLNAVARRM RESRGFLLSR
     QAPTLPTRAP DYTLDEHLQM AERIGLHYGP AFQAISRGWI EGDSVIGEVH LSEVMQGQLD
     TLHVHPGILD SAFQMFIPLL AQHSEFAAQL AFVPVRVGRI QVNAEAGVPV VARAVMGKRA
     PHSFTADFEL FDAAGNAVAV LRETRFKAIR LNRAHHQHFS YLDVELTPAP LDAATLALPA
     EALSRLAGLS DAYAHQTGQR YAQEVAPLLD SLSEAFAQQN SEQATDENEQ LPPDIIWQLL
     VQDYPDYFAP IHLVGRLGLH REQLTNGSAE LESLGITTEH LAGINRVLIG ESGWQVLATE
     LGALMEATLA TLPTGQRLQL LEAGPCAPAL GQRLLEQLAN ARHIAKDAHH YRAITTSDTA
     RHQAEQLQER FPLMDIQPLE DTLPLLACAE KAQLAFISVD VTQPERTRQL IDALPAQLSP
     GAQVMVVGIS PSRWLDDVLA TPGIDQTALE QSTLSDWLNN QGFRVSPPIA LEEGDTGAYL
     LHAQYTHAQK PTASPLPAAR HVVVANHAQE ALATQLAAQL DELSGTANAW LRISDATPQA
     LLDEALAENN ELFTVLNVID LRGLGAATTA AQTQRCHSAQ QWSLALEASG LEGQGSRVTL
     WLPTQEASTS DDAALWGFGR SLANEAVGHL VTLIDVPSAP SAATLATFAA SVTTPDNENE
     LVITQAGTRL ATRLRTLPAP HPLHAQETTP HQAMTLGFAL PGQLRQLQWR PRPLPALGAD
     EVEIRVKATG LNFRDVMYTL GLLSDEAIEN GFAGPTLGLE FSGDVIAVGE NVSHVAPGQA
     VVGFGPASFS DRLIASQHAV APLPDGISYA AAATIPTTFF TVYYALKHLA RLEPGEKVLI
     HGAAGGVGIA ALQIAQWLGA EIYATVGSEE KRDFLRLMGV EHLYDSRSLT FAEEILQDTQ
     GEGVDIVLNS LAGEAINQNL RALRPFGRFL ELGKRDFYEN THIGLRPFRN NLSYFGIDSD
     QLMKVQPALT QRLFGEMMAL FNEGTLSPLP FTAFSHSQVI DAFRYMQQAR QIGKVVVTYE
     QPIAPPKNEV LGTAAMQLPA HASYLITGGL GGFGLKTAQW LVSKGARQLI LVSRSGPASE
     EAQAAISEFE AQGVTVLATA CDITDRDALA KVLARAQHEL APLRGIVHAA TVIDDGLIRN
     LDAARIQKVL APKIEGARHL DALTREAELD FFILYSSATT LFGNPGQANY VAANHWLEAF
     AARRRAEGMP ATCVRWGAIE DVGFLARNTR TRDALQERLG GSALRSDDAL KVLEQMLITP
     GASLGVLELE WGALARFLPT ANAPRFTEIA RASDDDGSVD SNDDISALLA DLSPEELHST
     VTDLLRAELA SILLIDEEKI DVNRSVYDMG FDSLMGVELM TAIENRLGVQ VPVMVLSEAS
     TLNKLAGVLI QKLHQHDDDV EEAPQDALAS LAARHGADGL THESASSPVT ETP
//

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