UniProt: A0A0A8UV81

Database: UniProt
Entry: A0A0A8UV81_LEGHA

LinkDB:  A0A0A8UV81_LEGHA 
Original site:  A0A0A8UV81_LEGHA

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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 (24)   
   Pfam (9)   
   PROSITE (5)   
   SMART (5)   
All databases (50)   

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ID   A0A0A8UV81_LEGHA        Unreviewed;      2599 AA.
AC   A0A0A8UV81;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:CEK11022.1};
GN   ORFNames=LHA_1995 {ECO:0000313|EMBL:CEK11022.1};
OS   Legionella hackeliae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=449 {ECO:0000313|EMBL:CEK11022.1, ECO:0000313|Proteomes:UP000032803};
RN   [1] {ECO:0000313|Proteomes:UP000032803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC35250 {ECO:0000313|Proteomes:UP000032803};
RA   Gomez-Valero L.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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}.
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DR   EMBL; LN681225; CEK11022.1; -; Genomic_DNA.
DR   RefSeq; WP_052673660.1; NZ_UGOC01000002.1.
DR   STRING; 449.LHA_1995; -.
DR   KEGG; lha:LHA_1995; -.
DR   PATRIC; fig|449.7.peg.2151; -.
DR   HOGENOM; CLU_000022_71_0_6; -.
DR   OrthoDB; 9778690at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000032803; Chromosome I.
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   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd05931; FAAL; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation 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; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR049490; C883_1060-like_KR_N.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR040097; FAAL/FAAC.
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; IPR020806; PKS_PP-bd.
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; PF00501; AMP-binding; 1.
DR   Pfam; PF21394; Beta-ketacyl_N; 1.
DR   Pfam; PF00668; Condensation; 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; 2.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
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; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
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          576..653
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          666..1093
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2061..2139
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2599 AA;  291734 MW;  94049C8E34A2C301 CRC64;
     MREKVTNITL IDILKSRVET FPDKLVYTFL SDKEEYLITN AELLQKVRGV ASCLLPKISS
     GSRAILLLQP SLDYIIAFLG CLMAGITAIP AYPPSNTRHT QRLYSVIADA SASVMITTTP
     VSNQYCFENL QLFLIDHPEM VDIDEEKFPI ITQDTLAFLQ YTSGSTGNPK GVMISHGNIL
     ANANVISKLL NRSVRKVCSW LPPFHDMGLI GGILYPLTVD ADVILMAPTR FLRKPFLWLK
     AISDHQVDTS PAPNFAYELC INTITEEEKA QLDLSHWRIA LNGAEPVNAK TLEKFAQAFA
     SCGFKAESCY PTYGMAETTL MVSGKKPTGK TVVLHVDKEA LKRNEIKKVE DTYPSKISLV
     SCGKVDSDHK VNIIVPGTNQ VLGFYEIGEI TIAGPIVAQG YWNKPELSEQ QFRLRLQNNE
     EFFLKTGDLG FKDENGELFI TGRLKDLIII RGQNIYPQDL EASVAESHRQ LIPSGTAAFA
     LESEEDYELV IVQEVHRHAK NFDEIFSAIL KCCSEEFSIL PSKIVFIQQS TLPKTSSGKV
     QRNLCKQALL NNELKIIAQW QRGFEQGPSD SGQSSQQIDE LQRWMKQWLS SELKIDEQQI
     IPTINFAHYG IDSLKAVRFC VALEEKLKTK INPSLLWTYS TIEQLAGYLM GGLPENETVQ
     LHNAHFEPIA IIGMSCRFPG QVDNPETFWQ LLENGRDGIT EIPSERWNIA DYYDPKPATP
     GKMISRKGGF IDNIDKFDAT LFNISSSEAN EMDPQHRLLL ELTWEALECS GIPPLSLDNT
     SSGVFVGISS NDYSHLKLNF YAQDVNGFYG LGNAHSAAAG RIAYFFGTRG QAFAVDTACS
     SSLVAVSNAC RDLQTNSCDL AIAGGVNLIL EPSLSISFSQ AGMLSPDGKC QVFDANANGY
     VRSEGGGVVI LKRLSDAKRD RNKILAVIKS AVVNSDGHSN GITAPSPVAQ KELITKAIHL
     ANLPIDAIGY VEAHGTGTRL GDPIEFNALK DIFATGSRET PLCIGSVKTN IGHLEAAAGM
     AGLIKTILIL QHKKIPANLH FNQVNPLIDL DQIPARVPVN LESWETTATY PIRYAGVSSF
     GFTGTNAHLV LEEAPQSIEQ PTTTPERPVH ILTLSAHSQD ALKAQRSNLL ALLEHEKMLN
     LPSLCHSLNT ERSHLDFRLA VYAQTVDELK INLQNASIQS MPPCGLKKIA FLFTGMGSQY
     SEMGKQLYRT QPVFKAEVDY CCRIVNEYFP ECMQEVMFNP QKGTFLQESE YSQPALFILE
     YALARLWLHW GIKPTAVIGH SLGEYVAATI AGMMRIEDGL KLIVWRARLM QMQKPGAMLA
     LVVDGNKAQE LLKIVHNEIP DAILAIAAIN SKTQTVFSGD MTAISRLESF CQTLKIKTTK
     LDVAHAFHSE LMQPMIREFT QIANTITYSK PTMLVISNVT GKALESIDGH YWAEHVLAKV
     NFSVGINELI KENYTIFFEM GPQPVLLSFA MAHHPTPDEA LWLTSLKKGQ KDWDILSGTL
     VSIYRMGIDI DWFSFDNPYQ IKPCPQVLPT YPFQRQRYWL PLDKSDNKRP EKDYLEQVLN
     KSVYQIGWEK LSSPMAIVNN KSELWLIFAN EENTDTLEKM CSDLDNVIVV KPGEIYSENK
     NSVTLNPIDV SHFQQLLNNI SLPFSVIYFW GFQKNKVSSL SNKEFNNFLQ RACSGMLNLG
     QALATAKNIN KIWVATSAAL SPFKAEYMPL SMTLVGMCKT LVLEYPKLDC QLVDFESGAT
     GEEVANHLLQ LIGRNYEELV IAVSQNNYYA QRLDDYTLKL SRNKVINAEA SYLITGGFGG
     IGFTLCQWLI QQGARFIVLL GRRELNGIQE QLDTLVTAGV TISYFQADVS NFKQLKNTLL
     SVQQKMPAIE GIFHTAGVLA DSLWLSLNWT HFEDVFQAKI QGSWNLHCLS IELKLNLRHF
     ILFSSISSLL GSSGQANYAA ANAFLDGLAH YRHQLDLPAL AINFGPWERL GMTRRQNQSW
     LEVGIQNIPV QEGMATLEAM MSSSATELCL LPHTVSENKL RAFPRSHRKL LSRIVQTEKI
     QKVNDEPWQN LKDLSKEEQL LYINDVLFTA IQKILHLPEN KPITGDNTLL SLGMDSLLAV
     DLLHKLKAKL PPEVNLTAQV LLYENHSIYT LIEVIQQQLS SVKQTRSDSN VLMPPNSQFM
     QLSLQQVRIW RHIQQQPDNP AYVVSYSLEL NGIIDADILE QSIQAVINRH DMLRCSFHSY
     LGNIFQYCHE KVAFNLDRLD FSKLSDEEHD LYIEKQLRQV GHQQFDLAQA PLFKSTLIQC
     ARERALLTVN ISHLLTDGAS SLIVLQDILH FYHLYLTHSY TSLPAAVPYQ CFINWQLLNL
     VNGNYQHYAN FWREKLKNFN PPQLPVDKER QMSMTPQVGS KEIIPVTIRQ LKALQHMVKQ
     NQTTIATVLL AIYGLLLTNM ANTTHAFVTV LVSGRDLEDY KTTVGNIANE VPSILHCKPE
     YSFIEFIHKI QDDFAKSLPY QYFQPEQMVE LDLPVPDTSF DFQVLQPEQF DVGFSMKPVC
     LKQPNIPLWG EKPRKLSLKW TYDGSLSGYI KYRSDLYNTE TIVDFVQQFL KVLAEIIKNP
     TITCKELIAL SKEIRVWKG
//

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