ID G0AUI8_9GAMM Unreviewed; 2703 AA.
AC G0AUI8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=Polyketide-type polyunsaturated fatty acid synthase PfaA {ECO:0000313|EMBL:AEG12150.1};
DE EC=2.3.1.94 {ECO:0000313|EMBL:AEG12150.1};
GN ORFNames=Sbal175_2911 {ECO:0000313|EMBL:AEG12150.1};
OS Shewanella baltica BA175.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=693974 {ECO:0000313|EMBL:AEG12150.1, ECO:0000313|Proteomes:UP000002249};
RN [1] {ECO:0000313|EMBL:AEG12150.1, ECO:0000313|Proteomes:UP000002249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA175 {ECO:0000313|EMBL:AEG12150.1,
RC ECO:0000313|Proteomes:UP000002249};
RX PubMed=22328742; DOI=10.1128/JB.06468-11;
RA Caro-Quintero A., Auchtung J., Deng J., Brettar I., Hofle M., Tiedje J.M.,
RA Konstantinidis K.T.;
RT "Genome sequencing of five Shewanella baltica strains recovered from the
RT oxic-anoxic interface of the Baltic Sea.";
RL J. Bacteriol. 194:1236-1236(2012).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467}.
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DR EMBL; CP002767; AEG12150.1; -; Genomic_DNA.
DR RefSeq; WP_006080951.1; NC_017571.1.
DR KEGG; sbb:Sbal175_2911; -.
DR HOGENOM; CLU_000022_30_2_6; -.
DR Proteomes; UP000002249; Chromosome.
DR GO; GO:0047879; F:erythronolide synthase activity; IEA:UniProtKB-EC.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 5.
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 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; 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; IPR004432; Omega_3_polyunsat_FA_synth.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR02813; omega_3_PfaA; 2.
DR PANTHER; PTHR43074; OMEGA-3 POLYUNSATURATED FATTY ACID SYNTHASE PFAB-RELATED; 1.
DR PANTHER; PTHR43074:SF1; PKS_AT DOMAIN-CONTAINING PROTEIN; 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; 5.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 5.
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; 2.
DR PROSITE; PS50075; CARRIER; 5.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:AEG12150.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEG12150.1}.
FT DOMAIN 26..481
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1273..1353
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1374..1454
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1481..1561
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1583..1663
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1690..1770
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2336..2367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2347..2367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2703 AA; 286843 MW; 7BCC0A827E6070B7 CRC64;
MSHTPSVPNS ATESKKDKRL NKRLKDMPVA IVGMASIFAN SRYLNKFWDL ISEKIDAITD
IPDTHWRAED YYDADKSKAD KSYCKRGGFL PEVDFNPMEF GLPPNILELT DTSQLLSLIV
AKEVLADANL PTDYDRDRIG ITLGVGGGQK ISQSLNSRLQ YPVLKKVFKS SGLSDEDSEM
LIKKFQDQYI HWEENSFPGS LGNVIAGRIA NRFDFGGMNC VVDAACAGSL AAMRMALTEL
TEGRSDMMIT GGVCTDNSPS MYMSFSKTPA FTTNETIQPF DIDSKGMMIG EGIGMVALKR
LEDAKRDGDR IYAVIKGVGA SSDGKFKSIY APRPEGQAKA LERAYDDAGF APHSIGLVEA
HGTGTAAGDV AEFNGLKSVF AQGNDTNQHI ALGSVKSQVG HTKSTAGTAG VIKAALALHH
KVLPATINVS QPNPKLNIES SPFYLNTETR PWFQRADATP RRAGVSSFGF GGTNFHLVLE
EYKPEHSRDE QYRQRSVPQT LLFAAANKAA LLSELKAALS QSVNTNANKS SAASLNAIAQ
QYPLRTLAST DARLGFVAKD IAQLQAQLNQ SIAHLETNAI EVWQLPSGIS YRSHALVAQN
ESKKVAALFA GQGSQYLNMG RELACHFPEM RQQVMASDKV FAHHGQTPLS NILYPIPAFD
ADAVKAQEAA LTNTLFAQSA IGAVSMAQYS LLTQAGFAPD MVAGHSFGEL SALCAAGVIS
NEDYVELAFA RGHAMAQVPS DTGTQVDLGT MFAIILKQKN DIDALNSCLA QFDGVKIANY
NAPTQLVIAG GTEQTQLAAK AISELGFKAI ALPVSGAFHT PLVGHAQKPF AKAIDKAKFS
APSVALYANG TGQLHPSDGK AIKAEFKQHM LQSVRFSEQL QAMYDAGARV FVEFGPKNIL
QKLVENTLGE HLNELCLVSM NPNPKGDSDS QLRLAAVQLA VAGVALTDVD PYQAITSQEI
AEREAPSAMN IKLTATNHIS AATKAKMAKS LATGSVTSQV QYVDRIVETV VEREVEKIVE
KEVIVEKVVE KIIEVEANQV AAVEMKQTSP SVAQGLSNQQ QATAQLNPST PNVSGDALTA
FFSAQSQTAQ LHQQFLAIPQ QYGDTFTTLM TEQAKMASQG IAIPESLQRS MEMFHQHQAQ
TLQSHAEFMQ LQSSSSQAAL AMLNNAPINF TPAVAQPRVT APAPAPVAPV APAPVAPAPF
AATTVAHNAA PVAAQAVATR PAINTPVAPV VQTAPVAHAP AMTVQVAPAA PALVMPAVVM
PEVTSVAPAT SGLSAALVQQ TMMAVVADKT GYPTEMLELG MDMEADLGID SIKRVEILGT
VQDELPGLPE LSPEDLAECR TLGEIVDYMN SKLPAAGQVV VSTTAPTAPA ANGLSAALVQ
QTMMAVVADK TGYPTEMLEL GMDMEADLGI DSIKRVEILG TVQDELPGLP ELSPEDLAEC
RTLGEIVDYM NSKLPVVSVV AVAPPANVEA TPAQVPANNG LSAALVQQTM MAVVADKTGY
PTEMLELGMD MEADLGIDSI KRVEILGTVQ DELPGLPELS PEDLAECRTL GEIVNYMNSK
LPAVGSVIVA THVTTAAPAA SGLSAALVQQ TMMAVVADKT GYPTEMLELS MDMEADLGID
SIKRVEILGT VQDELPGLPE LNPEDLAECR TLGEIVDYMN SKLPVVSAVA VAPAANVEAT
PAQVPANNGL SAEKVQQTMM SVVADKTGYP TEMLELSMDM EADLGIDSIK RVEILGTVQD
ELPGLPELNP EDLAECRTLG EIVSYMQGKL GQNVAPISAV VQPEPTIDLP PHDLPPHSEV
VLKKLPAAAE LTQQSAQKAL PRVFAKDACI IISDDGHNAG VLAEKLHAQG LTVAVVRSPE
SLVASASPLN SHIASFTLAA IDDTSISAVI NEIKTLGQVA GFIHLQPQHK TSADAKGLVL
SSAAKASVEQ AFLFAKHLQP LLTTAATANT SSSFISVSRI DGGFGYLNHS QIARSELNQA
ALAGLTKTLS HEWPNVHCRA LDIAPALDAK QLANAVIAEL FATDKLLEVG VSESGVSEAG
ATETLARMTL VAGKADTRHS AANLTSADKI LVTGGAKGVT FECALSLAKR SKAHFILAGR
SSQQAIPAWA QGKNNSELKA AAIAHIQSLG EKPTPKQVDA LVWPVQSSQE ITSALQAFTA
VGASAEYLSL DVNNPDAIAS TIVPITELSP ITGIIHGAGV LADKHIQDKT LDELARVYGT
KVTGISNLLA ALDLDKVKLI ALFSSAAGFY GNTGQSDYAM SNDILNKAAL QLAQQLPNAK
VMSFDWGPWD GGMVNPALKK MFMDRGVYVI PLKAGAELFA SQLLSNTGAQ LLVGTDMQGS
APHDDTSNKV QETEGSNLKK PEADLTTDAS DPHALLNALN PSAVNISAVK LQRTLDPKAM
IFIEDHCING NPVLPTVCAI QWMREAAFDV LKQPVKVQSY KLLKGIIFDT VTLEKGALEN
GAPITLELEL APIALTDKAA KDTDECLSGQ FSALISFEGR PQYQAILVID DAPSDNLATN
SKATAFDAHS LAWLSAITTA SSLYSDGTLF HGPRLQGIEY VVKFDDASLI AKVSLPHVAL
ADCGSFVPNL APKGSQAFAE DLLLQAMLVW ARLKYGAASL PSSIGEFISH APFAFGDKGY
LVLEVVKHSG RALEANIALY HQDGRLSCEM NNAKVTISKN LNGAFLANKV ANKSIESVEA
KVE
//
