ID A0Z9T4_NODSP Unreviewed; 1584 AA.
AC A0Z9T4;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000313|EMBL:AHJ29034.1};
DE EC=2.3.1.39 {ECO:0000313|EMBL:AHJ29034.1};
GN ORFNames=NSP_27060 {ECO:0000313|EMBL:AHJ29034.1};
OS Nodularia spumigena CCY9414.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Nodularia.
OX NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ29034.1, ECO:0000313|Proteomes:UP000019325};
RN [1] {ECO:0000313|EMBL:AHJ29034.1, ECO:0000313|Proteomes:UP000019325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ29034.1};
RX PubMed=23555932;
RA Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., El-Shehawy R.,
RA Hayes P., Bergman B., Sivonen K., Dittmann E., Scanlan D.J., Hagemann M.,
RA Stal L.J., Hess W.R.;
RT "Insights into the physiology and ecology of the brackish-water-adapted
RT Cyanobacterium Nodularia spumigena CCY9414 based on a genome-transcriptome
RT analysis.";
RL PLoS ONE 8:E60224-E60224(2013).
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DR EMBL; CP007203; AHJ29034.1; -; Genomic_DNA.
DR STRING; 313624.NSP_27060; -.
DR eggNOG; COG3321; Bacteria.
DR eggNOG; COG4221; Bacteria.
DR HOGENOM; CLU_000022_35_4_3; -.
DR Proteomes; UP000019325; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd08953; KR_2_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; 3.30.70.250; 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; IPR049490; C883_1060-like_KR_N.
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; PF21394; Beta-ketacyl_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; 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; 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 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:AHJ29034.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AHJ29034.1}.
FT DOMAIN 49..475
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1459..1535
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1584 AA; 174388 MW; CC3B946D606505D8 CRC64;
MSFLLEIFKS REIMNYSIDE IKNYPASERI LAALKDARIK LEAVELERSE QIAIIGMAGR
FPGARNLDEF WYNLKNGVNS IEFLNDEELL ANGVKPEDLQ NPHYVRAYAS FSGIDQFDAA
FFGYSPREAE ILDPQHRVFL ECAWEALENA GYDSQQYSGS ISVYAGAALN SYLVNLSSNS
NYRDSANNVQ IVISNVMGLM PTRVSYKLNL TGPSCGLQTG CSTSLVSVHL AAQSLLSREC
DIALAGGVSI GSGEKTGYLY QEDGVLSPDG YCRAFDVNAK GTVFGNGVGI VVLKRLRDAI
KDGDHIYAII KATAINNDGS QKVGLTAPSV TGQAKAIATA LAKSKINPET IKYIETHGTG
TALGDTIEIA ALTKAFSPHT NKKQFCTIGS VKTNIGHLDA AAGISGLIKT ALILKHKQIP
PSLNFTAANP QIDFANSPFF VNTQLTSWTN NEYPRRAGVS SFGMGGTNAH AILEEAPTLL
SANSSRPWHL LTLSAKTLSA LETATKNLSE YFQQFPDVDV ADVAYTLQIG RRAFNHRRCL
VCQTPTQAIE ILTGLDSSQV LSHSPENTEP SVVFMFPGQG SQYVNMGQEL YATEAVFRTE
IDNCCELLTP HLGLDLRSIL FVQKNKKVAE EIALITQTAY AQPALFVVEY AWAKLWLSYG
IQPQAMIGHS IGEYVAATLA GVFTLADALV IVAQRGQLMQ KCPSGVMLSV SLAAEKLQVL
LTDDLVISVY NAPQLCVVSG TEAAINLLEQ RLENEHIAHR RLHTSHAFHS PLMVSAVTPL
TEIFQNIQLC SPQIRFISNV TGTWITSEQA TNPNYWATHL RQPVRFAEGI TQLQQIPNQV
LLEVGFGQTL SNLVRQFPDA HPTLSSGRHP QDNQSDVALI CKTLGQLWLW GVSVNWAEFY
TEQQRRRLPL PTYPFERQRY WVERYPLPET TSTTSKTLQK QEDISNWFYL PSWRQKPLLR
SAAPLNKQRY LVFCHGGGVG EKLVQQLEKI GQDVITVKPG ERFTQAGDNY TIALDHPEDY
KTLWLQLQTD DQLPDVILHS WTLQELTNFQ QQQNLGFYSL LWLIQALSSS SPSVRICVLT
QQVHNVLGNE TLNVDDATIL GLVKVIPQEY PNLTCQHIDV SIPNLNLQQI VREITTPPVL
SDTLPLARGG LGSAIAYRGK TRWLQEFTPI SLPDAEVTQL PLISGGVYVI AGDLVEGLGL
IYAKFLSATV KAKLVFLGRS DLPQPKLWDN WLATHGRQDS VSHCIQQLQA LQAQGCEFLF
NSVDLAQIDQ VEEAIAHSLT QFGTINGVIH AAAMGDRASC LIRNLTMDEC EKQFSPKIHG
LLTLEAALKN QPLDFFLLQS SLSAVVGGIG FAAYAGANCF MDAISHQHSQ NSNTPWISIN
WDAVSLAEIT TPTGAALVDL AMTPQEVWQV TQRILAQPVA AQISVSPIDL ESRPQSQIPE
NSISASNHAR PQISTTYVSP SNEIEARVTQ VMENLLGISP IGIHDNFFEL GGHSLLAIQA
VSQLRSEFQV ELPMRQFLFE SPTIAGIAKI IRENQSLVTD DTEALVSNLS ETSHKEEIAT
LLDQVEQMTP TQVQEYFLDT LEPS
//
