ID A8ZKN1_ACAM1 Unreviewed; 1665 AA.
AC A8ZKN1;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE SubName: Full=Beta-ketoacyl synthase, putative {ECO:0000313|EMBL:ABW31349.1};
GN OrderedLocusNames=AM1_A0228 {ECO:0000313|EMBL:ABW31349.1};
OS Acaryochloris marina (strain MBIC 11017).
OG Plasmid pREB1 {ECO:0000313|EMBL:ABW31349.1,
OG ECO:0000313|Proteomes:UP000000268}.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris.
OX NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW31349.1, ECO:0000313|Proteomes:UP000000268};
RN [1] {ECO:0000313|EMBL:ABW31349.1, ECO:0000313|Proteomes:UP000000268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268};
RC PLASMID=Plasmid pREB1 {ECO:0000313|Proteomes:UP000000268};
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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DR EMBL; CP000838; ABW31349.1; -; Genomic_DNA.
DR RefSeq; WP_012166727.1; NC_009926.1.
DR KEGG; amr:AM1_A0228; -.
DR HOGENOM; CLU_000022_35_4_3; -.
DR OMA; WVANLRN; -.
DR OrthoDB; 499075at2; -.
DR Proteomes; UP000000268; Plasmid pREB1.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; 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; 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 Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR001227; Ac_transferase_dom_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; 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; IPR013968; PKS_KR.
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; PF21089; PKS_DH_N; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 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; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Plasmid {ECO:0000313|EMBL:ABW31349.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000268}.
FT DOMAIN 7..431
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 1665 AA; 180109 MW; 5AD6E10E83437C4C CRC64;
MNVHRNGLEI AIIGLSGQFP GSPTLDQFWQ NLKAGVESIS VFSDADSQLA SAPSSATQTA
VKAGGILTDI EYFDAPFFGI NPREAETMDP QHRLFLECAW QALEQAGYAP GRGNDAVGVF
AGVGMGTYLL YNLSPHPEVM ASRGFLQTLV GVDKDYLSTR VSYKLNLRGP SISVGTACSS
SLVAVHLACQ SLLSGECDMA IAAGVAVKVP QMNLTLSPDE IASTDGQCHA FDARANGTVG
GNGLGAVVLK RLEDAITDRD TIYAVIKGSA INNDGGMKAG YTAPSQAGQT QVIRAAQAMA
EVEPDSITYM EAHGTGTPLG DPIEIAAMTE AFRASTNKVG YCAVGSVKTN VGHLDAAAGI
AGLIKTTLAL HHRLLPASLN FDTPNPDIDF ANSPFYINTG LKEWVANGTP RRAGLSSFGF
GGTNVHLVLE EAPAPAPSSL SRPQQLLLLS AKTRSALDTA TANLVQHLHL PDINLADVAY
TLQVGRSTFA HRRIVVCATG AEAIAALVDK ADCQAPQSEY GLTDSDTSQR PVVFMFTGQG
AQYVNMAREL YDTEPLFRQT CDRCFTILEP HLGFDLRSVL YPDAASPEFD IDQATQQLRQ
TAIAQPALFV IEYALAQLWM SWGIRPTAMI GHSIGEYVAA CLAGVFSLEE ALPLVVRRGQ
LMQQLPGGAM LSVNLSVDEV ASLLDEIDKT ISIAASNSPS LTVVSGSNAA IAALEQWLTQ
QQIGCQPLHT SHAFHSSAMD EIATPFAQAI GQIQLHPPQM PLISNVTGTW MTAAEATDPQ
YWVHHLRQTV RFAEGIAELL QDSHHLFLEV GPGRTLNTLT RQQATDRAVL SSLHHPKDHA
SDVAFLLQTL GRLWLAGVTV NWPGFYAHEQ RDRLPLPTYP FERQRYWIDP PKTLPSKASL
SQAVPLRQNS SQANDLADWF HVPSWQRSSR LSTPIRSSSS ANILIFLDQA GVGEVLVERL
QQQGHRVATV DIGSEFAQLS DTKFCLNPDQ ADDYQALFKT LRTQQFSTNA IAHLWSITTA
AEMPSGLDPL DATLSRSFYS LLFLAQALGD QPGTDPVHLT VVSNQLQSVI GNERMCPEKA
TLLGPVGAIA QEYPHLNCCS IDLELDEPLS EATDPDLLES LLAEITAPSD DALIAYRGRH
RWVQTMQPIR LEETLADPAN LRSGGVYLIT GGLGGIGLTM AEYLAQAVQA KLVLIGRSGL
PDDTAAADGQ DAPVRRKIAD LEALGAEVLV TQADVTDLAQ MQRAIAEAEA IFGSINGVIH
AAGIPGGGIM QRKTRAAAEA VLAPKVKGTR VLEAVLPADL DFLVLCSSLA SVIPLPGQVD
YAAANAFLDA VAQARTARDQ FTTCINWDAW TEVGMAVKAA NPSVQDTDQN PDPIAVEHPL
FEVCYPHDAD QVRYVSRLSL DQHWVLNDHR WGEQGLLPGT AYLEMARAAW ANHHQTNPTD
GIELRNVYFL TPLLVDAEQE VHTVLTQKDT YVEFQIQSPS GVQISGAQPL EWQTHTVGEI
AIPQPAQPRT FDLPALKATC SQPQAGSAAP SLDHLLDGPI QFGDRWRSLK WINRSDTEAL
ALLELPDAFH AELSVHRLHP ALLDVATGFL MMQLRQSDTA YLPFSYRRLT MWGTLSAQIC
SYIQWLNPSD SDSLKFNIVL MDDQGIELID IEDYTLRRKA NDATT
//