ID A0A1Q9DTR0_SYMMI Unreviewed; 2589 AA.
AC A0A1Q9DTR0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=beta-ketoacyl-[acyl-carrier-protein] synthase I {ECO:0000256|ARBA:ARBA00013191};
DE EC=2.3.1.41 {ECO:0000256|ARBA:ARBA00013191};
GN Name=fabB {ECO:0000313|EMBL:OLP98563.1};
GN ORFNames=AK812_SmicGene18976 {ECO:0000313|EMBL:OLP98563.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP98563.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP98563.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP98563.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467,
CC ECO:0000256|RuleBase:RU003694}.
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:OLP98563.1}.
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DR EMBL; LSRX01000392; OLP98563.1; -; Genomic_DNA.
DR OrthoDB; 211541at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11712:SF336; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 2.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Transferase {ECO:0000256|RuleBase:RU003694};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1359..1381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1424..1444
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1506..1527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1547..1568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1629..1654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1685..1705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1717..1735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..487
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2193..2223
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1885..1910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2247..2276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2484..2515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2530..2589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2248..2262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2589 AA; 277067 MW; B6A292374C00EC02 CRC64;
MSLAFTVGQP KLTQRTGPFD TRATGAPLQR NDGVTGTSGR GWQSVGAAVA LAAAAGAKVA
RRARGTSRIT LFADRRVVVT GMGITSCLGN SLDEVAETLH EGKSGITFSE EYEKFGIKSQ
VRGTPDLTQE EIKELIPRKA LRFMGRNAQF AYIALQRAID NAGLKPEDYE NNERCASILG
QGGTSIVDIT ESVGFVADQV KRWPSKVGPY RVTRTMGSTV SAVLSSSFKL QGPSFSISSA
CSTGAHCIGV AMEQIQMDKA DMAVAGAGEN ECWEFTAMFD CMGALSTKRN SEPTKASRAF
DKDRDGFVIA GGGGMLILEE LEHAKARGAK IYAELTGYGA NSDGYDVVAP SGVGGERCMK
IAMAMADKIG GEKEVGYVNT HGTSTPVGDV QELGAVNRVF TEKGYQPFVG STKSMSGHAL
GAAGVHEAIY SILMMERGFL AESINIEDLV DEAEGMKILT ERHDGGVART FNSAGITGIL
EAIKQQVVSL LVAVLDPSLK ASLPPALIST FQDKKMAKSM VQMMEHIMAD PDFVEVLKNF
INTSMTNEAL LGSLKKVMQE GFYYPRAAMD AKCYKVRGGL AWSLPYALLG GVFGIASAHP
GRAAAVIARS GPCQIDQRDL KRSETPTSAP RSLPKALQGS ELQATVESQL LSFGSFVETQ
IDQGKTATSE FFTGYSITVC SCLDMALGAY EEAAARSQRD TQSKRLHCHA LKYSSVPCCL
MPRCAMGSAC LQPVQLGVAF LTLAALAEAA AAPEECEDTP GWTNGYTACN NYVPVDPDCH
EDGVVCHFYK EHADFCAKGM NDPWLNCCTC GGGSTFNGER PTTTPRPTVD IPGLSWLPGI
HSVEKQISKM EEQMKPFEQG MHEVYQGLNA PDFNAPPELE GNSLVQVNWA VFLIIVVVAG
GTAVGWCCDL VAPACSIDEL RREAQRRLGV GRGKLLSPSG RYFPDGDITV AQAELSHGDL
LSLHREPLRL ASTVHAFAAI LGDGTVVTWG HDAHGGSSTA VRPELKNVKQ VQATGSAFAA
LLADGSVLAW GNPECGGDCS SVQERLVNVK RIEAGFHAFV AILDTGSVVT WGDAAFGGQC
SEVYEQLQGV QQVSCTGYAF AAILDNGSVV TWGHPAHGGD SRAAQHLLKN VQQIKGTMSS
FAAVLDDGSV IQWGPPAYGA KAVQVPVENV QRLEAGFHEF VAILQDASLV TWGHDPWADG
ITVLPFKNVQ HVQVTDTAFA ALLTDGTVAS WGDADSGGDS DAVQEQLHDV RCLESSGGAF
AALLEDGAVV TWGDRQRGGN SSSVQAQLKN TRAIYANGYA FAAIVQNGPV ESVVTWGNAF
YGGDSTYVQV GLGPKPPSLD EGLPGASAYH SASGGRPPVW STIMLILSYV LLVPGLTQVL
FSFNIVVNVL GHRIDVQPEK GHVACTETVT GLVHLLEKTG SRTGAVLIVL YAVVVPVVKL
LLLAIGEVFR FSSSEFLVLV ARLCILIVQS ISKWACPDMF AYILLVHLVR LLHSDPLVLT
AAKLDVGFSC FSVFCVCSTV SSLGISLPLL PTKTAVTGKP FCSAKAVQLL AGVIAAVFAI
FFIAGLSIPC MSLRIDERQL YPPNGSVPYS AKPLVESLAI PDLLKSDISI LSCTRWLIQE
IGSGEANSLF ALVMFGFCVI ALPLADVLFL LLAASRLEPT AAGKSLPPSD QPCWFYSWAK
VLRKLAMLDV SIMGVYVITF CMGIYKKQGI VLSTHNGVLL LIVAEVAHTL LYWLVSGAAE
HAEASARKEL IAYRAAAQEA GDPDADGPQD LSCCGLSKFL KLPVAMGAGP GPDERYKRAE
IKVAGFVLVL VEAMAPPRVV LADLPPAERE RMLSFLVANK VDFKPDISGK FSAVVKVVRP
EATSPAASPS LGADKAADQI NMAGWVPSAS STPSTSARTE ETPGAGKGTS LTAVQSELKK
RFPTFTGLLP ALGQHPKTMT KAELLSFIEE VYTARYNQDL LQIQQHAEAE AVGVQIKKKL
PSDLTSFPQS VVTVAGKRYG LRRMVGQVCW SVAKSVELHR AEHEGIETFA RFLEESYDAI
DALFYLEMRW AARQMTIPRG TWLRAWKMNQ GFTPGHHFLA GAARPRTVDG QVSKTSVPPG
ARPQLALKKA LAAVREGIDK EAPDSLKATI CARVKQESGD GANPIDWDRF LFLCTQEYRK
ARCIASQRKE RRGNQGILTA FSQLVSNTWG VSLQEAFAHF DVEGSGVISF DNFAQVVAND
LAYEGAAKDL WDILDVQSKG YLEEEEWSQL GTSEQVEGSA PTEDKSLPSG WDADLGPEES
QALLQEAREV AARLTNSLAE RGAGEADPDE VFGWALRVVL KRHGQPCLAK FHEGRDHQAV
EGEDEQRDLE AIVRKQLSLS TEELVWEALA EATGGGKDSE LTSLAEVLVN EFLLVTDALM
EALVSGNIEN WLTTLGIEAP GTESQKEQFQ ALTDELQGVL ATQEEGNEDS VAHVCRLTVA
APELRELCAA RTTELLQDQA SHRLLSTSRS PDEAQPETAL ETGVGVSDDT PETPNFAQVE
DTVTVEELPE AQLDEEVDGA IPAAEAPFSG EEPLAEQADE AEVPGPFGAE AAEAAEAEPG
SLEDLEDAF
//
