ID A0A139XBR1_9CYAN Unreviewed; 1619 AA.
AC A0A139XBR1;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:KYC42131.1};
GN ORFNames=WA1_19235 {ECO:0000313|EMBL:KYC42131.1};
OS Scytonema hofmannii PCC 7110.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC42131.1, ECO:0000313|Proteomes:UP000076925};
RN [1] {ECO:0000313|EMBL:KYC42131.1, ECO:0000313|Proteomes:UP000076925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC42131.1,
RC ECO:0000313|Proteomes:UP000076925};
RX PubMed=23221676; DOI=10.1093/gbe/evs117;
RA Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT of oxygenic photosynthesis from prokaryotes to plastids.";
RL Genome Biol. Evol. 5:31-44(2013).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {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:KYC42131.1}.
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DR EMBL; ANNX02000020; KYC42131.1; -; Genomic_DNA.
DR RefSeq; WP_017741944.1; NZ_KQ976354.1.
DR STRING; 128403.WA1_19235; -.
DR OrthoDB; 499075at2; -.
DR Proteomes; UP000076925; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR InterPro; IPR001227; Ac_transferase_dom_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; IPR014181; Omega3_polyunsat_FA_synth-like.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR02816; pfaB_fam; 1.
DR PANTHER; PTHR43074; OMEGA-3 POLYUNSATURATED FATTY ACID SYNTHASE PFAB-RELATED; 1.
DR PANTHER; PTHR43074:SF1; PKS_AT DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF53901; Thiolase-like; 4.
DR PROSITE; PS52004; KS3_2; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000076925};
KW Transferase {ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 1..450
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 464..938
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1464..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1619 AA; 177891 MW; 6F0C00D7D80815C7 CRC64;
MEKIAIVGFS CLFPEAKNSE EFWQNLIQQK DSTSFVTTQE IGVDPQVFYD PAKGQADKFY
SLQGGFIRNF QFDSTGYKLP AEFLQSLDNT FKWSLDTAKQ ALQHSGYLGN EAILAKCGII
LGALSLPTQF SNKIFAPIYQ QVLSPAIKEL LQCQNFDFTS PNEPAKVSAH NAMISGLPAA
IVAQALALSN IHLCIDAACS SPLYAAKLAS HYLRTHKADL MLAGGISCSD PLFIRMLFSG
IQGYPEDNDL SRPLDKSSRG LITADGVGMV VLKRYSDAVK DGDRIYATIS GTGLSNDGRG
KHLLSPSSKG QILAFERAYK EAQISPKDID YMECHATGTL LGDTTEFNSV ETFFGKHQAT
PLVGSVKGNV GHLLVAAGSV SLIKALLSMS KGVIPPTINI SDPIGTENNV IAPQRIVTST
TDWPNKTPVK RAAISAFGFG GTNAHMILEQ GENSPSSPTP PTPVAKVAIV GMDAFFGSCN
GLDAFDRSIY DGTQNFIPLP SNRWHGIEDR QDLLQQYGLP EGKAPVGAYI QDLELDTLSY
KIPPNELAKL NPQQLLLLKV ADRALKDAGL KEGGNVAVLI AAETEFSVHQ LQQRWNLSWQ
IKEGLATGGI SLPEDKLAQL ENITKDAVHH PVEIAEYLSY ISNIMASRIS SLWDFTGPTF
TVTAGENSTF KVLEIAQMLL SAGEVDAVLI GAVDLAGGLE NVLLRSKLAP VNTGTNTLSY
DQKANGWIVG EGAGAVVLKR HDTAKKDNDR IYAVVDAVGF GTAPCSRRTQ IEEQNISVHQ
RSSAVRITSL DAGTVSQACQ EAFQMAGIKP TDVEYLEVYG SGISQEDEAE IKGLIQAYPA
GENNLSCAIG SVKANIGHTY VASGMASLIK TALCLYHKYI PATPKWSGVK NQEVWQGSPF
YVSAESRPWF LGKDAKKRVA AINNMGMDGT YAHIILSDEP EQQQHNSRYL QQMPYYLFPI
VGCDRTELLQ QVNALQTTID NSHSLAAVAR QSFLEFQKHS EANYALAILG RNKNELAREM
ESAVKGVNKA FESGEDWQTP AGSYFTAKPL GKKGGIAYVY PAAVNSYLGI GRTLFRLFPR
VHGDTVIKSL FSLFAEVSQL VFPRSLNKLS TKQLESLEKQ LLNNALAIFE TDMAFARLIT
TIVRDDFRVK PKYVFGYSLG ETSMMTAMGV WSNFSEGINA FHSSPLFADR IAGPKNAVRE
HWGLPKTPSS NDDFWSTYLL MASPSQVQEC LKHENRVYLT QINTPEEVLI SGDSLCCQRV
IKTLGCNAFR APFNHAIHCE PMQSEYEEVV RVNTLPSHNI PGIAFYSSAE YEPIPLESHA
IARSLAKGLC QPLDFPRLVN RVYDDGARIF IEAGSGNVCS RWIDKILENK EHITIPLNRR
GIDDHASIIR ALGKLLSHQV AVDLSLLYGE TSEASSQRKP TVKTLTLGRA TPIGEIPQEK
VPQGNRIVAS ILTDENRKIF QNAARKLPPR IDTKQQQNKP QSTESESRNY PKTTIPNQPP
ASNIHNIITP SIPQPEKLNM KNAPNNSFEP KKRVQSGEQK TTQEIVSHRT LSTPNNIQQL
SHITTQRYPN KTQYEKLSNN NFIVHQTHAK FLKSRHQFSQ QMSEIIQLQL TCVENLLNS
//
