ID A0A037ZG63_9RHOB Unreviewed; 1583 AA.
AC A0A037ZG63;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Ketosynthase family 3 (KS3) domain-containing protein {ECO:0000259|PROSITE:PS52004};
GN ORFNames=ACMU_12040 {ECO:0000313|EMBL:KAJ55420.1};
OS Actibacterium mucosum KCTC 23349.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Actibacterium.
OX NCBI_TaxID=1454373 {ECO:0000313|EMBL:KAJ55420.1, ECO:0000313|Proteomes:UP000026249};
RN [1] {ECO:0000313|EMBL:KAJ55420.1, ECO:0000313|Proteomes:UP000026249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 23349 {ECO:0000313|EMBL:KAJ55420.1,
RC ECO:0000313|Proteomes:UP000026249};
RA Arahal D.R., Shao Z., Lai Q., Pujalte M.J.;
RT "Draft Genome Sequence of Actibacterium mucosum KCTC 23349, a Marine
RT Alphaproteobacterium with Complex Ionic Requirements Isolated from
RT Mediterranean Seawater at Malvarrosa Beach, Valencia, Spain.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KAJ55420.1}.
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DR EMBL; JFKE01000004; KAJ55420.1; -; Genomic_DNA.
DR STRING; 1454373.ACMU_12040; -.
DR Proteomes; UP000026249; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 2.
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; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR041354; 4PPT_N.
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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43074; OMEGA-3 POLYUNSATURATED FATTY ACID SYNTHASE PFAB-RELATED; 1.
DR PANTHER; PTHR43074:SF1; PKS_AT DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF17837; 4PPT_N; 1.
DR Pfam; PF01648; ACPS; 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 SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000026249};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..463
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 941..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..972
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1583 AA; 169223 MW; 0789EC332A3DF83E CRC64;
MPDLNEPIAI IGMDCIFPQA PDRVSFWQNI LNKVDAVDEA PADWHGDLFL DPDSRENDRV
YTTKGGFLRD LATFDPLKHG VMPTAIDGGE PDQFLALELA ARCLEDAEFD ARPVDGERVA
VILGRGTYIN RGFTSVVQHG IMIDRFLDVL KKLHPDTEAA ELAAVKKELK ASLPPFNAEI
APALVPNLVS GRISNRLDFK GANYIIDAAC ASSLIAMERG MADLRSGLCD MAIVGGVHAS
TPAPIYQIFC QLEALSKQGS IKPFSAEADG TLLGEGVGIL AIKRLSDAEA AGDKIYALMR
SVGVASDGKG LGILAPRIEG ETLALERAYQ QSGLDPKSVG LIEAHGTATS VGDATEVEAL
AGQFGGRASE EPEVALGAVK SMIGHCIPAS GSAGLIKTAM ALYHRTLPPT LVDTPNPDLG
IEDTPFYLNT EARPWIHGEE TPRRAGVNAF GFGGINAHAV MEEYTGAPQP APQLTRSSEV
VVLDAADGPA LVAKIAQVVD TLAAPEVTLA ALARQVNAQS GDGDWRAGVV AADKGEATAK
LQKIADRIGA GKKKLKDRKG AYLTSAPLAR EGKVAFMFPG EGSQHIGMLR EVMLHHPEMR
GWFDLVDGAF AGHPRALKPS QVIYPPSYVA AEGEGLWRMD IGPEAIFAAN QSVAALYDKI
GLRADMVVGH STGEYSALYA AGVTSREDPA QLQAEMRALN DAYEQMSAEG VIAEGALIAI
GAVDNAKLDA ALAGRDDVYL AMDNCPNQKV IAAFSPAARD WAEKLAGELG GFGEALPFER
AYHSPAFAEF TKRLEGFMAD MAISAPSMPC YSCLSTEPFG DAGDDIRKLT AAQWSGRVRF
TETIQRMHDD GARIFVECGP RNNLTAFTND ILRGKPHVAL AMDTPGRVGL DQLNHFIAQL
SVEGVALNAE AFAAPEEAVK ADEGPSRPQV LKMGLQPMEL TNVPPRKTKR APEVAPAAPE
APRAPEPQAP VAPSASPQEA LVASYFDTME QFVSAERDIM SAYFGAFTGE APKVAAPDAA
PQRFPMLQTT ERAADGRSLT ARIEIDTGRA PYLLDHSFGR DISMLWPDLS GLPVVPLTFT
MEALAETAAA LCPEMVVVAM NEVRASRWLA LDRPVLALEA TAELKEQGAV SKVHVRLRAA
DGPALRPILV EAEIELAAER PAAPLAEPLS YDAHRGAYWS LEDVYSRIMF HGPKLHAIEN
MDLASGDGCE GVLQGLPLDT LYQGIPQPYF ETDPITLDAV GQLVGVWSAE SLDEAFHIFP
FRVERLEMFR APLAPGEKAR CRCKIDLIGD DEMSSYIDVV SADGHLQCRI HGWWDKRFNL
PDRFFQARLA PSVNPVSAVI EAGDGLALTA VTDISTSLLE GSGGIWAKVL AGLQLSPSER
LEWDGLADAT EKRRWEWLRG RAAAKDAVRA VTGLAFCPAD VEVQPSTDDT PPMIGPSWPE
SWGQAPLISI SHSGEYAIAA AADATKYAGV GVDIERIVPR DEAFLATAFT TAERGYLAQA
TSGADRDRLA AAMWCAKEAA GKAYGAGLAT MFDRFEITSI TGDAEGFQVS EKSGGTLVNV
RVVTEIVPET VAVVALRPRS GAH
//
