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Database: UniProt
Entry: A0A127V838_9SPHI
LinkDB: A0A127V838_9SPHI
Original site: A0A127V838_9SPHI 
ID   A0A127V838_9SPHI        Unreviewed;      1436 AA.
AC   A0A127V838;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:AMP97138.1};
GN   ORFNames=AY601_0167 {ECO:0000313|EMBL:AMP97138.1};
OS   Pedobacter cryoconitis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=188932 {ECO:0000313|EMBL:AMP97138.1, ECO:0000313|Proteomes:UP000071561};
RN   [1] {ECO:0000313|EMBL:AMP97138.1, ECO:0000313|Proteomes:UP000071561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 27485 {ECO:0000313|EMBL:AMP97138.1,
RC   ECO:0000313|Proteomes:UP000071561};
RA   Lee J., Kim O.-S.;
RT   "Complete genome sequence of Pedobacter cryoconitis PAMC 27485.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP014504; AMP97138.1; -; Genomic_DNA.
DR   RefSeq; WP_068395264.1; NZ_CP014504.1.
DR   KEGG; pcm:AY601_0167; -.
DR   PATRIC; fig|188932.3.peg.170; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000071561; Chromosome.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase 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   GO; GO:0006633; P:fatty acid biosynthetic process; 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; 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; 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; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000071561};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          3..457
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   1436 AA;  157968 MW;  7E7479AE877E66DE CRC64;
     MKKTDVAVIG MSCIFPGAGD LDTFWKNIIN KVDSTQVVPP DRIDPVHFDK DSTGVDRFYC
     NRGGFIPDYN FDPQRFGILP VAVNGTEPDH LLTLDLVYSS LEDAGVFEKN TSLAKTGIII
     GKGNYAGPGA TRAIEIVRTG EQIAAVLKDL LPQLETAAIE KVKHEFQARK GRFGPDTAMG
     LIPNLVASLV ANRLNLGGVA FTLDAACASS LIAIDHAIQE LNSGRCNMVI AGGVHVGQNA
     AFWSIFSNLG ALSKQEKIKP FDAGADGLII GEGCGFVVLK RLEDAIQDKD RIYAVLKGAG
     VSSDGSGTSV MSPSVKGQLR AITQAWENSG LSAKDIGYIE AHGTGTPLGD KTELETLTQF
     FGHDAELPKA GIGTVKSNIG HAMPAAGIAG LIKTCLALYH DILPPTLHCE NPLTQLAKTQ
     FSAVQEPLSW EKSGLPKIAG VNAFGFGGIN AHVVLEGFNA PKKDKVLLLA RPTHEELIHA
     LENNDYSAGN GNYRIALFDP TPERIKKAIK IAAKNNPWRN KQDIWYTNEP LISNGGKIAF
     VFPGLDGLAG GEVSSVTDYF NIAEAQHAKA EGLLSDALKT LNKSSVLDIA LKQLGVQPDM
     NAGHSLGEWL AARSSELAEE SSVSQLLKVL DPETFELKDS RFIAVGCGIE LLLPIIANIN
     DVYLSNDNCP QQVILCGSKN ALEELTPLLK ARQIFHQILP FQSGFHSPFI ADKLEVILEG
     MKDMQFRKTT TPLWSATTLE LYPEGFEAIR QLSAEHLIKP VRFRELTAKL YEQGARVFIQ
     IGSGGLVGFI DDTLKGKNFS TISSNVPVRS GITQLQRVIA ALFVEGKETG LDFLGQIKSS
     PASKGKGIKL ELGLPTITGL NSLKELAAGS PSVHAQPNPA VYAKGLLEDV ADPVMEAFNE
     NILEMANIQA EIQQLFKDRV LQPANYTNRL TKPEFATPEV STPLAPQVLA TPLNRMPFSK
     QLDITLENCP YLKDHALLRQ PKDWHCVDDM DPVIPMTMIF ELFGEIAEEQ SRGEQVHKIL
     NIKVFQWMNV VKPFRETITG EWKDQQKVYL NLERFANAEV LLAEKLGIPP AQQSFDIGKI
     LDIQRTAEQI YENHMFHGPG YQGIKHLKAV GEKGITGTIE SGAGKGSLLD NAGQLFGLWL
     QLILTKDRIA FPVKIQEIEF FGNMHDQQGE FECTCVLTDM NEEFATGNFI IKRDHQVWAI
     ISGWQNRRLE IDDALWSVSM SPLHNRLSKE IAPGIFMFHN AYSRVVSWDF ILKRYFNQDE
     KKYHNALLPN KRKTWMISRV AVKDAVRDLL NKEKQHACYP ITFEIKSDEL QKPYPHGGQT
     AGIHVSLAHK GTDAVGIARL NRPVGIDIES IEERSAGFFD LAFTSTEMAL LQGRDKAEWA
     TRFWTAKEAY GKYLGKGLQG NPKAYGVEEI IGEELRIKDT IIKTIKHHNY IIGWTQ
//
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