ID D6ZYF1_STAND Unreviewed; 2436 AA.
AC D6ZYF1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:ADH89063.1};
GN OrderedLocusNames=Snov_1759 {ECO:0000313|EMBL:ADH89063.1};
OS Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM
OS 12100 / NBRC 12443 / NCIMB 10456).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Starkeya.
OX NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH89063.1, ECO:0000313|Proteomes:UP000006633};
RN [1] {ECO:0000313|EMBL:ADH89063.1, ECO:0000313|Proteomes:UP000006633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC
RC 12443 / NCIMB 10456 {ECO:0000313|Proteomes:UP000006633};
RX PubMed=23450099; DOI=10.4056/sigs.3006378;
RA Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A., Copeland A.,
RA Berry K.W., Glavina Del Rio T., Hammon N., Dalin E., Tice H., Pitluck S.,
RA Richardson P., Bruce D., Goodwin L.A., Han C., Tapia R., Detter J.C.,
RA Chang Y.J., Jeffries C.D., Land M., Hauser L., Kyrpides N.C., Goker M.,
RA Ivanova N., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the facultatively chemolithoautotrophic and
RT methylotrophic alpha Proteobacterium Starkeya novella type strain (ATCC
RT 8093(T)).";
RL Stand. Genomic Sci. 7:44-58(2012).
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DR EMBL; CP002026; ADH89063.1; -; Genomic_DNA.
DR RefSeq; WP_013166567.1; NC_014217.1.
DR STRING; 639283.Snov_1759; -.
DR KEGG; sno:Snov_1759; -.
DR eggNOG; COG0236; Bacteria.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_31_0_5; -.
DR OMA; KMRGGEF; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000006633; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
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; PF13602; ADH_zinc_N_2; 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; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 20..440
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2301..2378
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2380..2402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2436 AA; 255067 MW; F59B6A1A0EA68EA7 CRC64;
MDSNVHGAGA ALSSVSQRPL HAAAILGCAC RLPGAADEAA FWSLLARGEC SVSEIPADRW
SHERFLHPGR GVPGRAYTFA AGVLDDIYGF DAGAFGLSPR EAEQIDPQQR LLLELVREAF
EDANVPLSAL AGSNVGVFVG ASSLDNSLHF ISDISAADAH FVTGNALSII ANRISHVFGF
TGPSLTIDTA CSSSLVAFDR AVKAIESGEI DTAVVAGVNI LASPFHFIGF SRAGMLSPTG
RCRPFSGEAD GYVRAEGGVV TVLSRLDRAS AAGWTPRAVV MASGTNSDGR TNGIAMPETR
AQQRLLEELY ERRGIDPNRL AFIEAHGTGT LVGDPAEALA IGSAVGKRRA SPLPVGSVKS
NIGHLEPASG LAGMLKALNA LERRELPASL HLDTLNEYID FEALNLTPAA EPLPLDAESR
VAGISSFGFG GTNAHAVIRL PEAHELPARD APAAAPVLMI SAHDPQALSA LADAYADRLE
VEPAPERLAH AAAHGRARLA HRLAVSLKAP DAPARLRRIA RGTGEGALLR GAPRGSGSGV
AFVFTGNGGQ YAGMGRAAWQ ASPAFRDAVE EIDALFEPLA GWSLAEAFRQ PPNEAKLAAT
EIAQPLIFAL EVALARTLMA NGCMPAAVVG HSVGEIAAAY IAGALSLSDA THLIYWRSQL
QGETRGSGVM AFLMASPAQA GELVAAAAQP EVVIGAVNAP KGVTLSGPAG AVDAVLRLAR
RRGVVGKRLG IDYAFHSPAM GPLYEHLFEV LTVLVPRAPA IPFISGVTGE PIEDASLDAY
YWWDNIRQPV QFDAAVRTAA RDSSIGIFLE IGPKAVLTGF LREILADAGR PATVLASLQE
KDTADEDPVE RTLLAALVNG AAVDEAKLFG PPAPPGRIEL PKTPWHRQPI RPPRTGEAID
LIGTGIDDHP LLGARLLGDG SEWRGTLDID SRPFLADHKV GGNVVLPATA LAEMALAAGH
GALGTDRLRL EEFAIFSALR LSAGESLETR VAVDAEGGVV ISSRARGSEE WSLHARGRVL
ADSGVSAPLA PPPEVEGESE LDAEALYAAA ARLGLDYGPS FRLVRSARRI GAEIHLDLAA
PDEPQEPYLL PPTLADAALH GLVLAAEGQP TRAGTAYLPI RFARLTVRGA AAPVRAALTV
RRASPRALEL DVALFDETDT ETARIEGVEL RAVALAAEDE LDHDFRQSYV RLGPARTDAG
SRIETFLDAA GDVPTADDAL MLDALAYAIA HRAVAGVAGE EMLAAERLDI EALIAQGRLS
AERRGAFLAL LDILSEGGLA RYASEEGWRV LPQSDLPTPE PLLHEIERIA PDRAAELAIG
ARLVVDLAAH LRGALALTHA AGLVDQWEAA SPAARAVAEQ AVALVKAASR DLDAPLAVLL
VERHGTVLKA LRPLAEAGAI NLAILPADAS ARPRLADRVR PSEGMALCDE EALPAADLVL
HADPRQPLDP AGELGRRLGA ALRPGGALLA LGFAASGFAR LLTIDAPAGT VRGERRLRSA
RAATDIAVIG APAPEAPDHR VVGEAVMALL REDARSCLVS DAGHVLDPDL SLPAARSGAV
LVWRPSPGVD AASLAAAMDE TRALLEVLRA GADAGSPALR LLVDGDPLGG SPAAAALWAF
ARTAMNEYPD LDVRLIALDR TVVDGAAMNE LARAIVGLPG ERELVLDDRG LKAVRLAPAA
PERAVGSEAA ARLAMQRPGS LDRLVWRPES RRAPEAGEIE IEIAAAALNF RDVMFAQGLI
GDDMLASGFA GPTLGFECAG RVVRVGDGVA DIRPGDEIVA FAPGSFATHT TVPAAAVLPV
PAGVSLDAAA TLPVAFLTAW YGLVQCARLE AGETVLIHGA AGGVGLAAMQ IAKARGARIV
ATAGSPEKRA LVRLYGADAV YDSRDTQFAE TLRADGGCDV VLNSLAGRPM ELSLRALKPF
GRFVELGKRD FVANTSIGLR PFARNLTYFG VDADQLIAAR PALAQQMLAE LKRLFEAGTL
RPLPHRVFAA DDVRAAFRLM QGSGHVGKIL VRPPADISAM PAEKPAFVAA AEGVHVVVGG
TGGFGRETAR WLAERGAKHI VVASRRGVID PPLEVDGAEI VAESLDVRDA RACAAFIEEL
RMRHGRIAGL IHTAMVLDDA LIRDLDYDRF EEVLAPKVDG ARNLDVATAG LDLDYFVLFS
SATTLIGNPG QAAYVAANAY LEALARRRRE EGRPALAIAW GAISDAGVLA RNAATSEKLS
RRLGLGMLTA NAALEFLGAC LTDEATSPVV VHAPVDWRVA RELAVMGGAS FAALRPAIDD
PATAAGEADL LALIQGQSDA EARTTVLRLL TGELARILRL PAEAIEPTRP LSDIGMDSLM
GLELDMEMQR RHKVALPMLG LGAGATLEDV SDKVLRKLRP SGEASGGESS APGIQIPEEG
AGLIDRHLRA EPTAAAIQSL HAKASADSRR DGSLLR
//