ID A0A3F2VB60_9GAMM Unreviewed; 3692 AA.
AC A0A3F2VB60;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=SDR family NAD(P)-dependent oxidoreductase {ECO:0000313|EMBL:RLP56431.1};
GN ORFNames=D6160_03320 {ECO:0000313|EMBL:RLP56431.1};
OS Ketobacter sp.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Ketobacteraceae; Ketobacter.
OX NCBI_TaxID=2083498 {ECO:0000313|EMBL:RLP56431.1, ECO:0000313|Proteomes:UP000280615};
RN [1] {ECO:0000313|EMBL:RLP56431.1, ECO:0000313|Proteomes:UP000280615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BinD {ECO:0000313|EMBL:RLP56431.1};
RA Xu J.;
RT "Metagenomic reconstruction reveals the metabolic diversity of the novel
RT genus Ketobacter and the trajectory of genomic evolution within the
RT Alcanivoraceae family.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467}.
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:RLP56431.1}.
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DR EMBL; RAHY01000001; RLP56431.1; -; Genomic_DNA.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000280615; Unassembled WGS sequence.
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:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08955; KR_2_FAS_SDR_x; 2.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 3.40.50.11460; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
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; IPR013154; ADH-like_N.
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; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
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; 2.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 2.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 2.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 5.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000280615};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..458
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1428..1503
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1520..1946
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3564..3639
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 3643..3692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3658..3675
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3692 AA; 398073 MW; B0405B680289CDDF CRC64;
MSTSNATDTA KLLKQALKEL KKSKDSVSRL EKEKYEPIAV IGLGCRLPGG ANSPEQLWDL
LDKGGDAITE MVDQRWIADD YYDSDPEAVG KLYTKANGLV DDVDMFDADF FGVAPVEATL
MEPQQRLLLE TTWDSLEHAG IAPDSLMGSK TGVFVGICHM GYSHMQAQSG SLEDISPYNG
TGNAHSVASG RLSYLLGLQG PSLSVDTACS SSLVAIHLAV QSLRKGESDM ALAAGVNLIL
EPTTSMIFAR AGMLSPDGRC KTFDGGANGY VRGEGCGTVV LKRLSDAMRD GDNVLAVVRG
SAVNQDGKSQ GITAPNELAQ EKVLRAALED ARVKPNEVSY IEAHGTGTPL GDPIELAALN
TVYGKERTEK LVVGSIKTNM GHLEAAAGVA GFIKLVLSIH NQAIPKHLHF DTPNPYIDWS
TIAIDVPTEQ RAWNSPTRIG GLSSFGFSGT NCHIIVEQAP IPSDIADEKP AQQFAPDLLT
ISAKSKEALQ AYLAAYADAL TLPTVQDRDW SDVCFTASTG RTHFRHRATI AAGSAQQAAD
RLNALLKNGT SEGINIADVG TNPAKLAFMF TGQGAQFAGM GQELYQRFPV FQQALDSVAE
LMKEELDQPL LSVMWGDNSS LLNETQYTQP AIFALQYALT QLWTATGVQA ACVTGHSIGE
YAAAVYSGVM SLADAVRLIC ARGRLMASEC EKGSMAAVFA SAEETRNVIE TLDSVIDIAA
VNGPRNCVIS GEKPAVEQAV ALLTDEKIKA KLLTVSHAFH SPMMQPMLEA FAKEVAKVTL
KAPRIRFISS KTGKTATQDV KKPEYWVEHV RDAVLFLDAA KELGNQKIQA CVEIGPGANL
VKLAPQCIES TQPINYLHSV DREAIESEHL TSVIAGLHCS GAVINWNTLF IGGALARVDL
PTYPYQRQSY WVDKIRHGNY SKASGMSFGR LLYATDWFET ALAGDSSGEG DGQSTLFDDM
VIIGNQPAWV SALNSSATIL HLDGQSNADA IKAAVAPLQE KAQQNGKILP VLITAPNMPS
QLQEVPSVVH SQIPVVMAAA KAIVAGSDST NPARLWCVSE NAYNLDQINL AAYPLIGFAK
GFALEAGELW GGIVDLSGSA EEQASALWAE LNANAQEDVV KYQGATRSVL RLGQDRLNDA
KVVTLDADAS YLVTGGLGGL GLYVADALAR SGAKHIVLMS RRGSLDSLEG ERAELIGRLQ
QQGVEIKVAN VDVCDEAALA DLVGELAQSA NPLKGVVHAA GISEIALAHE MQIEQWQKVT
QSKLEGALNL HNATQSVELD LFVVFSSIAS VWGSGGMAHY AAANHFLDGL VDYRIANGLP
ATAFNWGPWG GAGMAAGEAS DEAERRGLTP FDPESAIELL SKAWHGGAAH QTVADIDWTR
FREIVEMRRP HPMFGTLGRS LAATSGVTGE KSAFFKSLYP LEVEARVEQI VGYLQGLLGK
VTGKAEGEIV DPEMPLMDLG IDSIMALEIK KQLEADTGQA MKATLIFDYP TINKIAEYFS
VALYGAESEA QSVSVGSYHG EAIAIVGIGC KMPMAPNGPG DFWKLLKNGE CGINDEPSDR
WDLTKYLDKN EDAPGKTYTL SAGLVDNIES FDGKLFGIAP RELESMEPQQ RLVLEAAWSS
LENAGYAPNA MNGSKTGVFV GVGANEYIRA CATGAREDDI MFIPTGNALN VIAGRVSFNM
GLQGPAMTID TACSSSAVAI HLASQSLRNG ECDMALAGGV NAMVMPETFV ALSKAHMLSK
EGRCKTFDES ADGYVRGEGV GVLALKRLSD AERDGDNIVA VIKGSAVNQD GRSSSLTAPN
GPSQETVIRA AVANAGLTVD DIDWVETHGT ATPLGDPIEV QSLESVYCAN RNSDNPLIIS
SVKTNIGHLE SAAGVSSVMK AALSLQHGEI PPHLHFNKFN PHIAVDASKF TIPTESREWK
SGERKRRVGI SSFGFSGTNV HMILEEAPVR SDVINAVERN SHVLTLSGKT EGAVLGLAKR
YAEFLQQDYM NPKEVAFADI AFTANTARQH FEHRIAVVAP DSAAAIDKLK QVAEGVSVAG
SFSSDGVAAV TAQAWLFTGQ GSQYAGMAKE LYDTNPAFKA RLDECEVLFE QETGDSLLQL
LWGDRSAEID NTQYTQPAIF ALEYALACHW QSLGLKPNVM VGHSVGEYAA AVLAGVMSLE
SAMRLIVARG RLMVEQCETG DMAAILTTYD KVEALLQGVD DVQIAACNAP GNTVVSGTAA
GIAAIIEKAG AEDIDARLLT VSHAFHSNLM QPMLAEFKAV AESIEFHPAK LDIVSTVSGS
LNQGELSTAA YWVEHVKRPV LFVNAVQKLP EMKVDLCLEI GPGSTLTGLA TQILGTDKCR
FVHTLRMKQD SGRQFNLAAA QLYSLGVDIK WAAFDSPYSR QRVAAPSYAF DRKRYWLGDN
DNGMVGGGGS MGQVTENLLS VMHSPMSDDY FFENNFGVNH PFNLDDHRLY EVVVAPGAFH
VANTILCARD VYGDKPVVLD DVVFPEPFIL EEGQKRRLHY GFKKLAAKDG GPDFEVKGFS
RDEKANADAD WTMHASMNVS ACEQPDSTQV LTAEDVEQIQ SRALRTFDGQ TFYNEMWKVG
YQLGSQFRWI EGFWRRPGET LTKLRLPESA LEQGKYIIHP GLMDSCFQSS ALATMHTDFD
TSKVDAIYIP FALENLRFFR KPSTELWCHV KIKNPPEDPE AVVESYSHTI QVYDDQGNIL
IDVDTLHSKR APKEALLRAI SKDPFDGHYD VHWKTQSIPA DQELAALKGS YLVIGETSPL
AAAIYDELSA NTDITTWRIA CDSADGFNQE DNTIRLNPED GGQWMQMIGA VGGLANVSGL
LYVAPQEMPA SDVLGLQKRI FSPILNMLKA LQLMSAAGSP RLWCVTESAV AVQRSDSYIN
PAQTALLGFG KVLDMEHSEY ASVLVDVDSE GNSRAARSVI TEMQQAGNEK QVAYRRGARL
VARLARTGIE SAGMSIPEAP YRLIIEKKGT FEDLKFVPFE PRTLGSTQVG VRVLSAGLNF
RDVMGVLDVY PGEAGPLGGE CIGEVIELGA EVKDFKVGDR VMLPLTESCM STQTLSEELL
TCRVPNNLSI NEASTIPVVY CTALHGLKNL AKLKKGERVL IHAGAGGVGL AAIYIARHLG
AEVFATASEK KRDYLRKIGV EHVFDSRSLD FAQQIRAATG GEGVDVVLNS LAGEFITTSM
QLLNPNGRFI EIGKADIWTQ DRVTAFRDDI YYEAFDLVVV TLQDPMALRK LMDEIVENIE
AGHYKPLPFT VFRHKEAMEA FRYMAQGKHV GKILINRDDP EITVQSDRSY LITGASGGLG
MLFANWFADQ GAGEVILAAR RDVRDVDAEG VKEIEAKGTK VTTVKADSGD AESVQAMISA
VQENSLPLAG VIHAAGVLAD AFVVNQDMAS FEKVMAPKLA GAWYLHNATK HLNLDMFVLF
SSLSSLLGAP GQANYAAANA FLDGLAQHRR ALGMPGIAIN WGPWGEVGMA ANSQVEANAK
ASGVHLIEPQ DGLNWFAQVL ESNPVQRGLM VIDWAALANM TGSIPAFLSE LDVKASVGVD
ADLQKMADEF RSSLLDAPID ERTPMLVDMI CEQIKRVMGL DESDTINPNQ PLQELGLDSL
MAVELRNILC ALIGKQLPAT LMFKYPTVSS LSTFLIQDMF PEEAAEEAQQ EEQAAADAQA
QQDEDENDQL DDLSDDELAA MLAAELGEDD ED
//
