ID A0A088QGW3_9CORY Unreviewed; 3034 AA.
AC A0A088QGW3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Ketosynthase family 3 (KS3) domain-containing protein {ECO:0000259|PROSITE:PS52004};
GN ORFNames=DR71_1675 {ECO:0000313|EMBL:AIN82717.1};
OS Corynebacterium sp. ATCC 6931.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1487956 {ECO:0000313|EMBL:AIN82717.1, ECO:0000313|Proteomes:UP000029247};
RN [1] {ECO:0000313|EMBL:AIN82717.1, ECO:0000313|Proteomes:UP000029247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6931 {ECO:0000313|Proteomes:UP000029247};
RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|ARBA:ARBA00005254}.
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DR EMBL; CP008913; AIN82717.1; -; Genomic_DNA.
DR RefSeq; WP_038629446.1; NZ_CP008913.1.
DR STRING; 1487956.DR71_1675; -.
DR GeneID; 64052863; -.
DR KEGG; coa:DR71_1675; -.
DR eggNOG; COG0304; Bacteria.
DR eggNOG; COG0331; Bacteria.
DR eggNOG; COG2030; Bacteria.
DR eggNOG; COG4981; Bacteria.
DR HOGENOM; CLU_000114_7_0_11; -.
DR Proteomes; UP000029247; Chromosome.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00828; elong_cond_enzymes; 1.
DR CDD; cd08950; KR_fFAS_SDR_c_like; 1.
DR Gene3D; 1.20.930.70; -; 1.
DR Gene3D; 3.30.70.3330; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.25.70; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR047224; FAS_alpha_su_C.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR10982:SF23; FATTY ACID SYNTHASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18094; DNA_pol_B_N; 1.
DR Pfam; PF08354; Fas1-AflB-like_hel; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF16073; SAT; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000029247}.
FT DOMAIN 2472..2949
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1660..1723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2363..2396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1660..1676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1707..1723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3034 AA; 321646 MW; 9BCE6F9F1A87B466 CRC64;
MKYEKLATLQ TNVVNAPDLG TFAVTFAGQS QPWLDTLSSV MASGNSKKLR EVFTRAEELL
APLDDDLIGQ LPAGFDPFGW AISLVTDDPF TGDTTNPAVS VPGIVLAQLG IVELLAKQGI
NIDDAIAVTG HSQGVLTAEI VAHPEKAAEL LALARLIGVA CARGSRVAGF GRAPMMSISG
LTVEELEPFL SQDCVIGLKN TQTTSVVIGK QDELEQLAEQ LTAQQQKGRA VECTVLPVSG
AFHHPALAPA AAWVVERAER IGLDAETADW LARAILVDSS DWSAEVRGLI DQGATTILDL
GPHTGVVKLT ERNAEGYGVA VIAAATAAGR SILSESDIEY PTSWLEFAPR LVTGVKPRVE
TKFTKLTGRS PILLGGMTPT TVDPEIVAAA ANAGFWAELA GGGQVTPEIF EANVARLSEL
LEEGRSAQFN TMFLDPYLWG LHIGSRRLLP RAVAAGRPID GVTISAGIPE VDEAVELVKQ
LREGGIPYIS FKPGTIAQIE SVLEIADTLA QHGTPYPIIM QVEGGRAGGH HSWEDLDDLL
INTYAKIRRR DVVLAVGGGI GKPEQSRDYL MGTWSTRYGL APMPVDAVII GTAAMAAKES
TASESVKQML VDTVGTDNWI PAGSAMDGMA SGRSQLGADI HEIENAAARA GRLLDEVAGD
LTKVTERRAE IIEAINSTAK PYFGDVSTMT YAEVLNRYLE LCAPEGTFLD PTWSTRFVAL
VDRVEARLSA VDAGTFAALA DGDSLRTQPR SEISRLSGLL DLDTQLHPAD VTFFISELCR
TPGKPVPFVP VIDAEVRRWW RSDSLWQAHD SRYDADQVCI IPGPQAVSGI TRANEPVAEI
LGRFEKATAQ ALMDTGYLPE VPVDALSRML AAPVIWWAGR QQPNPALALG AEHEWVCVSD
ASDVSRSQRL EHPGTGAILE IIGADGSNDE GGEDLVWAQL TVPLPDAAGE NTKLRIRLCQ
SAAVGAVPVV KHEDAAAAMR ELTRIAAGGE LANVVDGVAE WESVWDPMAM ADYDAVTIAA
AGDESQAAVP DALVGHAWPA IFAAVAQART ETGIDVVEGM LALVHLEHHI RMIGALPQKT
TTLRISARVD EIVDTDLGRL VVVRAEVRDG DTLLATLSEC FAIRGRNGGE TARTNTVPFP
TVTDTPRSFR GALTVEAPKA MEPFSCVTGD RNPIHVDSRA AALAGLPGVI VHGMWLSAMA
EHAAVATSDA GIGNRVIEFT ATMLSPVLPG QEVKFSVERR GFDDRPGAGE VREVTATVDG
ELVLTATAVI AAPKTAYVFP GQGIQSQGMG LSARTRSVAA RRVWDQADAM TREKLGFSVL
AIVRDNPVEV VVDGVRYFHP EGVLNLTQFT QVAMATLGLA QVAELREAGL LDETAHFAGH
SVGEYNALAA LAGALDADAV LEVVYRRGLT MHELVERDEQ GRSNYGLCAL RPDKIGVGED
EVTEFVNRLS QEIGEFLEVV NLNLAGKQYA VAGTVAGLAA LAEQCERRSS DGKGYVRIPG
IDVPFHSSVL RDGVDSFRKH LERLLPAEIA PELLVGRYIP NLTATSFELT EKFVRQMAAV
VDSDILENIL ADFDSAAENP ARLARMLLVE LLAWQFCSPV RWIETQDLLL EDLGVSRIVE
VGVGTAPTLA NLAARTCQLP RHRSRDIRVL NLERDADAVF MRDQIQPEKT EPESEVTTEQ
DSAQALSGES GAAGETGEAG AAAPTVSPDQ SAATEQSTTI TSAATPATEV ADIAVSPAQA
LEVLICQWTK VRPDQLGAAD SIETLVDGVS SRRNQLLLDL GVEFDLGSIE GAADAELADL
KDKIDSLASA YSAFGPILSE AIADGIRRIT GPAGAGANYL DDYVLGEWQL GKGWATAVSA
EVMLGTREGA SLRGGDLAHL APAAPTNTAE LNQLIDEAIL AVATQRGVAV AKPSASDSGA
GVVDSAALTE FADKLTGQRG ILATAARTIL EQLGHEITDD IDFDAEDADS NLVNLVTAEL
GADWPKLVTP TFTPTKAVLL DDRWATSRDD LARLWVAADG HVAGTAPGSI HETAVEQAQW
WAAKADEAGR TQLASIYRQL ADEVITNVDE LPMSSDIAVV TGASPNSIGS AVTAQLLSQG
ATVVVTTSRL GRERLSFYKQ LYRVNAQGEA KLWVVPANLS SFQDLDSLID WIGTEQTTTI
GAEVVVTKPA LSPTLLFPFA APTVSGSLAD AGPASETQMR LLLWSVERLI AGMSALGVDN
NLQHRLHVVL PGSPNRGRFG GDGAYGEAKA ALDAVVARWN VEDAWRTRTT LAHAQIGWVR
GTNLMGGNDP LVAAVEAKGV RTFSTEEMAA ELIELASSET RKNAQTRPIQ ADLTGGLGDV
DLNIAQLAQE AAQAAGLSAQ NSEVASGARS QEPSSSRVLS SLPSPRRPIS QTTPTFGDIA
AAPEDMVVIV GAGELGPYGS SRTRFEAEVD DISAAGIVEL AWSMGLISYE GGWRDADGQP
LAESDIASRY RDEVLARVGV RRYADDGDLV DNTMTELTTV YLDRALSFAV RDRAAAETFV
SSNPDNTTAS FDAETGQWLV TRAAGTPVQV PRRMAMSRYV GGQIPQGFDP ARYGIPADMM
DNLDRVSLWN IVCTVDAFLS SGFSPAQLLE AVNPARVSST QGTGIGAMES LRSLYIDGLL
GQPRANDVLQ EALPNVIAAH VMQSYVGGYG QMIHPVAACA TAAVSVEEGV DKIALGKADF
VVAGGFDDLS AEGITGFGDM AATADSATME DKGIDHAYFS RPNDRRRGGF VESQGGGTVL
LARGDIARDM GLPVLGVVAY AQSFADGAHT SIPAPGLGAL AAAQGGEKSR LARALAALDV
TGDQVAVLSK HDTSTNANDP NESELHERIA DELGRERSNP LLVVSQKSLT GHAKGGAAAF
QIIGLTQVLR SGIVPGNRSL DCVDPALAEH SRLVWPTKAV NFGNTLPLKA GFVTSLGFGH
VSALVAVVHP EAFYQAIVQH DGAEAAERWR SAAHNREAAG LRRIDEAIYG GETLYERPRE
RNLADGGRFG SPAALEKAVL LSDGARLIDG VLQP
//