ID L0J007_9MYCO Unreviewed; 3082 AA.
AC L0J007;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=3-oxoacyl-(Acyl-carrier protein) reductase {ECO:0000313|EMBL:AGB24659.1};
DE EC=2.3.1.- {ECO:0000313|EMBL:AGB24659.1};
GN ORFNames=Mycsm_04419 {ECO:0000313|EMBL:AGB24659.1};
OS Mycobacterium sp. JS623.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB24659.1, ECO:0000313|Proteomes:UP000010844};
RN [1] {ECO:0000313|Proteomes:UP000010844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL Submitted (OCT-2011) 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; CP003078; AGB24659.1; -; Genomic_DNA.
DR STRING; 212767.Mycsm_04419; -.
DR KEGG; msa:Mycsm_04419; -.
DR PATRIC; fig|710686.3.peg.4454; -.
DR HOGENOM; CLU_000114_7_0_11; -.
DR OrthoDB; 4746285at2; -.
DR Proteomes; UP000010844; 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; cd03447; FAS_MaoC; 1.
DR CDD; cd08950; KR_fFAS_SDR_c_like; 1.
DR Gene3D; 1.20.930.70; -; 1.
DR Gene3D; 3.30.70.2490; -; 1.
DR Gene3D; 3.30.70.3320; -; 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; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:AGB24659.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transferase {ECO:0000313|EMBL:AGB24659.1}.
FT DOMAIN 2543..2998
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1182..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1730..1781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2409..2429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3044..3082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3044..3062
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3082 AA; 329119 MW; 6D248FBCF206D1FD CRC64;
MTINEQSRVT TSRENDPSEV LAGTHALVDR LNAGEPYAVA FGGQGGSWLE NLEELVSSAG
IESELSEVVG EAALLLEPVA RELVVVRPIG FEPLHWVRAL AAEEPLPSSK QLTTAAISGP
GILLAQMAAI RAVARQGLDL YMTPPVAMAG HSQGVMAAES LRAKGARDAE LLALLQLIGA
AGSLVSRRRG MVGRGDKSPM VSVTNVDPER IAELLEEFST DVRTVLPPVL SIRNGRRSVV
ITGTPEQLGR FELYCSNITE KEQAERKNKV RGGAVFSPVF HGVQVEVGFH TPRLADGVEM
VERWAEKCGI DAELAHEMTE SIFVRPIDWV GEVERLHDAG AKWIIDLGPS DTVTRLTAPI
IRGLGVGIVP AATRAGQRNL FTVGGEPEVP PAWSSYKPTT VKLPDGSVKL STKFTRLTGR
SPILLAGMTP TTVDAKIVAA AANAGHWAEL AGGGQVTEEI FEGRIAELTQ LLEPGRAVQF
NTLFLDPYLW KLQVGGKRLV QRARQSGAPI DGVVVSAGIP DLEEAVDLID ELNTVGIRHV
VFKPGTIDQI KSVINIAAEV PGKDVIVHIE GGRAGGHHSW EDLDDLLLAT YAELRKLSNI
TVCVGGGIGT PERAAEYLSG TWAEEYGFPA MPVDGILVGT AAMATLEATT SHAVKQMLVE
TTGTDHWISA GKATGGMASS RSQLGADIHE IDNTASRCGR LLDEVAGDAE AVAARRDEII
AAMANTCKPY FGDIGDMTYA QWLRRYVELA IGDDDSTADT KLPGTPWLAD TWRDRFEQML
ERAEARLHPQ DSGPIETLFN DVALLDDPEQ AIALLLTRYP EAETLQLHPA DVPWFVTLCK
MLGKPVNFVP VIDKDVRRWW RSDSLWQAHD ARYTADQVCI IPGTQSVAGI TRVDEPVGEL
LDRFEQAAID AALATNGQPV AVVSRRQARA DVTGPLAVVL DSPDVRWAGR TSINPVHRIG
APDEWQVNEN RSATHPSTGA RLELADGTVT LAVPLSDIWI NIRFTLPSCT VDGGMPVVTV
EDASTAMRSV LAIAAGVDGP EALPPVHDGT AKVTVGWDPE EVADHTGVTA TFGAPLAPGL
ALVPDALVGH CWPAVFAAIG SAVTDDGFPV VEGLLSLVHL DHAAHLLTAM PKTKAELTVT
ATVSAATDTE YGRVIPVSVN IASADGTALA TLEERFAIRG RTGAAELSDP PRAGGAMTDN
ATDTPRRRRR DVKVAAPTDM SAFAVVSGDH NPIHTDRAAA LLAGLKSPIV HGMWLSAAAQ
HVVAATDGKP APPARVVGWT SRFLGMVLPG DEIDFRVDRV GIDRGAEIIE VAARVGSELV
MSATAQLEAP KTVYAFPGQG IQHKGMGMEV RARSKAARKV WDTADKFTRD TLGFSVLHVV
RDNPTSLIAS GVHYHHPDGV LFLTQFTQVA MATVAAAQVA EMREQGAFVE GAIACGHSVG
EYTALACVSG VYELEALLEV VFHRGSKMHD IVPRDHLGRS NYRLAAIRPS QIDLDDADVK
QFVADISERT GEFLEIVNFN LRGSQYAIAG TVRGLEALEE EVERRREISG GKRSFILVPG
IDVPFHSSVL RVGVADFRRS LERVMPRDKD PNLIIGKYIP NLVPRPFTLD RDFIQEIRDL
VPAEPLDEIL ADYDTWRNEK PAELCRKIVI ELLAWQFASP VRWIETQDLL FIEEAAGGLG
IERFVEIGVK SAPTVAGLAT NTLKLPEYSH NTTEVLNSER DAAVLFATDT DPEPEDDVEE
TAPAPEAAPV EATAPAAPAQ AEGGPHPSVA PTGAPRPDDI GYDAADATMA LIALSAKMRI
DQIEPLDSIE SITDGASSRR NQLLVDLGSE LNLGAIDGAA EADLAGLKGQ VAKLARTYKP
FGPVLSDAIN DQLRTVLGPS GKRPAYIGER VKKTWELGDG WVKHVTVEVA LGTREGSSVR
GGELGGLHDG ALADAATVDK VIDAAVVAVG ARQGVPVSLP SAAGGAGGGV VDSAALGEFA
EQVTGRNGVL ASAARLILGQ LGLDTPVPVP EATDAELIDL VTAELGSDWP RLVAPTFDGR
KAVLFDDRWA SAREDLAKIW VLDESEIDAD WQRISTRFEG AGNVVGTQAT WWQGKALAAG
RNIHASLYGR AAAGAENPGK GRYTDEVAVV TGASKGSIAA SVVSQLLDGG ATVIATTSKL
DDDRLAFYRN LYRDNARFDA KLWVVPANMA SYTDIDKLVE WVGTEQTESL GPQSIHLKDA
QTPTLLFPFA APRVAGDLSD AGSRAEMEMK VLLWAVQRLI GGLSHIGAER DIAARLHVVL
PGSPNRGLFG GDGAYGEAKS ALDAVVSRWK AESSWAQRVS LAHALIGWTK GTGLMGHNDV
IVDAVEEAGV TTYTTDEMAS MLLGLCDIES KVAAAREPLQ VDLTGGLAEV DLDLSELANK
AREEMLGEAA VEETDDEGTI RALPSPPRGY QPAPAPAWDD LDVDSADLVV IVGGAELGPY
GSSRTRFEME VDNELSAAGV LELAWTTGLV KWEDDPTPGW YDTQTGDLVD EGELVERYHD
AVVERVGIRE FVDDGAIDPD HAAPLLVSVF LEKDFTFVVS SEQEAREFVQ FDPEHTVIAP
VPDSGDWQVT RKAGTEIRVP RKTKLSRTVG AQIPTGFNPM VYGVSQEMMN SIDRLAIWNL
VTTVDAFLSA GFTPAELMRW VHPSLVACTQ GTGMGGMTSM QTMYHGNLLG RNKPNDILQE
VLPNVVAGHV VQSYIGSYGS MIHPVGACAT AAISVEEGVD KIRLGKAEFV VAGGYDDLTL
EAIIGFGDMA ATADTEMMRA KGISDSKFSR ANDRRRLGFV EGQGGGTILL ARGDLAFKMG
LPVLAVVGYV SSFGDGVHTS IPAPGLGALS AGRGGRESQL ARALAKLGVG PDDIAVVSKH
DTSTLANDPN ETELHERLAD AMGRSPGAPL FVVSQKSLTG HSKGGAAAFQ MMGLCQILRD
GVIPPNRSLD CVDDELAHAA HLVWLRDTLR LGEKFPLKAG LITSLGFGHV SGLVALVHPQ
AFIAALDPEQ RKDYQQRFEA RVLAGQHRLA SAIAGGPALY EKPADRRFSH EAPEKRQEAE
MLLDPASRLG DGDVYVRPSG VR
//
