ID Q6E7K0_9CYAN Unreviewed; 3302 AA.
AC Q6E7K0;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE SubName: Full=JamJ {ECO:0000313|EMBL:AAS98781.1};
OS Lyngbya majuscula.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Lyngbya.
OX NCBI_TaxID=158786 {ECO:0000313|EMBL:AAS98781.1};
RN [1] {ECO:0000313|EMBL:AAS98781.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JHB {ECO:0000313|EMBL:AAS98781.1};
RX PubMed=15217615; DOI=10.1016/j.chembiol.2004.03.030;
RA Edwards D.J., Marquez B.L., Nogle L.M., McPhail K., Goeger D.E.,
RA Roberts M.A., Gerwick W.H.;
RT "Structure and biosynthesis of the jamaicamides, new mixed polyketide-
RT peptide neurotoxins from the marine cyanobacterium Lyngbya majuscula.";
RL Chem. Biol. 11:817-833(2004).
RN [2] {ECO:0007829|PDB:5DOV, ECO:0007829|PDB:5DOZ}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 260-594 IN COMPLEX WITH NADPH.
RX PubMed=26526850; DOI=10.1016/j.str.2015.09.013;
RA Khare D., Hale W.A., Tripathi A., Gu L., Sherman D.H., Gerwick W.H.,
RA Hakansson K., Smith J.L.;
RT "Structural Basis for Cyclopropanation by a Unique Enoyl-Acyl Carrier
RT Protein Reductase.";
RL Structure 23:2213-2223(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC Evidence={ECO:0000256|ARBA:ARBA00023693};
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|RuleBase:RU003707}.
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DR EMBL; AY522504; AAS98781.1; -; Genomic_DNA.
DR PDB; 5DOV; X-ray; 1.80 A; A/B=260-594.
DR PDB; 5DOZ; X-ray; 2.26 A; A/B/C=260-594.
DR PDBsum; 5DOV; -.
DR PDBsum; 5DOZ; -.
DR SMR; Q6E7K0; -.
DR BRENDA; 1.3.1.104; 12270.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd06558; crotonase-like; 1.
DR CDD; cd05195; enoyl_red; 2.
DR CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 6.20.390.20; -; 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; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 4.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR049490; C883_1060-like_KR_N.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
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; IPR013217; Methyltransf_12.
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; IPR029063; SAM-dependent_MTases_sf.
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; PF08240; ADH_N; 2.
DR Pfam; PF13602; ADH_zinc_N_2; 2.
DR Pfam; PF21394; Beta-ketacyl_N; 1.
DR Pfam; PF00378; ECH_1; 1.
DR Pfam; PF18558; HTH_51; 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; PF08242; Methyltransf_12; 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; 2.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 4.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5DOV, ECO:0007829|PDB:5DOZ};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0007829|PDB:5DOZ};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 709..1134
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3176..3251
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1137..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 420
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:5DOZ"
FT BINDING 422
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:5DOZ"
FT BINDING 423
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:5DOZ"
FT BINDING 442
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:5DOZ"
FT BINDING 443
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:5DOZ"
FT BINDING 446
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:5DOZ"
FT BINDING 461
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:5DOZ"
FT BINDING 462
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:5DOZ"
FT BINDING 508
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:5DOZ"
FT BINDING 511
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:5DOZ"
FT BINDING 531
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:5DOZ"
FT BINDING 533
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:5DOZ"
FT BINDING 588
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0007829|PDB:5DOZ"
SQ SEQUENCE 3302 AA; 364520 MW; D150083674597EA2 CRC64;
MAKLNLNQDL GNGNSEVVQL AELGDGIVQI TMNDEKNRNS FSKNFIDKLF RCFELVNQNP
IYKVVIIAGT SHYFSTGATQ EQLQSIFREE IKFTDFYEIL TLALDCPLPV IAAMEGHALG
GGLNLGLYAD FLVLSRESFY ANNLMKYGLT PVGSTSLILP KKLGAELGQE MIYTGRQYRG
EELAQRGIPF PVLPRKEVLN SARKLAKEIA EKPRLSLLAL KENLTAEIRT KLPEVVSKEL
EMHEKTFQQV KVASQAIHQT TSQPVQLKIA SYGLLKNLTW VSLENQVPGV GEVKVQIQAV
PVNFRDILNA LGMLQEHNQT KLGITSVDHL TFGFEAVGVI VGVGLGVSQW QIGDEVMVIG
CHDAFSSFII CSPNNLVAKP ANLKLIEAAT IPIPFFTAYH GLYNLAKIQS GERVLIHAAS
GGTGQAAIQL AQFWGAEVFA TTSPQKMAVL REQGIKHVMN SRTTEFANEI RELTQGKGVD
VIFNSLTHGE YIQKNLDVLA LEGRYIEISK RKIWSHSQVA QKRSDIKYFP FDLLEEFNRD
NQLYYQIWKK LIQCFENKEL HPLVYKTFPN EDIVEAFRYL QRSKHIGRVV VTMPEIYSHK
ESSSYRLPNQ GQMSQQEEVL QQLQSGEVSL EDAEKLLLEV TGEEVQQKIL FKQINNGQNQ
QIKKDKSENI LALLSSGEIS LENAEKLLLE PESTKETEKE TDAITPAQNT DIAIIGISCR
YPGAKNYREF WENLQNGVDS VTEPPPGRWE GQNWYHPDPE HPDTSYCKCA GFIDDIDKFD
PSFFQISPGE AQFIEPQQRI FLEEAYHAIE DAGYAPDFLK GRQCGVFVGA VKSDYSKLLS
DSGLGTHRLA LSGNQLSIVP ARIAYFLDLR GPVMTVETAC SASLVAVHQA CESIKRGESE
LALAGGIHTM LTPDFQILSS QFQMVSPAGR CKTFDAEASG TVWSEGCGVL LLKSYEQAIR
DQDHIYGVIK GTGINYDGNT NGISAPSSQS QTRLEETVYQ KFGISPETIS YVEAHGTATS
LGDPIEVEAL TETFAQWTNR KQFCAIGSVK TNIGHASTAA GVSGLIKTIL CLKHQKLVPS
LHFNQPNPHI DFANSPFYVN TEFQDWEAQE GKPRRAAVSS FGFSGTNAHI VIEEALREGN
RQQATGNSED YRKGNRQQAT GNSEDYLERP VHLLTLSAKT ETSLAELVRA YQNYLKTYPG
LGLADICYTA NTGRTHFNHR LAVVAADQQE LVEKLQQHQQ GDEVAGIYSG QQEYNTTTAK
IAFLFTGQGS QYVNMGRELY QQAATFREAI NQCDDILKTV ETFRDKSLRE ILYPADDSSD
SSLLNQTAYT QPVLFAIEYA LCQLWKSWGI EPDAVMGHSV GEYVAATVAG VFSLEDGLKL
IAARGRLMQQ LPAGGEMVSV MANEAKILET LNAMSRSDKV AIAAINGPQS IVISGEGEAV
RAIATHLESA GIKTKQLQVS HAFHSALMEP MLAEFEAVAN QITYHQPWIP LISNVTGKLV
DTGITSAEYW VNHVRQPVRF AQSMTTLDQE GYELFLEIGP KPILLGMGKQ CLPEEVGVWL
SSLRPGVEEW QQMLSSLGQL YVEGTKVDWL GFEQDYACQK VALPTYPFQR ERYWLETNNG
LPKKQYLSTS QNIHPLLGQK LNCASEQQIF QSVLGEGSPA YLSQHRVFDQ ALFPTTAYLE
MATAAGNYQL KTSHLVVEDF LIRQGCILPP GELVSAQTIL TPADNQGYQF QIFTQQEQKK
QEEQKWVLHA TGKIRSDQTE TTPTPVDLEK YQRECNHSIE ISQHYQQCRQ IGIDYGSSFQ
GIQKLWSGSN QALAEIKLPE ELLGETIDYQ FHPALLDAAL QVTFSALPQT DSDKTYLPVG
IEQFKVYRSP GLSLWAYASV MTPVEESQES LTTQVTLVSP SGEIIATVKG LQVKLATQQT
LLKTEVESIT NWLYGVEWRN KGRLGRLLPP DFLLAPVEVS QQLTPSLAEL VTQVDNARTA
EIGKSIEALS VDYIVQALSS MGWSYQPTES FDLQAAVQRL AIVPSQRRLF QRLLEILAEV
GILQSQQQRW QVQQTLEKVN PTQKSQSLLS QYPEEAATLT LLDRCASQLS GVLRGAIDPV
QLVFPKGDLT TAAELYKNST VAKVMNTIVQ QTITKAIDKL PPSRGVRLLE IGAGTGGTTN
YILPYLNPNQ TEYIFTDIGA LFTSKAQDKF RDYRFLGYQT LDIEVDPTSQ GLESHQYDVI
IAANVLHATT SLKQTLSHVR QLLAPGGMLV LYEATTRTRW VDLIFGLLEG WWKFSDYELR
PDYPLLSRQQ WKKVLSETGF TQVVTLPEVE GMAKALSEQT VIVAQAATTT LEQTKETSKG
WLILADTQGI AQHLASQLRS VGDVCTLVFA GESYQQLAPE EFTINPDNLS EFEQLIETLT
AKSPSLSGVV QCWTTEAGLG KTINSEELEN LSRLGCGTTL SLVKALVKAG LSQSPRLWLV
TNGAQPVPSN HPVIPGVAQS SVWGMGKVIS LEHPELNCTR IDLDPEETIE GQADALFNEI
WSEDSEDQVA WRGDGRYVAR LVGSRHRQPV TQQLVPSQPF KLGSSEKGSL DNLILEPVTR
RSPGAGEVEI RVKATGLNFL DVVSALGLVP EQVDGMSQKH LVEMDSFGAE CAGEVVAVGS
EVTGFHIGDT VMAMAHGSFS QYVTVDATYV VIKPENLSFE EAASIPANFL TAYYALHHVA
KIQAGDRILI HAGAGGTGMA AVQIAQQAGA EVLATASPPK WEALRNLGVK HIMNSRTLEF
ADQVMEITQG QGVDVVLNSL TSGEFISKGL SVVSSGGRFV EISKRGVWDS SQVAALRPDV
SYFVVDLVKE SIEQPGLINS MLQGLKDKLS NGLLQPPPIK VFPIEEVIDA FRYMQQAKHI
GKIVVSQTQL ADGTTQKPLS FRSGASYLIT GGMGGLGLLV ANWMVSKGAK HLVLLGRRSP
DDATRKKITE LEMAGAEVVV EKADVSDLES MTRVLHKIEQ SNIPLTGVIH SAGMLSDGVL
QNQSWSSFEQ VMDPKVQGAW HLHQLTKNKP LDFFVLFSSV ASLFGSPGQG NHSAANGFLD
GLAHYRRGMG LSGLSIHWGA VAQVGEAAER GADMRASKQG MGVISPTQVL ESLELLMSGE
DVEVGVVPLE WSAWQERLAQ WPFLADWQET IQTTSETSKS EFLLKLEATA PNERRSLLVA
HVRRQLALVL GINNPESIAL ATGFFDLGMD SLSSVELRNK LQNSLDYSLP SSLAFDYPTV
EKLVDYLVGK VVAKESYDTL VPKPTENKND QKQEKLLADT KELSEEQLEE LINQELNLII
NE
//
