ID F4XWJ9_9CYAN Unreviewed; 1704 AA.
AC F4XWJ9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=NADPH:quinone reductase/Zn-dependent oxidoreductase {ECO:0000313|EMBL:EGJ31035.1};
DE Flags: Fragment;
GN ORFNames=LYNGBM3L_44020 {ECO:0000313|EMBL:EGJ31035.1};
OS Moorena producens 3L.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Moorena.
OX NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ31035.1, ECO:0000313|Proteomes:UP000003959};
RN [1] {ECO:0000313|Proteomes:UP000003959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3L {ECO:0000313|Proteomes:UP000003959};
RX PubMed=21555588; DOI=10.1073/pnas.1101137108;
RA Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., Esquenazi E.,
RA Niessen S., Hoover H., Rothmann M., Lasken R.S., Yates J.R.III.,
RA Reinhardt R., Kube M., Burkart M.D., Allen E.E., Dorrestein P.C.,
RA Gerwick W.H., Gerwick L.;
RT "Genomic insights into the physiology and ecology of the marine filamentous
RT cyanobacterium Lyngbya majuscula.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:8815-8820(2011).
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DR EMBL; GL890943; EGJ31035.1; -; Genomic_DNA.
DR eggNOG; COG0300; Bacteria.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG2518; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_002925_0_0_3; -.
DR OrthoDB; 499075at2; -.
DR Proteomes; UP000003959; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR049490; C883_1060-like_KR_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF21394; Beta-ketacyl_N; 1.
DR Pfam; PF18558; HTH_51; 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; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1587..1665
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGJ31035.1"
SQ SEQUENCE 1704 AA; 187977 MW; 850DD5E35FA0AD7A CRC64;
VKGAKIDWSG FDSDYSRQKV ALPTYPFQRE RYWIETNNNF WPKQQFSKGE NLHPLLGQKL
NCAGEQQIFA SQIGEKSPNY LSNHRVFNQA LFPTTGYLEI AIAAGNHQLK TPQIVIEDLT
ISRGWILPAG ELTNAQTILT PTDSQSYKFQ IFSQLEEEEW KLHTTGKIRK ESTPPPQTKI
DLEKYKSECN QAIEVKQHYQ KCQQVGIDYG NSFQGIQQLW SGSNQALAYI KLPEELITQT
RDYNFHPALL DAALQVIFQA LPATDSDQTY LPVGIEEFKL YKNPGLSLWA YASVTSPEVK
TPESLTTLVT IVTPSGEIIA NLKGLQLKLA TKQTLLGTET ESIENWLYEV EWRSQGILGK
LLPPDFLRPP VEIAQKLAPT LTELVTQVDQ KRTGSIETSL EELTVDYIVQ ALHEMGWSYK
PTESFEFDAA VKKLGIVPSQ RQLFKRLLQI LTEVGILNYN QQQWQVEQTL AQVKPTEKSQ
SLQNQYPEEA ATLTLLERCA SQLSGVLRGA IDPVQLVFPQ GDLTTATQLY EESTVAKVMN
TIVEKSITKA IEKLPKSRGI RLLEIGAGTG GTTSYILPHL NPQQTEYIFT DIGALFTAKA
QDKFQDYQFI SYQTLDIEVD PKSQGFEANQ YDIIIAANVL HATTIMKQTL SHVRELLADG
GMLVLLEVTT AQRWLDLVFG LLEGWWKFND YELRPDYPLL SRDQWQKVLR ETDFTEVVTM
PEVEGMAETL SGQTVIVAQS SQTKLEQTND GSKSWLILAD KEGIGKQLAR QLNSVGEVCT
LVFAGEKYQQ IAPAEFTINP NNLEDFEEVI ETVAGKSPSL YGVVQCWTTE AGVGQTVNSE
ELGSLSKLGC GTTLSLVQAL VKAGLSIVPR LWLVTSGAQA VSSNHPVIPG VAQSSVWGMG
KVISLEHPEL NCTRIDLDPE ETIEGQADAL FNEIWSEDSE DQVAWRGDGR YVARLVASHH
RQPVAQHLVP SQPFKLGSSE KGSLDNLVLE PVTRRSPGAG EVEIRVKATG LNFLDVVSAL
GLVPQQVDGM SQKHLVEMDS FGGECAGEVV AVGSKVTGFH IGDTVMAMAH GSFSQYVTVD
ATYVVIKPEN LSFEEAASIP ANFLTAYYAL HHVAKIQAGD RILIHAAAGG TGMAAVQIAM
EAGAEVLATA SPPKWEALRD MGVKHIMNSR TYEFADQVME ITQGQGVDIV LNSLTSGEFI
SKSMSVVTQS GRFVEIAKRG VWDSSQVAAL RPDVSYFVVD LVKESIEQPG LINSMLQGLK
DKLSNGLLQP PPIKVFPIEE VIDAFRYMQQ AKHIGKIVVT QTQLADARTQ KPLSFRSGAS
YLITGGMGGL GLLVANWMVS KGAKHLVLLG RRSPDDATRK KITELEMAGA EVVVEKADVS
DRKSITEVWK RIEESNRPLA GVIHSAGMLS DGVLQNQSWS SFEQVMAPKV QGAWHLHQLT
QNQPLDFFVL FSSAASLLGS PGQGNHSAAN AFLDGLAHYR RAQGLPGLSI HWGAVSQVGE
AAERGADMRV SKQGMGAISP AQVLESLELL ISGSDVEVGV VPIEWSGWQE RVAQWPFLAD
WQETILEVAE PSKSDFLLKL EATPASERRW LLVAHVRRQV ANVLGISHPE SIALETGFFD
LGMDSLTSVE LRNKLQSSLK RSLPSTIALD YPKIQDIVNY LAKDLLILEE NKENDSDNIV
NLNFQQNLQI DRIAKKLAEK LGAN
//
