ID U5DJ17_9CHRO Unreviewed; 1665 AA.
AC U5DJ17;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=NADPH:quinone reductase {ECO:0000313|EMBL:ERN41671.1};
DE Flags: Fragment;
GN ORFNames=KR51_00017190 {ECO:0000313|EMBL:ERN41671.1};
OS Rubidibacter lacunae KORDI 51-2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Rubidibacter.
OX NCBI_TaxID=582515 {ECO:0000313|EMBL:ERN41671.1, ECO:0000313|Proteomes:UP000016960};
RN [1] {ECO:0000313|EMBL:ERN41671.1, ECO:0000313|Proteomes:UP000016960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI 51-2 {ECO:0000313|EMBL:ERN41671.1,
RC ECO:0000313|Proteomes:UP000016960};
RA Choi D.H., Noh J.H., Kwon K.-K., Lee J.-H., Ryu J.-Y.;
RT "Draft genome sequence of Rubidibacter lacunae KORDI 51-2.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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:ERN41671.1}.
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DR EMBL; ASSJ01000045; ERN41671.1; -; Genomic_DNA.
DR STRING; 582515.KR51_00017190; -.
DR PATRIC; fig|582515.4.peg.1952; -.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR InParanoid; U5DJ17; -.
DR OrthoDB; 499075at2; -.
DR Proteomes; UP000016960; 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 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; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_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; PF00107; ADH_zinc_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 Reference proteome {ECO:0000313|Proteomes:UP000016960};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1568..1650
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ERN41671.1"
SQ SEQUENCE 1665 AA; 183796 MW; 8564CBD29E3547F3 CRC64;
PNIALPAYPW QREHHWQETR ESNDRRLLPC VHPLLGVRLD RFEPCWTNTI DLRRHAFLND
HRFKGLIIFP AAGYVELALA AGRELHGAGN LQLENMEIDQ PLILKQGQRR QIQVQALAND
GTISINSRVA GEEDGCLPHM RGRIRKMSVP GRRRFNLDEL KQQCPENITE LLYPAFEKAG
HDYRGAFSGI DGIWRGGDEV FSILRPLNSL VPGLNSHDLE AYLLHPALLD LGFQALFGTF
LSHQQTQFKA RLPIALERLR LYGVPRPDAE HVVYARRLTP VEDDFALGDI YIIDKDGNTL
VEIGNLAGKP PSAKSEQSDW LYAFEWDRQE IVHGIDESWA GRVAPGTLSA IVQPDIPSLA
ERFNLDQYYG EVRSFGEAMT VAFVWEAFVE LGGCWSEGRE LTVKGVCTDL KIASQHERLT
RRLLQCLESW DLLAKTGSDT WQVLSVYTGP EAAAIIETYL SKYKEKHPEF NLLEQCGQQL
ARVLRGDVDP VRVLFPNGSQ ELMEPVYDRS SMFRPYNKIV EFVVRAMCSG MPENRPLRIL
EIGAGTGALA SLLLANLPVG RIQYTFTDIS PAFFVRAKEK FSGFGNVDYQ VLDIERSPIQ
QGFNPESFDL VIAGDVLHAT KDLKQAIAHA NELLVSNGML LLLEMTSPSF YVDVTLGMLK
GWWAFEDTGL RADHCCLDRD SWKKLLGECG LQDVNILTDR SDGTGIQSVI SSRKPGGSVR
AGDRDRDGVW FLFVDRHGTG DRVKEEFDKN GYITLPVTLA GPDEPPRPVP SSSQVIAAGD
LAEMRALFHE AAGRYGTIAG VVYLRPLDAV PLDEAGRETL DASCTGECLN VVNILRAFDD
LDLDGGLRLV LVTRDAQQIK DDDIVTGVLS SPLWGLGRVA ENEYPDCHIT LIDLPGAAEA
IDTARIYEEA TQRTSRELEV ALRGGERHVA RLRRTSRERL ARAQSRPRPV KQDEKFYLDL
HKPGDLSGFV LKPAARPQPG PGEVEIEVHH AGLNFRDLMK AMDIYPDDGG THFYLGDECS
GIVLSVGPGV EDFVPGDRVA AIARGFGSVV ITPADCVVRI PEHLSLADAA TIPLVFCTVW
HALHELAGIQ RGERLLIHAA AGGVGLAAVQ IAQNAGAEIF ATAGSDEKRA YLSSLGVKHV
LNSRSLDFHD EIQKATDGEG VDIVLNSLSG EFIQESLKLL RSYGRFVEIG KTDIYQKQAL
NLYPFRNNLS FFAMDLEKLI RQHPKRIRRY LHEVMQVFDD KTLTPLPVTA FDINDAEKAF
RHMAQAKHIG KIVFDMHGGS PGRAVSEAPN FKGFHKDASY LLTGGLGGFG LAVAQWMAAE
GAGHLILAGR RAVLKDPQRE KIEAIEESGC KVSVVSLDVV DGDKIQQVLN ELCTEKAPLK
GVIHMVMVLD DRAIGNQNAG SFSRVLDPKV KGAWNLHRVT STKDLDFFVL FSSIAAVVGN
PGQSNYAAAN QFLDTLAYHR RARGLPALTI AWGPISDVGY LTEREDIQQR FDRRGLHAIG
TAEAIKILHG CLQDELSSAG VLFVDWLKYS SHFPRLLSSS RFRHLVVSSA NVMPIADSGG
RLLADLKGAS SSKRQELVHK WLAEQLARIL DCELEKIDAS RSLNDIGVDS LMAVELSALI
EKSLGISIPS MELAQTTTIG RLAARLAEEA TGNIDEARPA ATSAA
//