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Database: UniProt
Entry: D2PWV7_KRIFD
LinkDB: D2PWV7_KRIFD
Original site: D2PWV7_KRIFD 
ID   D2PWV7_KRIFD            Unreviewed;      3497 AA.
AC   D2PWV7;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:ADB35337.1};
GN   OrderedLocusNames=Kfla_6335 {ECO:0000313|EMBL:ADB35337.1};
OS   Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Kribbellaceae; Kribbella.
OX   NCBI_TaxID=479435 {ECO:0000313|EMBL:ADB35337.1, ECO:0000313|Proteomes:UP000007967};
RN   [1] {ECO:0000313|Proteomes:UP000007967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC   {ECO:0000313|Proteomes:UP000007967};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Pukall R., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Kribbella flavida DSM 17836.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADB35337.1, ECO:0000313|Proteomes:UP000007967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC   {ECO:0000313|Proteomes:UP000007967};
RX   PubMed=21304701;
RA   Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA   Cheng J.-F., Lucas S., Chen F., Nolan M., LaButti K., Pati A., Ivanova N.,
RA   Mavrommatis K., Mikhailova N., Pitluck S., Bruce D., Goodwin L., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C.D., Chen A., Palaniappan K., Chain P.,
RA   Rohde M., Goeker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.-P., Brettin T.;
RT   "Complete genome sequence of Kribbella flavida type strain (IFO 14399).";
RL   Stand. Genomic Sci. 2:186-193(2010).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC       family. {ECO:0000256|ARBA:ARBA00029443}.
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DR   EMBL; CP001736; ADB35337.1; -; Genomic_DNA.
DR   RefSeq; WP_012923890.1; NC_013729.1.
DR   STRING; 479435.Kfla_6335; -.
DR   KEGG; kfl:Kfla_6335; -.
DR   eggNOG; COG0318; Bacteria.
DR   eggNOG; COG1020; Bacteria.
DR   eggNOG; COG2141; Bacteria.
DR   eggNOG; COG3321; Bacteria.
DR   HOGENOM; CLU_000274_0_0_11; -.
DR   OrthoDB; 9808669at2; -.
DR   Proteomes; UP000007967; Chromosome.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd19531; LCL_NRPS-like; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 3.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   Gene3D; 3.20.20.30; Luciferase-like domain; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR   InterPro; IPR010071; AA_adenyl_domain.
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; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR024011; Biosynth_lucif-like_mOase_dom.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR04020; seco_metab_LLM; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   Pfam; PF00668; Condensation; 2.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 3.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 3.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 3.
DR   SUPFAM; SSF51679; Bacterial luciferase-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 3.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE   3: Inferred from homology;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007967};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          574..649
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          672..1086
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1555..1630
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          3016..3091
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          553..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1495..1533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1693..1733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2288..2309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1513..1528
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1693..1713
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3497 AA;  373170 MW;  DF3522DE25129056 CRC64;
     MANSSLTRGS QLILTGADPA DAVQALTRAA TEFPAAGVRT PAGLLTYADL LDRARRILTG
     LRATGLSSGD PVIVQGLSLD DFFPAFWACL LGGIQPAVIS EQVSPGSPVL DRLRHTWALL
     DTPPVLTDRT GAVVLADRGF QPAVVDELQQ SLPADELHRP DPAEVALLML SSGSTGAPKA
     AALTHRGLAE FAAGSRRVLD VRPGETMLNW LPVDHSGALL LYHVLPVFTG STNVHLPTAD
     VLANPSLWLE KAAQYGVAHA WSPTFGLQLA ADAFAARQDL ELDLSCVRSV VSGGEQIVLP
     VVDRFFAATA RAGLGRERFR PAWGMAETAT AITIGALTSQ GGVLRVLKSS LAGDLVLAEP
     SVPDADCTTF VAVGPPAPGA TVRVVDDNDE VLPELRIGRL QVRSARITAG YLNNPSATAA
     ALPDGEWLRT GDLAFVADGQ VVITGREGDS VVLNGHTVFC HEIEEVVGGV DGLSLRGVGV
     CGVPNPGTGT EDLVVFVDDA GTPGEVEPAI RAALFRRLRL TAAEIVRVPA GEFPRTASGK
     VRRTELRARY QAGRYSRDSA ASQGGRSAGE DRMAPSVGEV GAVVRRLVAE LAGQPVAVDA
     PFYEVGLSSI KLARLRAGLT EQLGIDVPAT TPFEHPTVDA LTHWLTEQLA ASGPAQVEPD
     GRADEAGRRV VDRRVAVVGM AARFPGARTV EEFWANLWGG VDSVSTFAAA GGPDHVPVGG
     VLEDAETFDA EFFGMSPKEA ALTDAAHRQF LEVAHEVLEN GGYPSAEPGV RIGVYAGTGM
     NLYGHQDQPA GAAAADIPTA MQATIGATAD FLATRVAYRL GLTGPAIGVQ TACSTSLVAV
     HLAVQALLDD DADLAVAGAA AVRLPQDAGY RHVPGSILSP TGRCRPFDAA ADGTVGGNGV
     AAVLLKRLDR ALADGDTVHA VILGSAVNND GTSKVGFTAP SVSGQVDVVR RALERAGVGA
     DTISYVEAHG TGTALGDPVE FEALSRVFGA GQRTAKCGLG SVKANVGHLD SCAGLAGLIK
     TILMLQHGRL VPTLNLTQPH PDLRVERSPF ELITASGPWR TDGVPRRAGV SALGVGGTNA
     HIVLEQPPLE SGRDETPVPQ ATDGQTNGFH PVVVPVSAQS VEALGELSAS LRAYLAARPE
     VAVADVATTM GVGRRHHACR RAVVGAEVGE VVAALGEDPG EVVTGPLTFA YSGQGSAYSG
     MSEWMYRTFR PAREVFDEIE RVLGVPVLEG EGELGQVALF AHQAAWTEVW RGLGVVPDFV
     VGHSLGEYAA LHAAGVLSLT DGALLTARRG ELMQAGMEPG VMVAVGAELA EAEQIAAECG
     VEVAAVNGRD RVVLSGAEDA MARAVGVLDG RGVSWRRMGV ERAFHSVMVE PVLGELRAFA
     EKVAFRPPRV PVFRGTDGAV LSGVDGRYLV EHARRAVRFD LLMRAVRERG GNRFLDVGPD
     AVLSGLGRRA LPGSAWVASQ RKGAEDQFAQ TLAALYRAGA DINWSMVSTG RRIPLPGHPL
     ARRRYDRPST PTVPPQTAVP PQPTVPARTP EPMRATEPMQ GVEQMQVQSV GAERAAVLQQ
     VRQLVAPSLG MEPDAVPAEA TFLSLGADSL SLMRLVGDLD EVFGVKIPVR RLFDDADTPN
     RLVDLLSPSA AVVPQPLQQE SQPVQLQEAP AAQAVDDGGR RELVDRQLRL AERMVDRVTD
     LMSEQLAFLN GASPTTQQAS TPMVDSSTAP PATVTHPEAP PQPTPARRNS PHRRTGCDFS
     LYFFGDYPDH AAQDKYGLIL KATEYADAHG FHAVWLPERH FHSFGALFPN PSVLAAALAT
     RTQRIRLHAG SVVLPLHHPI RVAEEWSVVD NLSGGRAGMC VASGWHARDF VFAPDSYGRH
     REELYEHLDT VRRLWAGEAI TATAGNGEST EVRLHPRPLQ DQPPLYAAVV GNPESYKLAA
     RNDIGVVTNL MAQSVEDLAA NIALYRSTRA EHGLDPDAGR VVVLLHTYVG DDLEAVRAAA
     YRPFCDYLRS SLSLFGQVTN SLGFQIDLDK TPADDVDFLL GQAYQRYCES RALIGTPDSC
     ATIVDALLAA GADEIACFVD FGVAPEQVMQ SLTAVDALRA EYDGAAPPRH EGRELTPPER
     RIWFLEQLNP GTNRYHEPKA IELRGPLDPV ALRGALQKVA DRHPALRTTF REIDGEPRAF
     VGATAPIDCP MVDAEGKDLS SVLRDVRLGE LDPATGPLVR AQLVRFSERH HVLLLVAHHI
     VFDSASTPVL ARDLGAYYRS WPDDPDLPAA TDGLHLPAGG DQEPAALEAR KKGDLDFWVE
     HLSGAPELQL PADRPRPPRR SGAGSSLTHD LDRRLTEQLT AFAGRTGVTV FSTLLAGLSV
     VLSRFSGQRD FVLGTGVSGR GKHAGDAIGM FVDTLPLRVR IPATAAFADV TRDLGLALMD
     AVDHRDLPFE DIVAALNPER SAGRNPLFGV AVEFESGSEQ ISFAPPTVSA TLLDLPSERA
     PLDLVLYLTY RPDGVQCVVE YDTDLYDEST IQRLLDYLGT TLDLATASTP VAVPDLAVLT
     EQDSRLLAQL EGRPAEESTL CLHELFERQV DQHPEALALT GAYGDTTYAE LDRQANRIAA
     ELLTRGVRRG ELVALCLPRG PQQIAALLGV LKSGYAYLPL DPTVPVERLR LVVDDADAAL
     VVTAEGMPDL GDRPRLRIDD LDAGPVDRPR TDVTPDDLAY CIYTSGSTGT PKGVLVPHRG
     TVNHVLQYVA AHPPTRLLQW ATPTFDGSVH EVFTTLAAGQ TLVLIDDASR YDVEALAATI
     DRYQVQRIVM PYSAVHSLLA TKPSLPSLRE ILTAGETVRL TAADLEFLAA HPNCVLYNGY
     GPTEASIGVT EHRVEPGEIA PPVGRPIPGV RLRLLDAERR PVPMGAVGEI CVEGVCVTDG
     YLNRSAETAA AFFAPNSYAT GDLGRWRADG GLEFHGRRDE QVKIRGARIE PGEVRAAVLD
     HPLVTDAAVL AVDGELVGYV VGTVGGDELT DHLSAQLPQY LVPRRWVRLD RLPLASTGKL
     DRAALPAPEN ARGSATPSTA MEHTLHEVWC KVLGVTAVGV DDSFFALGGH SLLAVRLLNL
     VRETAGVELT LTEFFRAPTL RAVAAKAQGD VVVETAPLTF AQRRVLGRHR SRRDASVYNG
     ITRVDVTGDL NPATLQAALR TLANRHTALR TRIAADRQEV FAAVPITLPV HELPDDESQI
     QAWCVAAAQP AMDPAQAPLW RVCLGRVSAE HWVLVVVVHH LIYDGWSARL FWQELSALYT
     GAELAPPTAQ LTDYARWERD TLTGETRTQL EAFWRNELAG ASLRPNLPVD HPRPDVLSGD
     GATHHVDLPH ELAARLRARA AEAGTTPYVV IAAAFARWLG DLCGEDQVIL PASSARRSRP
     EHDGIIGYLG EAVLVRVRLD APDLLGETAG ALYAALDHEA LPLAEVVRTA LPDQADLPYP
     AVLFTVITTP GATLTLPSGE FRTRGFSVPG QARTELYVVF TVTEEAFTLD IEYSTDLFTS
     TTIAEWAMSL VTALTGP
//
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