ID U3GDT3_9RALS Unreviewed; 2556 AA.
AC U3GDT3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGY64254.1};
GN ORFNames=HMPREF0989_02274 {ECO:0000313|EMBL:EGY64254.1};
OS Ralstonia sp. 5_2_56FAA.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=658080 {ECO:0000313|EMBL:EGY64254.1, ECO:0000313|Proteomes:UP000016506};
RN [1] {ECO:0000313|EMBL:EGY64254.1, ECO:0000313|Proteomes:UP000016506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5_2_56FAA {ECO:0000313|EMBL:EGY64254.1,
RC ECO:0000313|Proteomes:UP000016506};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Daigneault M.,
RA Ambrose C.E., Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Ralstonia sp. 5_2_56FAA.";
RL Submitted (MAY-2012) 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:EGY64254.1}.
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DR EMBL; ACTT02000012; EGY64254.1; -; Genomic_DNA.
DR RefSeq; WP_009240835.1; NZ_JH815238.1.
DR GeneID; 61389997; -.
DR PATRIC; fig|658080.3.peg.2306; -.
DR HOGENOM; CLU_000022_31_5_4; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000016506; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 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; 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; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
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; 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; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
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; PF13602; ADH_zinc_N_2; 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; 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; 1.
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; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
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; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000016506};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..428
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2421..2498
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2556 AA; 271938 MW; 6BE18EFAADCE1F76 CRC64;
MKDAIAIVGM SCRFPGGVHS PEDYWKLLVA ETDAVTEVPA DRFSTEFYQH PSKREPGKSY
TFAAGVIDNV AGFDADFFGI SPREAQQMDP QQRLLLELAW EAFEHAGHHP QQMAGQDCAV
FVGVAAQDYG DRGVDDLSVV DAYSATGNTL SIASNRISYL FDLRGPSMSI DTACSSSLVA
LHQACNAIRA GEVETALAGG VNLLLHPFPF VSFAKASMLS PTGRCRAFDA SGDGYVRAEG
GALVLLKSLS KALADGDTIH AVIASSGVNS DGHSQGGINV PASATQAALL ENVYARAGVD
PREVDYLEAH GTGTAVGDPI ETRALIDVIG KLRSPDAPLL IGSAKTNVGH LETASGMAGL
IKAILCLKHR AVPASIHFRT PNPNIDFTGG NLRVVDRYTP LAAKDKRLLV GVNSFGFGGT
NAHVLLREAA PPSKAAKAGK ATSVAQNRPA PLMLSARSQE ALQALAAAYR DQLGAGTSWQ
ALAGATAHRR QPLRYRAVID PSNAADVAAD GIAALAALAQ GDTCPAVVTG EAVANDGKLA
LVFSGNGSQW AGMGQRLLQE DSVFCATVKQ IDAFWCADGS ASLLDVMRAG ATAEWLQRTE
NAQPLLFAIQ AGIVQSLLEQ GLRFDACYGH SVGEVAAAYA AGALSMEQAV RVIKVRSRAQ
ALTAGKGRMA AAGVGEGAAR ELIAALGLDD VLEVAGINSP GAVTLAGPLT ALEAVQAHLA
QANQFFQMLD LDYAFHSRQM DAIHDVVLEG LRGLQPRATH STFVSTVTGT PLSGAELDAS
YWWRNIREPV QFEPATRQLI DGGMRLFLEI GPHSILRAYV SQSLEAARAN GSALPTLKRN
HDQSSQLRHA FCTALAHGAR LDRNTVYPDA HRDVVLPTYP WQRTPYWAPI TAEGYDLVHR
HRQHPLLGYR LKDCAAAWEN QIDPVKLPML ASHVVDGAVT FPGAGYAEMA LAAARSYFGT
VTCAVENLEI RTPVVFQPQQ GRLFRFTLDP RTAGFVIETR PRVSDDPWTI NVAGRLLIGG
PSQTAPAIEP QSMAALEEQA PIAGSTLYQA ALAIGLEFGE AFRWVQTVRI DGNVALAELA
APASQQAHLD RYTMHPGALD SGLHPLLALM AAGKPGAEQA AYVPVQFGRM DYFGGVPARV
VARIERRSPH SLVANFQYLD AGGNTVLKLS ACRFRRVDLI RRRHGKPGRY VFALEAKPAT
EAIAAAATPS PASLLATAAT MVAGTEDAAH RDRHLTEVMP LIDVLAAAYA LRAVEALHVR
AKAELPACAN PALLARLVDM LLEDGILVRR DGVLALGDET LPPIEELWRS LLSLSPSHVA
ELTLLAHCGA SLPAILNGEL EAGAVLPPAR NSLLDHLFEA SPTWSHVNAM ASASLDACIE
RWTLRRPMRV LEIVPPEANL FEPIGAHLQG RCEYTIAGSP EQLGAFDTGR HPLIRTATIQ
LSDQPELTVE PGRSHTFDVV VVNNLLRTSG KPNRLLAAVR TWMTPGALLV LSEAQPSRFS
DIVFGLSPEW WSAGRGDLLP AESIEAMLLA EGFQSPARHV EADLQIEGAP ALLLARRQLG
RQADSCDIGE IVTEGIDGNA EQLGANWLVV CPGTPAELAT TLAAALEEAL AGASLASRSP
RVALVESPEA ALEHAALDEA GAPCQIVFLA ADAPRLDDSA DAGTLMQAQE PTSVALARLV
RGLNGKRASA QLSIVTCGGA PLAAPGTPAT ALQPSQATLW GLGRVLMNEH AELHCRLIDI
DPRETQPVPA LSRELLCADA EDEVVLGLEE RYVPRMLTAE VSELREQATR AAAGASAIPA
VLGFESPGSL RHLQWFPLPE FELEPDEVEV EPMAAGLNFR DVMYAMGLLS DEAVENGFAG
PTIGMEFSGR VTRVGSAVAN FASGDLVLGF APACYASRLR TRATALAHKP ARLSFEEAAT
IPTTFFTAYY GLNELARIRK GERVLVHGAA GGVGIAAIQL ARHLGAEVFA TASSNEKREF
VRLLGASRVF DSRSLAFADE IRRATGGEGV DVVLNSLAGE AMVRSIDVLR PFGRFLELGK
RDFYENSRIG LRPFRNNISY FGIDADQLMD ASPQLTASLF AQVMALLDQG VLDPLPYRAF
PAARIEEAFR YMQQARQIGK IVVTFAGGVP APQAASASHL ALDPSAAYLV AGGTGGLGFA
TARWLVERGA RHLVLASRRG TLAPELAEEA AHWRDTLQVD TAVVSCDLNN GAAVRALVDG
LGRSGTPLKG LVHSAMTIAD GLIANLDDAK MRDVLAPKVA GAWNLHQATR ELALDFFVVY
SSATTFLGNP GQSNYVAANA FLEALIHQRR AQGLPGTYMA WGPLEDVGFL ARNAQTLEAL
QARIGGRAIT SAQAMTALEQ VLQCGHAGEA LLWLDWKSIS RVMPAARSLR YLDMRGGIGQ
ETQRADGASM KAEIRALDSA EAVQLVIETL QAQIARILHL SAAKVDPDRS VTDLGMDSLM
GMELGMAIEE CFEVKLPVMM LAEGATVRSL AQKIAESVRA GATDGQEAGA ASDVEQQLAS
LSAIHGSEIS SDELQRMARE MTANRAVADV LTETTS
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