ID G2E5C9_9GAMM Unreviewed; 4605 AA.
AC G2E5C9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:EGV28841.1};
DE EC=2.3.1.94 {ECO:0000313|EMBL:EGV28841.1};
DE EC=5.1.1.11 {ECO:0000313|EMBL:EGV28841.1};
GN ORFNames=ThidrDRAFT_3492 {ECO:0000313|EMBL:EGV28841.1};
OS Thiorhodococcus drewsii AZ1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodococcus.
OX NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV28841.1, ECO:0000313|Proteomes:UP000004200};
RN [1] {ECO:0000313|EMBL:EGV28841.1, ECO:0000313|Proteomes:UP000004200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ1 {ECO:0000313|EMBL:EGV28841.1,
RC ECO:0000313|Proteomes:UP000004200};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA Frigaard N.-U., Bryant D.A., Woyke T.J.;
RT "The draft genome of Thiorhodococcus drewsii AZ1.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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:EGV28841.1}.
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DR EMBL; AFWT01000030; EGV28841.1; -; Genomic_DNA.
DR RefSeq; WP_007042205.1; NZ_AFWT01000030.1.
DR STRING; 765913.ThidrDRAFT_3492; -.
DR PATRIC; fig|765913.3.peg.3562; -.
DR eggNOG; COG0001; Bacteria.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR OrthoDB; 9778690at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000004200; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0047879; F:erythronolide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0047462; F:phenylalanine racemase (ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
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; 4.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 4.
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; 4.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
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; 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; 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 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; PF00202; Aminotran_3; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF00668; Condensation; 4.
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; 4.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 4.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 4.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 8.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:EGV28841.1};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Isomerase {ECO:0000313|EMBL:EGV28841.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGV28841.1}.
FT DOMAIN 676..1093
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1554..1629
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2603..2678
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 4057..4132
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1533..1553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1626..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1676..1729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2585..2608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1683..1697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4605 AA; 496704 MW; 8C506E41581112B4 CRC64;
MLKPISFPDL RSAFLADGAS SGILTRIAGD GSETVLSPAG LREAADRIAR QLDHGGIGPG
AYVMLVMRDP LAYVTGLWGC IAAGCTAVPM PPLDNPTQQQ RTLAAAGVIG RCIVLTDEED
ARSSFEGTEA IDRAYRLIGE RFDRIAELDE TPSATSQVAP PIHPDDIAII QFSSGSTAAP
KGVELTHRAV LAQIDVLQRH LALTADDSFL SWMPLSHDFG LFHFHILPLL VDLPQVLMAP
DDFARRPISW LRAMDKHRTR LTGAPNFALQ MVASLLKPKS AAQLDLSALR SITNGAEPLN
PATIAVFLDA LAPSGLSRTA ITPAYGLAEA TLVTAIRTPG EPLAVIAVDR DHLTIGAEIV
EHEPDAPNTA HLCLLGRAAY GFAMRIVDES GTPLPSGTVG RLEVRGSSLM RGYINDPEHS
RAALHEDGWL DTGDIGFLWQ EELVLVGRHK DVIIVAGLNY HPADLERVAQ EAPGLSAANP
VAIVQARCPH SDEIRTLCFV RFRGTPEKAE RLQTAIADHV LAKSGLALDQ VVPVHQLPRT
TSGKLKRYEL GQHFEAGALG AETADRVRET QTEAAAFRQA IAGGHISEVT RLLCRLASHL
SGTPIEPESG LMDQGVSSQQ ALALTARIGT WLNRRVNIAV LFDHPTPRGF ARALIAQHAE
ISPAPAQVVS AQETTACSIA VIGLGCRFPG AENPEAFWDL LIGDRNPIRP IPEDRWPASA
WPEEAPCPPA ALLDDIDRFD GTLFGIARGE SEGMQPLQRL LLQVLWQALE HSGLDPAALR
GQRVGLFIGL SESGLGAGDR RLMDDAERLG AYSVTGHAGS VAVGRMAHLL DFRGPAIAID
TACSSSLVAL DMAAHSLRQG ACDLAIAGGA NLIISPELHA GLSRMGVLAP DGRCKTFAEE
ADGYGRGEGA GLLVLKRLAE ARRSQDQIWA EILGSAVNHD GQSQSVTAPN GTAQRDLLRR
ALREAGLDGK DVDWVETHGT GTPLGDPIEL AALHEVLRPE SQAPLPLGAV KSRIGHLEAA
AGIAGVIKAI LAMTHGRLPR NRPRKAPSSR YDWSTSPLTP LDQTLDWDDA KRRVAGISSF
GMSGTNVHVL IGQGQVSEAV APMPNRTPIL ALSAHTPEAL QQLHDRWSAL LSERPAEHWP
SLCAGQATRR WSGPYRMAVT RLDAGRGSSH PPVVKAKTVT RLLFCFTGQG AQFPSMGAEL
FAQEPLFRDA VIAASEAAGP IDGKDLLAWL YGPDAADAAR MNRTDLAQPA LVAVAHGLMR
LWADWGIQPD AVIGHSIGEI PAALAAGQLD LQTAMRLAVR RGQVMEHAAP EGAMLALRAD
EERALELLRG FDEVVISGYN APGSLTLAGS VEQIESLLAR AEEAGLAAQR LHVTRAFHSP
QMSQASAELA NGLSLPERAG VIPVYSTATG ALLGDSEMTQ PGYWSSQMLS PVRFRQAVAT
AAESGDLICI EIGPRAVLAK LGPACAPDAT WIGGGDRLED LAHAVGQAWT HGAPLDWLRY
FGSRGAPGQD LPRLPLNETP IPRRTWSGAV VAPNAPSVPR TTTAASDAPP PSGHALDAIV
LPLTSRVSGI ETDRIDPDRP MVALGLDSLG LVQIQRSLAK SCGLQIELKA LFQTLDTPRK
LADHIDAQRP QPAPPPTATA APDSAHPSPE VVALMQEQLR TLQQVMERQL TLLGAPASAP
SESAGPAKTS PVQTLVQTPA RPHARKPNTG EIKGLFRQPS RSGVGLDPGQ RTHVARLTRS
WNTKSAGSKA GAERARKRVA NSRAVFGFAP EYKELTYPLM ASRAQGSQVW DLDGNAYVDV
TMGFGVYLFG HNPDFVAHAL REELDRGAPL GPTSPLAAEV AERIHQLTGV DRCAFFATGT
EAIMCAVRIA RALTRRDRIV VFKGDYHGSF DGVLATGWID EDGSPQSAPL TDGTPQGMVD
PVIVLDYGDM SGLDLIRRHA SEIALVLVEP VQSRNPENRP IEFLQALRAL TQERDIPLLF
DEIISGFRFA PGGMQSMLGI KADLVTYGKV LGCGQPIGVL AGDARLMDAI DGGDWAYGDD
SGPGTRTAFV AGTFNAHPLG LAAARAVLDR LIADGGALQQ DLARRTENLC ATLDALFETA
AMPVRMERFG SLFRFAFGPG MEILNSHLLN GGIFVWEQRN CFLSTAHSDD DIAKIVEATR
RGIAALQAAG WLGQSQRQDQ TESARPSRLQ PAISETTMRR HAGTAHPGTW TDLVILRLSV
DRLDPDRLTT AWSALCRRHA ALRACLAADG TRCVADGMAP ALERTQLPEK PEFRIGLDRW
AQSALAKPFR LDRAPIEPVL LETAAGEQAL AVRSSHLGFD GWSVALLLRE LFQLIDDTPL
PEADRWNAYL GWEAQAEFTR ASMQARPMHL PCDVEPASMT AAGGRITRTD IGTLFARVSE
TARSGGQTPL VGMLAAFALL IRGLTGEERV TIGLPVAGQA LSGLTGLVGN VSFIRPVTLD
IADAMTLAEL RRTLHHRLLE PGAHPPADAM PERHVLFNID GPIRFGGASR QVALHSVPIV
GARADLFANI LLLDDQVILD FDWNSDRFSE DSAQSWLATF LEIAERSCAD RAAVAQILAD
RAWPAPPATP VQRKAPRAEK PAHPSTATEQ TLADLWREIL DTGTDLGSSD FFDLGGGSLH
AVRLLARIRE TFGVELSLAQ IFGAPLLEDM ARQIETAATA DGGIDPVRPI PAQVPATRQQ
QQLCLLEQMS EAGPAYNLCL RLDFDYPLDA QTLGGALRRV GARHTSLRTR LCMDGESIVQ
SIASEPDISL RTLDASTAEW IAPFVQEPFD LAESPLWRAG LAFPGDGCTL VLVVHHLIAD
AWSMEILARD LLGAYQQILA GQDPGLMPLA IDYSDYALAR ALGTEHRERD LEHWRTSLRH
APRLTALAGD APRPPTKSFA GQQTRLTLAP ALQQRMRGLA KRLRTSVYQL VVAAIAQLVA
RRNGSGNLVF GCVVAGRDLP GLDRPIGFFA NTLPLHLVLH EDWRAVDLIA AVRSALMDAT
EHSGCSLQDI CTALQLTPDP AANPLFEICV THDDRSGLSQ LGAELGFAFA EPPLPTSQFD
LSFYVVETGD GVSLDLTYAT AIFQPHTITG ILDEIERMLQ ALCHDPEAPI ASWSRTDQLR
EPSALQKRLW FVDQFENGQL YATAPTYYNM AATFALDANA DPALLQQRFE QLLADTPDFR
ATFRTLDGNP RISAASIQVP SCTAICGDEI DAQVRRFILT PFDLQTGPLL RMAVVEHAPA
RRALLLVGHH IIVDEASLAG IADWLRVGTE IPKQAAPGQS PVPDASVLQL ERDFWQRYLG
PNPPRLLLPV DRPRAAVHVF GSGLSQVSLT AAEFAAIERL AADSHVVLDD LILTGFVGLL
SRLSGQEEIV LGQTVPRRSG YPRGQANLVT LRIDLTRLSD TTEAIAEVAR HSTETLAHAQ
TDFDQVVLDL KPDNDMSRTA LFDVLYVRSA EPVAGRGMAP AIGWGKYDLT LAANHAGDGR
LDLMLVFNSE MFDAETVDHW GRLLCRLLAA LCAHGDRHFL SLPLATGTEI DQLIADGGPR
RTQATWPYAN LPDAVSDRAR RMPDMIAVSD ATGTLTYADL ELQARALAQA LIARGVLRGD
RVALMLPRDR DTVVAMLAVL CAGAAFVPMD LSAAPERTAR ILQDAGAVSV IVKGAMGRDL
LPLDLPRVDM TRLAEDRSGA EPEWPEVRAT DGAYVIFTSG SSGRPKGVMV EHRNVLALML
GQEDLFPVAP GDRWSWFHSP AFDFSIWEIW GALLTGGRIV VIPEAARDDF ALLRAQLKQQ
EVTVLSLTPS AFNVLSDQEM NEAQADLAVR SLWLGGEALT PTLLRAWSDR YPDCALINLF
GITETTVHTT FRRLAKTDLD RTDSLIGRPL PSYGVTIRDA ELRPVPATVQ GEILVSGSGV
ARGYLGHPEL TAARFVEDPY RPGSRLYRSG DLGRYDLAGE LTYLGRADSQ VKVRGFRIEL
GEIETALSGF PGMRKTVVGT RQSAGEETAL AAWIIADAEP DADRLNAYLA KVLPAYMIPK
HLYRVDHIPL TLNGKADLRA LAGMCERQIG AASEDDAPSP GLETEIAVIL CELLGRTEMS
RSASFFALGG HSLMANQAVL RLRKRLGLQL TLRDFFTAQT IAALAVLGQD GRNTATTGIA
RIPDADSYPL SSAQRRLFAI QTAHPDSASY NMVGGFIVSG ALDPDALAAA FADLVDRHEI
LRTRFLILDG EARQRIDPPG RTVALDLIRN ADAADEQAII DRALDAEFAH AFTLSQGPLF
RVRLTALGPE RWLMVLNLHH IISDGWSVPI MIADLSRCYA ARAAGSGPPQ LKPLAIQYRD
FASWQQTACA NPEAEAALAH WRARLASDAP LQTTLPTDSA RTKTRAGRGA MALRRLDEER
SRALRTAAAQ SGLTLFSVFA ATLHIVLELR GESGGATVIG TADAGRDALE TEDQLGFYLN
LLPHVLSGSA DLSIERWVEL SRAETVAMLA HKTYPFDRML EELAIDTLPG HSPVFDILLL
VQTNADPQTR LGDLELRMLP DQTRTARYDL SLMVEDRPAI ELLIEYDTDL FRAQTIDWVF
ADLLSLLDAF VDSPSLSPLA ILGQTEPAMD PSLGLLDLAD PLMEV
//
