ID H0TSD4_9BRAD Unreviewed; 2698 AA.
AC H0TSD4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:CCE09372.1};
GN ORFNames=BRAS3843_3160060 {ECO:0000313|EMBL:CCE09372.1};
OS Bradyrhizobium sp. STM 3843.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE09372.1, ECO:0000313|Proteomes:UP000002686};
RN [1] {ECO:0000313|Proteomes:UP000002686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX PubMed=24704842; DOI=10.3390/genes3010035;
RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA Smith A.A., Giraud E., Medigue C., Moulin L.;
RT "Comparative genomics of aeschynomene symbionts: insights into the
RT ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL Genes (Basel) 3:35-61(2011).
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:CCE09372.1}.
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DR EMBL; CAFK01000242; CCE09372.1; -; Genomic_DNA.
DR RefSeq; WP_008971883.1; NZ_CAFK01000242.1.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000002686; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
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:InterPro.
DR CDD; cd12116; A_NRPS_Ta1_like; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR CDD; cd00610; OAT_like; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
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; 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; 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; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
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; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
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; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000002686};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..441
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 942..1020
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2584..2658
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2657..2698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2698 AA; 292592 MW; 9240D2E7DA025176 CRC64;
MNENAGLEEG GIAIVGMAGR FPGAQSVAEF WRNQLDGIEA ISQFRVDELE ITNKQAVGND
PRYVKARSIL EDVDLFDAEF FGIYPREAEL MDPQQRLFLE CCWQALEDAG CVPQTYPGLI
GVYAGTSMSS YFLTRLCTEP GFIEKFAAGY QVSNYVEMMG NSPDFLATRV SYKFNLRGPS
VTMLSACSTS LVAITQACQS LLTYQSDMAL AGGTSITLPQ KRGSVYQDGG MVSRDGHCRA
FDADAQGTVF GSGVGVVVLK RLEDALQDGD QIYAVIRGYA VNNDGSSKVG YTAPSVEGQA
NVIAMAHQAA DIDPATIGYI EAHGTGTPLG DPIELAGLTQ AFRARTDRTQ FCTIGTAKTN
VGHLDIAAGV TGLINAAHVV RHGVFPPTLH FKNPNPKFDF KGSPFRVVAE RTEWDAGDAP
RRAGVSAFGV GGTNAHVVLE QAPEQQSSAS RRTKQLLVLS ARSQTALDAA GDRLRAHLEA
HPGSNLADVA WTLQTGRREF GYRRAVVAGD VAEAVRSLSE RARVPAPSRS REVSDVCFLF
PGQGSQHPNM AREIYDLEPV FRETVDRCAE ILRPHLGADL RTVLYPDAGA SDEARRAVTD
TIIAQPAIFT IEYSLAQLWF SWGIRPKAMT GHSIGEFAAA CIAGVISLED ALGFVALRGR
LMQGVAPGGM LSVRLPEAEL RQRLGAPLSL AAVNSPSLCV VAGPLDPLAQ FERELNEAGV
ACRRLVTSHA FHSAMMDPLI DPLANALSGI RLNPPQIPYV SGVTGTWVTD REATDPVYWA
RHAREPVQFS AAIQELRNRP DAILLEVGPG NVLTTLARQH GQPAANSVIA PSLSDGFSGE
GDYEALLSAM GKLWVAGEKP DWTAFHAGER RHRMSLPTYP FERKRYWLQN AQAAFDQSVP
GSTEAPVTSL SSEAKPQVLQ GSDAVNVMSS VSSAVAPATS AKRRDRIQAA LVEMFEGLSG
VDLAAADPAT TFLELGFDSL FLTQVAQALQ EKFAVKITFR QLLNDVSSLN ALVDHLESQL
PADAYAERVE SRSELQAVAP VVVVTATAAS EPAVQAALVS AGSVSEGAME RLMREQLQAM
NQLFSKQLDA LNATRGPTAA APATIPASNA TVELRAAAEA VTSAPAAAPA APQKAFGPYK
PPQTTASQDL TPAQQKQLNI LIDRVTRRTA KSKAFTQQHR QALADPRVVS GFRPQWKEMV
YSIVTDRSQG SRIWDIDGNA YIDLVNGFGP IMLGHRPDFV EKAIEAQLRN GFETGPQTPL
AGEVAQLFCE MTGNERMAFC NTGSEAVLAA LRVSRTVTGK NKIVTFSGDY HGMFDEVLVK
GFMNKAGEPQ SVPIAPGIPR QSVSNMVVLD YGAEQSLDWI RRNAADIAAV LVEPVQSRHP
SLQPVDFLKQ LRKITEDCGA ALIFDEVVTG FRVHQGGCQA KFGIRADLAT YGKVVAGGMP
VGVLAGKSRF MDALDGGMWQ FGDDSYPQVG VTFFAGTFVR HPLALAAMRA VLRHFSEQGP
ALQERLNQRT SELVQKLNEV VREHGLPTQV ETFGSFFYLG FPASEPLANL FYFYMRDKGI
HIREGFPCFL TTAHSDADLE AIVTAFRESA IEMRQAGFLG DVVEAPALAP AAVAAQLDRP
EAAEAPLTES QLEVWLSDQL SSDASCSYNE SVSLHLRGNL DVTALRRALD LVVARHQALR
STFGGEGDRQ SFAARLTLEV PTIDLRSLAP QEQESQLHQI IATDAQTPFN LSAGPLVRAR
LVTLAADHQI LIFTAHHIVC DGWSTNVLVD ELSQAYNATK QGLSWNPPAS MPFADYAKSQ
AEFVDSAEGR KVESYWLEQF REVPAPLNLP LDRPRPAIKE FKGATFRTRI EADAYNRIKK
FGASQKCTLF VTLLAGFEIL LGRLSGQDDI VVGVPTAGQS LLDNVTLVGH CVNFIPLRGR
LTGNPTAAEF LAQMKQTVLA GYEHQNYTYG RLVRKLALQR DPSRLPLTEV QFNLERIGGK
LGFDGVDAEV DPNPKSFVNF DIFLNIMEAS DGLTLDCDYN TGLFDEDTIG RWLEHYKILL
EGMAAQVHAP VSKLPLLSAA ELDGLARWND TFTNRPNQST VHGLIEAQVG RSADAIAVMF
GPERLTYAEL DGRANQLAQH LRKLGVKPGV LVGLFIERGL DMLVSLLGIM KAGGAYVPID
PTFPPERVRF VLEDAGAQVV VTQAELTKQW SFGDAKVVQI DTEWPVIARE SSARLDGGAG
PADLAYVIYT SGSTGKPKGV EVPHRAVANL LQAMQVQPGL NSSDVLAAVT TLSFDISGLE
LFLPLTVGAR LAIVSRDTAQ YSVRLLEYLK EVNATVVQAT PVTWQQLLDA GWTGEPALKV
LCGGEAFPRE LANELVKRAA SVWNMYGPTE TTIWSAVLQV AAGEGPVPVG YPIANTEFLV
LDHDLQLAPV GVAGELYIGG AGLARGYHNR PELTSERFVA HPFRSEPGTR LYKTGDLVRR
RRDGTLEFLG RLDNQIKLRG FRIELGEIES ILETHPGIAQ GVVSLREDVA GEKRLIGYVI
PKNGVAPGAA ELREFIVKKL PAYMAPAAYV SLDAMPLTPN GKIDRNALPA PSWTKQQESM
AYAVPRNADE EKLAAIWAEV LRLPRVGIND NLFELGADSL HVFQITARAN KAGIQVTPRQ
ILKFRTIAAI FDELSKGTQD QTTTSDRAIK PVPRQQYRLA PQPVRQVSRW PQSSSSHN
//
