ID E8X008_GRATM Unreviewed; 2626 AA.
AC E8X008;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:ADW68904.1};
GN OrderedLocusNames=AciX9_1858 {ECO:0000313|EMBL:ADW68904.1};
OS Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343};
RN [1] {ECO:0000313|Proteomes:UP000000343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Pagani I., Rawat S.R., Mannisto M.,
RA Haggblom M.M., Woyke T.;
RT "Complete sequence of chromosome of Acidobacterium sp. MP5ACTX9.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002480; ADW68904.1; -; Genomic_DNA.
DR RefSeq; WP_013580223.1; NC_015064.1.
DR STRING; 1198114.AciX9_1858; -.
DR PaxDb; 1198114-AciX9_1858; -.
DR KEGG; acm:AciX9_1858; -.
DR eggNOG; COG0001; Bacteria.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_70_2_0; -.
DR OrthoDB; 9765680at2; -.
DR Proteomes; UP000000343; Chromosome.
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; cd19531; LCL_NRPS-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; 3.40.366.10; 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; 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; 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:UP000000343};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..435
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 911..989
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2523..2597
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2599..2626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2626 AA; 282438 MW; D0ECBD1D6AC9F14E CRC64;
MSDEVMDGIA IIGMAGKFPG AKDVATFWEN LLAGKDTVSH FTATELEARD GQSGGEDYVA
ARGILEDVGM FDAEFFGIAP KEADRMDPQH RIFLEACQQA LEDAGYVSQE YAGEIGLFAG
CSLNTYLLAN LSHDREFLDR LTANYQVGEF QVALGNDKDF LTTRAAYKLD LRGPVVSVQS
ACATSLVAIC QASQALMNYT CDMALAGGAS ATFPQRRGHI YQDGGMASRD GVCRPFDASA
TGTVFGHGVG VVVLKRLEDA VRDGDHISAV IRGFAVNNDG SAKAGYMAPG VDGQSRVIAA
AQAMAGIEPE SVTYIEAHGT GTPLGDPIEI AGLTKAFRLG TDRNNFCSIG TAKGNIGHLD
SAAGVAGVIK TAMSLTHRTI PGLAHYEAPN PNIDFAETPF FVSKDARAWT ADGPLRAGVS
AFGVGGVNAH VVLEEAPGIE KSGESERDQV VCVSARSAAA LEAVVAGLAG FFEAGSAVKL
ADVAYTLSVG RRAYEHRFAF SAANVEGAVS ALRSQRKRTA VGKGQRRVAF LFSGQGSQFV
GMGRELYAAE PVYRRVVDEC CEAVGGALEV DLRELMFAPV SETASATLQQ TRYAQPSLFV
TELALARLWE SWGVTAEAVV GHSLGEYVAA TVAGVFTAAD AMRLVCLRGR MMQELAAGAM
TSVALGEEAL GKYVTAGVSI AALNSPRASV LSGSFEAIVG LEAELERDGV GFRRLHTSHA
FHSEMMEPML AGFEAEVAAL ELKAPAMRFV SSVSGTWITS DQAMSPRYWA EQCRKAVRFG
DAVATLLGDG FDVLLEVGPG EALTSLSMHQ RGVSEFSAVA SLPMPRADRE SKPVQAAVAE
LWSVGVGIDW AAYYANEVRH RVSLPTYPFE RKLHWVEPPA RTTPEGISKI EATPMNNTAP
LAAAMPTAVE ARPVRLQKMI AGVFAEMSGI ETSAEEMDHP FLELGFDSLF LTQATQSLQR
TFGVKLTFRQ LMEQYSTIAS LAGYLDEILP ADAFPAAAPV AVVAPISTAG TVTVTNANTG
NTPIERLLSD QLAAMSELFA NQLATLRGAA GMAAPAVSAA MVVSKPAVAT TSPVPVSNAD
VKHGSFRPLQ AKTSHELDDK QKKYIADLIA KYEAMTPTSK SMTQASRARL ADPRAVAGFR
PQWKEMVYPL ITDRARGSKI WDVDGNEYID IVNGYGCIMF GHSPEFVVEA AKAQLDKGVA
IGPQSALAGE VAALICELTG NERATFCNTG SEAVMAAIRV ARTVTGRDKV VYFAGDYHGT
FDEVLIRNTP RGSAPVAPGI PLANTTNIIV LEYGTDESLA WIRANAGELA AVLIEPVQTR
NPGLQPFDFI REIRTITEKS ETVMIIDEVV TGFRLAPGGV QEKYGIRADM CTYGKVIGGG
HPIGVLSGKA MYLDALDGGA WQFGDDSGPE VGVTFFAGTF VRHPLALAAA RSVLNHLKAN
GPELQLELNR KTARIAESLD RFFADEGVPC RVHHFASWFY FVFPHDARLG SLFYYAMRAK
GIHIQEGYPC FLTTAHTEAD LDAVEKAFKD TILEMQTNGA MPRELAEAPV AAGMHPDALS
ETPARIQLTE PQREVFLAAA LSDEANCAFN ESLTLRLHGP VRMDDLSFAL DAVVARHDAL
RSTVSVDGES LCFSPAFTGQ NEIVDLRLTS AEEQKKLIDE RVVSEGKAPF DLHNGPLLRS
VCFIASDRDA VLVLTAHHIV LDGWSANQLL EEVGKVYSKG ASALTGLAPL LPFSSYAVRE
SKRQESGEFA DNERYWVSKF EGRSPRLDLP TDRTRPVNKT FNGATIEGSL GAQLYADLKK
LSAKNGCTLY VTLLSAFQIL MHRLSRQDEV VVGISTAGQA LFEGASLVGH CVHFLPMLSE
LKGDETVQQH MKATRTALLD AYDHQEFTYG SLLQKLKFER DPSRLPLIEV QFNLEKVGAN
VQFDGLTTEI KANAKQFVNT DLFLNVVEMG SDLEFMCDFN SDLFDAATLH RWMGLWAQML
TSETLDATVQ VLDLEMLPAA EKALVVSEWN KTDVYFGAFE AMPAAFLNVA AKHPERVAIQ
CGPQSWSYGE LMEYSTILAK RLVREGLKPG GLAGICVERS PEMVGAMLAV MMAGGAYLPL
DPRHPRERLS MILGDAGISM LLAGRDSSVE TTAPILKITG PQPQGNEALP GTIGSDSLAY
VIYTSGSTGV PKGVAIEHGA LMNLLRSMER EPGLGSEDVL VAVTTLAFDI AALELLLPLL
TGAKLVIATD EQVQDGTMLL RLLESTKATV LQATPGAWRI LLDAGWTSAL PLKVLCGGEA
LPRDLAEKLL ERSNDVWNVY GPTETTIWSS ATKVTHGDGP LHVAPPIANT QFYVLDERQR
PVPVGVTGEL YIGGDGLARG YWKRPELTAE KFVASPFGEG KIYRTGDVGR WHMDGSIELM
GRADFQVKIR GYRIELGDIE SALGKHAKVR EAIVVQQKIG ESGASRLVGF VDAGESAAEP
AGLVEELQLL LERSLPEYMI PNAIIALREM PRTPNGKVDR KSLIRHADAE GLGVKSVTRE
FTAPVTEAEI RLAGIWAEVL ALKAVSTTDS IFELGADSLL IFRIAARSQR EGLAVTATQI
FQHRTIRALC RELEEKAGTA TAGRPAARIS AASRESYKRP KVQVDA
//