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Database: UniProt
Entry: E8X008_GRATM
LinkDB: E8X008_GRATM
Original site: E8X008_GRATM 
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}.
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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
//
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