ID A0A168HDV0_9ACTN Unreviewed; 1001 AA.
AC A0A168HDV0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Acyltransferase family protein {ECO:0000313|EMBL:OAA17959.1};
DE Flags: Fragment;
GN ORFNames=UG55_11451 {ECO:0000313|EMBL:OAA17959.1};
OS Frankia sp. EI5c.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=683316 {ECO:0000313|EMBL:OAA17959.1, ECO:0000313|Proteomes:UP000077018};
RN [1] {ECO:0000313|EMBL:OAA17959.1, ECO:0000313|Proteomes:UP000077018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI5c {ECO:0000313|EMBL:OAA17959.1,
RC ECO:0000313|Proteomes:UP000077018};
RX PubMed=27389275;
RA D'Angelo T., Oshone R., Abebe-Akele F., Simpson S., Morris K., Thomas W.K.,
RA Tisa L.S.;
RT "Permanent Draft Genome Sequence for Frankia sp. Strain EI5c, a Single-
RT Spore Isolate of a Nitrogen-Fixing Actinobacterium, Isolated from the Root
RT Nodules of Elaeagnus angustifolia.";
RL Genome Announc. 4:e00660-16(2016).
RN [2] {ECO:0000313|EMBL:OAA17959.1, ECO:0000313|Proteomes:UP000077018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI5c {ECO:0000313|EMBL:OAA17959.1,
RC ECO:0000313|Proteomes:UP000077018};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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:OAA17959.1}.
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DR EMBL; LRTK01000145; OAA17959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168HDV0; -.
DR STRING; 683316.UG55_11451; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000077018; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; IPR013968; PKS_KR.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:OAA17959.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077018};
KW Transferase {ECO:0000313|EMBL:OAA17959.1}.
FT DOMAIN 1..117
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT DOMAIN 187..372
FT /note="Polyketide synthase dehydratase"
FT /evidence="ECO:0000259|SMART:SM00826"
FT REGION 309..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OAA17959.1"
FT NON_TER 1001
FT /evidence="ECO:0000313|EMBL:OAA17959.1"
SQ SEQUENCE 1001 AA; 101905 MW; 76B97D7263C1DA2F CRC64;
TRRLTVSGAF HSPHTDPLLD DFTAIATTIT YTPPTIPIIS NLTGTTANPT DITTPHYWTR
HLRGTVRFHQ SIQTLHTLGT TTYLEIGPDA TLATLTEEIL DGAERRCRVS AALRRGRGER
LALLTALAEI HVEGHPVDWR ALTPPPDGLV GRPVDLPTYP FQRRRFWIGP PAADTDATGL
GLLPGAHPLL AAAVDVAETG TSVFTGRLSV DETPWLADHA IAGTILLPGA ALVDLALHAA
AHAGASAVAE LTLAAPVTIP HPGTRTIQLT LGGPDEAGRR PLTVHTAADG AEPGEDPGWV
RHATGIVDTA APADGAGGTG STGGTGSTDS TDGESLAGTP WPPAGAEAID VSGHYDRLAG
AGYEYGPAFQ GLRAAWRDGE DIVAEVAADA GASAGYPGDA TATGTNGHVL HPALLDAALH
AISLLPGTGT GGDADTASVY LPFSWEGVRL LTADAAAGAA RAAGAAPDVL RVRVTPRPAA
DGAVAGADGG TITVGLRLYD GAGVPVAAVA GLRLRPLRPE QAGGAAHRHH EDLYQVRWEP
VTAAATSTAP GTATARWGWV GSPESPFEDG PGGLAAAVSA AGAEVVRYAD LPALGAAGQA
PEVVLTAFTG QPAEPGPADA RQAAARALDL LTAWLGDERL ASARLVLLTR GAVATDGPAD
ASTGTPADVP ADPPAGAAPA GGVDLTHAAL WGLVRSAQAE YPGRFLLVDV DGEDASPPAV
AAAVRWALVA DEPALAVRRG AVLVPRLARV PVSAGTLPAD PADLPDLPDL PADPPGTVLV
TGGTGTLGAL AARHLVTHHG IRHLLLASRR GPAAPGADNL AAELTALGAD VQITAADLTD
PAAARALIET IPSHRPLTAV IHTAGILHDA TLAALTPDQL DTVLKAKIDT SWNLHQATLD
QPLTAFVLYS SLAGTVGTPG QANYAAANTY LDALAHHRRA TGLPATSLAW GLWEDTSTIT
AELTATDHTR IRRAGLLPLP APLGLALLDT ALTRADPLLV P
//
