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Database: UniProt
Entry: A0A1H8JUR3_9RHOB
LinkDB: A0A1H8JUR3_9RHOB
Original site: A0A1H8JUR3_9RHOB 
ID   A0A1H8JUR3_9RHOB        Unreviewed;      2131 AA.
AC   A0A1H8JUR3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Acyl transferase domain-containing protein {ECO:0000313|EMBL:SEN84245.1};
GN   ORFNames=SAMN04488103_108105 {ECO:0000313|EMBL:SEN84245.1};
OS   Gemmobacter aquatilis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Gemmobacter.
OX   NCBI_TaxID=933059 {ECO:0000313|EMBL:SEN84245.1, ECO:0000313|Proteomes:UP000198761};
RN   [1] {ECO:0000313|EMBL:SEN84245.1, ECO:0000313|Proteomes:UP000198761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3857 {ECO:0000313|EMBL:SEN84245.1,
RC   ECO:0000313|Proteomes:UP000198761};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOCE01000008; SEN84245.1; -; Genomic_DNA.
DR   STRING; 933059.SAMN04488103_108105; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000198761; 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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd08953; KR_2_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
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; IPR049490; C883_1060-like_KR_N.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
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   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
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; PF21394; Beta-ketacyl_N; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198761};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SEN84245.1}.
FT   DOMAIN          13..441
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1758..1833
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2131 AA;  229653 MW;  18F7E08A90BC66AF CRC64;
     MADQTLLSDP VSETDIAIVG MAAHLPGAPS IVDYWENLRA GIESIRHLTE AELLANGESP
     AKMRHPNYVP AAAPLDKFAE FDAEFFGFSP KEAAILDPQH RQFLEVAWEA LENAAHVPER
     FNGSIGVYAG CGMGSYFYFN LCSNPDLVEN TGMFLLRHTG NDKDFLSTRV SHIFDLKGPS
     INIQTACSTS LVAVHFASQA LLNGECDMAL AGGVTIELPQ GRGYVFNEGE ILSPDGHCHA
     FDHRAQGTVF GSGAGCVVLR RAVDAIRDGD HIWAIIKGSA INNDGAAKAG YLAPSVDGQA
     RCIAEAQAIA GVPSDTVDYV ECHGTGTFLG DPIEVAALTA GFRESADSVG TCRIGSVKTN
     IGHLDTAAGV ASLIKVALQL HHREMAPSLG YEAPNPAIDF ETSPFKVNDR LTAWEAKAHP
     RRAGVNSLGV GGTNAHAVLQ EAPVRGASDE SDWPFQPLVI SARSKGALDD AARNLAAHLR
     AHPEQKLADV AWTLKEGRRA FEKRRVLVAG SPDEAADLLE GKDARRVFSH DHLGDNPEVV
     FMFPGGGAQY AGMARGLYDT EPEFRDWMDK GLAILQPKLD YDIRALWLPE PGQEAAADAR
     LKRPSVQLPL ILITEYALAK LYQSWGVTPA ALIGHSMGEN TAACLAGVMS FEDCIGLVHL
     RGQLFDTVPP GGMLSVPLAE ADLRPRLTGD LDMASVNAPG LCVVSGSDAA LAALAAGLAA
     EGVETQRIAI DIAAHSRMLE PILGRFGEYL RAIRLHAPQI PIISNRTGLP LSADLARSPE
     YWVQHLRNTV LFQQGLAQLT ATPGRVYMEM GPGRALSSLA QANGVAAGQV IPALRHPEQK
     ISDDQWHIAS IARLWACGVA VDWEPIWGGA RRLRLPLPGY AFQRKPYFIE PGKAGVVEAE
     ALPMRLADVA DWGWQPVWRQ HAAAVEFDEP AEAPKHSWLV FVDEAGLGAQ VVAQLRAAGQ
     SVVTVRAGDA YARDGEGGFI LNPERGREGY DALIRDLVAA GRAPDRIAHF WLVTARESFR
     PGSSFFHRNI EQGFYALMFL GQAMAEENLP RPIHLSVVTT GAAQLKDEGL PYPEKAAIAG
     PAKVMPHELP GVSCATLDVQ LPAAPKGRWA KADPQAMAVL AGQVVEDLLA APSSHAALRR
     GEKRYERALK RLALPEAAMG LPEGAPVLIT GGFGGIGLTL AEKLAVEARA KIVLIARSAL
     PARADWPQHL AQGDAVARRI LAVQRLESLG AEVLVARADV CNAEEMRAAV AEAEGRFGPL
     RAVIHAAGVV DDAPLLAKTP AQVEGVFAPK LHGTHVLDAL FPDGRLDLLV LFSSTSTVTG
     PVGQVDYVAA NEYLNAYAQG RRGGKTRVLA LNWGIWADVG MAAEALAERT GARPLAPRVP
     VKRPLLDEAG YDRAGNRIFA TRLTTERWIL DGHRTKGGTA LIPGTGYLEM AAEVAREEGF
     GAFELRDLTF FRALDVADGA SREMRVKLLR SDEGFGFEVR SGVDHRGRTG FALNAQGRLM
     PLRAKPGQID PAAIAARCGV AREDIRGLRS PQEEHLNFGP RWRVLHRMAL GQGEGIASLT
     LPLAAQPDLA QGWLLHPALM DLATGWAMEL ISGYQPTHLW VPVSYARLRA HAPLPARVIS
     WVRNAAVNRG EGPVAVFDVT LATETGEVLV EIEGFTIRKL EGAFATKAPE LRDLEFDDAQ
     AQKAASPQEE RLIHNLGQGI RAAEGADAFA RALATGQAQV IVSSLDLPAL VRQADAVEAE
     RPEGQSFARP DLDSAYIEPR NDIERTLTGF WQELLGVGQV GVEDDFFALG GHSLIAVRLF
     SMVRKAFRVD FPISVLFEAP TIAACAALIE ERIGPQDGTA PKAEAPTRRF THLVAMHEGA
     GGPKQPFFLV AGMFGNVLNL RHLAQLLGGD RPFYGMQARG LYGDAEPHRT LPEAARDYIA
     ELRQVQPQGP YLLGGFSGGG LTAWEMARQL EAAGEQVSLL VLLDTPLPMR PPLSRLDKAL
     IKAAEMKARG PGFVADWARR RVAWEIEKRR PKQATDTAHQ FHNTEIEAAF RAALPIYALP
     LRKGPTALFR PPLDRRWAVS NGQWVSAARE YVFPDNDLTR FAPALQVVEV PGDHDSMVLE
     PNVRVLAARL REAIAGAEEK PPAPTLREAA E
//
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