UniProt: A0A1V0GR36

Database: UniProt
Entry: A0A1V0GR36_9RHOB

LinkDB:  A0A1V0GR36_9RHOB 
Original site:  A0A1V0GR36_9RHOB

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Ontology (3)   
   GO (3)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (41)   
   InterPro (23)   
   Pfam (10)   
   PROSITE (3)   
   SMART (5)   
All databases (46)   

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ID   A0A1V0GR36_9RHOB        Unreviewed;      2093 AA.
AC   A0A1V0GR36;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=KR domain-containing protein {ECO:0000313|EMBL:ARC36268.1};
GN   ORFNames=A6J80_07655 {ECO:0000313|EMBL:ARC36268.1};
OS   Paracoccus yeei.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=147645 {ECO:0000313|EMBL:ARC36268.1, ECO:0000313|Proteomes:UP000191257};
RN   [1] {ECO:0000313|Proteomes:UP000191257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_252 {ECO:0000313|Proteomes:UP000191257};
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA   Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S., Nadendla S.,
RA   Geyer C., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP020442; ARC36268.1; -; Genomic_DNA.
DR   STRING; 147645.A6J80_07655; -.
DR   KEGG; pye:A6J80_07655; -.
DR   eggNOG; COG1020; Bacteria.
DR   eggNOG; COG1028; Bacteria.
DR   eggNOG; COG3319; Bacteria.
DR   eggNOG; COG3321; Bacteria.
DR   Proteomes; UP000191257; 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: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; IPR009081; PP-bd_ACP.
DR   InterPro; IPR002347; SDR_fam.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 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   PRINTS; PR00081; GDHRDH.
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   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:UP000191257};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..439
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1714..1789
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2093 AA;  224172 MW;  AB484052278F51EC CRC64;
     MAFDESQISE TDIAIVGMAA QLPGASNVAE YWDNLCRGVE SIQRIPQAEL IARGESRARL
     SDPNYVPAAA ILGQYNEFDA EFFGLSPKEA AIMDPQHRKF LETCWHALED AAHVPDRFAG
     NIGVWAGCGM GSYFYWNVCS NRDLVDGVGH FLLRHTGNDK DFLSTRVSHV FDLTGPSINV
     QTACSTSLVA IHMACQSLNS GETDMALAGG VTIEMPHGLG YLYKENEILS PDGHCHAFDH
     RAQGTVFGSG AAVVVLRRLR DAIADGDHVW AVIKGSAINN DGAAKAGYLA PSVEGQAQAI
     AEALVMSGVS SDSIGYVECH GTGTALGDPI EVAALNQAYA RVSDGTRQGP CRIGSVKTNI
     GHLDTAAGSA GLIKSALAVH HGRIPASLGY EAPNPAIDFE GGPFQVNDRL GDWPVAGLRR
     AGVNSLGVGG TNAHCVLEQP PAPVAAEDSD WPFHIVAVSG RSKAAVDANG AALAAWLRAN
     PGVDMADLSF TLTQGRRQFD RRRVLVAHDA AEAAALLDGG DNRLVFDHQL VAEGAEPVFM
     LPGGGAQYAG MARGLYQTEP VFREWMDRGL DHMAQAHGTD LRALWLPEPG AEAEADRRLL
     QPSLQLPLLM ITEYALAKLW ISWGVRPTAL IGHSMGENTA ACIAGVMSFE DCIGLVRLRG
     LLFDRVPAGG MLSVPLEPVE FQTELDALGL DLAAVNGPSM SVVSGPDAVL DQFAARMAAR
     EVECQRIAIS IAAHSRMLEG ILAEFRAYLA SIPLNAPQIP IISNRSGQPL TEAEATSPDY
     WVQHLRGTVR FADGIAHLAQ NPDRIFLEVG PGRAMQAMAK AHPAVNAGQV ISTLRHRDHA
     TADDAYFMAA LARVWACGGH IDWDQIWGGA RRRRLSLPGY QFQRKRYFIE RSTTAVAEAE
     AELARIEDPA AWGWRPAWKL ASPAIEIGPK GPIASQRRNW LVFADDLGIG DRLAELLRAL
     DQAVAVVSIA DTFADKGEGR FTLPVESDRE GYEMLLAALA AQDRVPDRIL HLWSLTRGAS
     FRAGSSLLNS QLERGYFSLL HLAQALGTEL PDARLDLIAV CNDALQVAGE PASAPEKACA
     AGPIRVLPHE MPQVSARLVD IRLPDRKGQD AVASMLLEEA LAPSGAALAA WRDGRRFEQS
     LERVALAEDG MAGIPDGAVC LITGGFGGIG QAIARELAPR GVKLALTTRG RTDAAPVTAA
     VRHLESLGAQ VLAIRADVTS AEDMARAAAE VRARFGSLDV VLHAAGVIRD SLIAAKTDDE
     SWDVLAPKLL GTRALAEALA DDPAKLTVLF ASTSSVIAPA GQADYVAANE YLNAVARSAP
     AALGRVVAVN WGVWADAGMA ARALGLDQPP PAGAVVDRPL LDQVMPMPVG REFRTALRME
     HWIIGGHKTA QGQALMPGTG WIELVAEAAL ESGLSLPFVI RDLEFQRPVL VDDTALVTTR
     VEPAGDSLRV TILDDPQGAP NVTALLAPLQ EAAPAPLETA GPWDKDGQGA ALPSAQEGQM
     DFGPRWKVLR RFRLSAGEGL AQLALDPEFR SDLDQGWLAH PALMDIATGW AMALIRGWGP
     GHLWVPMGYR SIRLYRPLPA EVVSRIRNAG ENTDALGMAQ FDITLAAPDG TVCAEIRGFA
     LRKLTAAISA QPRRAQAGRS MSPAERRLHH NISQGIPAAV GPAMLSRAIS TGLSQVYVSS
     LDLNALMAEA AVVTDAAPAE GGFERPDLDS DFVEPTPGTQ AELAAIWSEL LGIAQVGAAD
     SFFDLGGHSL IAVRMFGQLR KKFDVDLPIS TLFEAPTIAE LAALVEERTG PRLPVADNVR
     ALPAAEGRAR RRFLVDMGGR GDGTPFFMVA GMFGNVMNLR QLAQRLGADR KFYGLQARGL
     LGDDKPHESF ADAARDYIAE LREVQPQGPY LLGGFSGGGL TAYEMARQLR ASGEEVAMLV
     MLDTPLPLRE PLSRKDRLLI RLAETREGGF GYIRQWVGDR IRYEVSQRAK SQALEAGAQA
     AEGAFHDLAI EAAFLSWLPG MTLTEWDGPV AMFRPPLDPR FRVSGGRHVT SAREYLLEDN
     GWGPWMPKLR VIEVPGDHDS MVLEPNVRRM ASVLRELLRD ADGEASARAQ AAE
//

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