ID A1VQP6_POLNA Unreviewed; 410 AA.
AC A1VQP6;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=Nodulation protein E {ECO:0000256|ARBA:ARBA00039445};
DE AltName: Full=Host-specificity of nodulation protein B {ECO:0000256|ARBA:ARBA00041756};
GN OrderedLocusNames=Pnap_2672 {ECO:0000313|EMBL:ABM37974.1};
OS Polaromonas naphthalenivorans (strain CJ2).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM37974.1, ECO:0000313|Proteomes:UP000000644};
RN [1] {ECO:0000313|Proteomes:UP000000644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644};
RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT tar-contaminated sediment, reveals physiological and metabolic versatility
RT and evolution through extensive horizontal gene transfer.";
RL Environ. Microbiol. 11:2253-2270(2009).
CC -!- FUNCTION: Proposed to synthesize NOD factor fatty acyl chain. Involved
CC in the synthesis of a highly unsaturated fatty acid moiety, which forms
CC part of a lipo-oligosaccharide that is responsible for host
CC specificity. {ECO:0000256|ARBA:ARBA00037576}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004533}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467,
CC ECO:0000256|RuleBase:RU003694}.
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DR EMBL; CP000529; ABM37974.1; -; Genomic_DNA.
DR AlphaFoldDB; A1VQP6; -.
DR STRING; 365044.Pnap_2672; -.
DR KEGG; pna:Pnap_2672; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_4; -.
DR OMA; IEPEWSA; -.
DR Proteomes; UP000000644; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11712:SF352; BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE I; 1.
DR PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:ABM37974.1};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Reference proteome {ECO:0000313|Proteomes:UP000000644};
KW Transferase {ECO:0000256|RuleBase:RU003694, ECO:0000313|EMBL:ABM37974.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 1..408
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 410 AA; 42640 MW; BA9F62F3FF956D93 CRC64;
MRRVAVTGMG VVSPLGHSAQ QAFDAARAGR SAVRRLDVAF AHRLAAPIAA TVNFNGADHF
DPPRLRMLDR VSQFALVAAS RAMADAQPEL SDTERSRAGV FVGTGMGGIN SIDEGYQTLY
GENSDRIKPF MVLMGMHNAP AAWIGIEHGF SGPNMSYSTA CSSSAVAIGE AWLRLAHGDL
DIALAGGTEA PLAFGSLKAW EALRTVASID AADPSASCKP FAGNRSGMVL GEGAAMLVLE
PWERALARGA AIHGELIGYG LFTDAGHITR PSVEGQAAAM RAALRSARID AAQVDAINAH
GTGTPANDGI ETAAIKAVFG NRAARIPVSA TKALHGHLLG ATSALECVLS FMAMQHSVAL
PTMHLQQADP QCDLDYVANA AREGVPVRTM LSSSFAFGGT NAVLAFRAAP
//