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Database: UniProt
Entry: A0A1G7NYQ3_9SPHI
LinkDB: A0A1G7NYQ3_9SPHI
Original site: A0A1G7NYQ3_9SPHI 
ID   A0A1G7NYQ3_9SPHI        Unreviewed;      2577 AA.
AC   A0A1G7NYQ3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=PfaB family protein {ECO:0000313|EMBL:SDF78987.1};
GN   ORFNames=SAMN05216464_13110 {ECO:0000313|EMBL:SDF78987.1};
OS   Mucilaginibacter pineti.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1391627 {ECO:0000313|EMBL:SDF78987.1, ECO:0000313|Proteomes:UP000199072};
RN   [1] {ECO:0000313|EMBL:SDF78987.1, ECO:0000313|Proteomes:UP000199072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47C3B {ECO:0000313|EMBL:SDF78987.1,
RC   ECO:0000313|Proteomes:UP000199072};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194}.
CC   -!- SIMILARITY: Belongs to the thioester dehydratase family. FabA
CC       subfamily. {ECO:0000256|ARBA:ARBA00006714}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000256|RuleBase:RU003694}.
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DR   EMBL; FNAI01000031; SDF78987.1; -; Genomic_DNA.
DR   STRING; 1391627.SAMN05216464_13110; -.
DR   OrthoDB; 9778690at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000199072; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0008693; F:(3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:InterPro.
DR   GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0034017; F:trans-2-decenoyl-acyl-carrier-protein isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01287; FabA; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 4.
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; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR010083; FabA.
DR   InterPro; IPR013114; FabA_FabZ.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
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; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF51; INACTIVE PHENOLPHTHIOCEROL SYNTHESIS POLYKETIDE SYNTHASE TYPE I PKS1-RELATED; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF07977; FabA; 3.
DR   Pfam; PF00109; ketoacyl-synt; 2.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 4.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199072};
KW   Transferase {ECO:0000256|RuleBase:RU003694}.
FT   DOMAIN          3..435
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   2577 AA;  283087 MW;  C18D51C705BE3318 CRC64;
     MKFEEIAIIG EGCVLPGCFN PAQLWETVLH NRVNISNAPD NDWRVPMVEV LHRQNNSDMA
     NRAWHDKGGY IKGFEQHFDA GDYNLDTRLV EELDPLFKWS FYAAKQALTD AGITNNDLLQ
     SAGLIMGNLS YPTRSFSRLF EEFQLKQFFP DIKGKTSVND LNRFCSGLPA MLTAKAIGLQ
     GEAFALDAAC ASSLYALKLA CDRLHDHRAD MMLVGGVCAA DQLFLHTGFT ALNALSPSGQ
     SRPFNAAADG LIPAEGAAFI VVRRLADAIR DGNKIRAVIK GIGLSNDGRS GGFLSPSTDG
     QVRSIKQALA LADIRPAEVS YLECHATGTS GGDAIELASI KAVYGDNPDL VLGSLKANLG
     HSITASGVAG ILKVIAAFKH KRIPAMLNHL PLAPVVAASG YPVLSADKPW LGNKKIAGIS
     NFGFGGNNAH LILAEWDRQP VAVAVQNKKN GVAIIGIAIR SDRFSGTSQV FNYLINDVVS
     PPASELEFEA RALNFPPNDL KQTLGQQLLL LSTVQDLLTT CGPIDAQQSG VFIGMGVDAE
     INRYGLGKRL ASLLKEHSLG VSAEALAETE ASIAAPLTPA SVLGTMPNIP ANRISNQFNL
     EGPGFTVSAE ELSGLKALRI AVDAIRNGEL KSAIAGAVDL SNEELHGDVL KKITGFEGDT
     TDLAVALLLK DHEQALAAGD TIFAIISDKG GEEENLSIDP DWVNKKLGYT HAASGLLSVA
     IAALFTRNRL RIDPTGTGLL PIPEPKNGLA YQIVVHSYFG GSETFRLVAQ PVGSISGRAI
     NFVKIYCYAG SAVTSLREAV LAGKINGKGT HKLTIVCSED EIAQNSQLAV HLLDKPDLRE
     GWLNDVIFYS SEAVDGKIAF AFTGAASAYP RMGQHLLQEF PALSASLAPS CSNPGFAANW
     IYENDSGKAD LPFYQLAGSS FLCQIHAAFS MKILGIKPDI ALGLSSGETN SMFAMGVWDD
     MDALLAEIEA SDLYTKALGV DFAAVRTHWN LAENEPVNWE SWRAIATVAE VEALLATETR
     AYLTIVNTDT DCVFGGDAEA CARIIDKIGK HRVMQLHHDI AVHCEVVNPY EAEWRRLHTR
     NSKPIKGIAF YSNYLNDIYE TTTENVADAL TGQAVKPIHF PRIIEKAWAN GVRIFIEHGP
     RNSLSAAIST ILQGKDHVCV SFDRAGKNSL LQAAKVAAQL WAYGVAVDLS CFKPGPIHNA
     KNPITLSFPL RMPAIKRLPL AATVMPQPPM SAIKKMRPAP TLALTGQALP KESNVQPFVK
     PVLTTKAEVP VAESADHLQT QATGDPVLQL LLSQHKAMLE AHQLFLQTAS AGYEQFSHMM
     NGMAASLGSV QEAVKEDRLI AAALTTRETL PEYLATHEVV PDETTIDAHL SSRVREISTE
     VALVPVGLPG PKFSRKQLEV LSSGKISTIF GPLFEQQDKY DIQVRMPEPP LLLCDRVTGI
     QGEPGTLSLG TIWTETDVKA DSWYLHNNRM PPGIFIEAGQ ADLLLISWLG IDFENKGERA
     YRLLGCELTF HGGLPKPGET LQYEIHVDGY AKSGETTLFF FHYNCHVDGK LRISVSGGQA
     GFFSKQELTE SKGVIWNPEE ATYDAFDTTI LANATKKNNF TIDEVIAYTE GDMASCFGTQ
     FDFTQTHSRS PRSQEGYRNF IKTVTDFDLK GGPSKLGYLR SETMVSPDDW FFKGHFKNDE
     CMPGTLMADA CLQMMAFYMV GAGLAVDKDG WRFEPVTDEK YKFVCRGQVT PASVKVTYEL
     FIAGITLDPV PTMHAHVLTT VDGTKAFLCE NLGLQLIPDW PINTLLAELG LSDANLPSAD
     YKGFKLDHLS LLNCALGNPS DAFGEDFNHY TGLIRSPRLP RPPYHFMTRI VSLHALPGGY
     KDKPSVTAEY DISQSVWYFN ENGRATMPYA VLMEVALQPC GWLSTFTCQY DIKGKDLLFR
     NLDGEAIQHR EITPADKTIL THTELSGVSI MGEIIIVKFE VTSTSFGEPV FTMKTVFGFF
     DPESMKTQKG LPQSAQEQEN YHAAANYETS LHSFPAKFFL NSSARLPASK LLMIDRLVRF
     DPIGGQYGKG YIRAQKDVNK NEWFFKAHFF QDPVQPGSLG IEAILQVMQA YLLDQGLHLG
     ITDPVFEPVL IKETTEWHYR GQVTPENELI SADFDVESVI KEENYVILTG YGRLWVDGLK
     IYSAPRIGMK VYAASTPVSR KFLLSPMQRI IYGQYNAPGN EPWIYHTQFS YHLQIKQLDK
     TLFERAVSLV LSRHPLFKTV FFKEDGLVMQ GINADIKPNL FIRDLPGDVT EQVLQIQNQL
     LADRKAPFDV NQTSAALYRV YLLHRNRNEL QFVLTIHHAI WDGWSLAVFM KEILDLYTML
     KTNHAYLPLP ATYSFANYLD KNVLPAKNIT KKGSSPQFKH DSDGQAYLPV QTTLGAKLAI
     AIKKVAKERK VPLKALFLAA FAHLLSDDNG TVIIDVVTNG RDLALTDPLG TFGLLWALMP
     VHLSARENDQ EYLQHVQQQL AAVEKKALIT DYTDSLAVFN YINFEGANIL SDSPDVQFME
     TGGLDRFHHP LHLLVGKSPF TGEFSLVWNY DSRLYKLEEI EQLMQQYVQI LAAYAIP
//
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