ID C5B1M9_METEA Unreviewed; 2468 AA.
AC C5B1M9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Fatty acid synthase multidomain protein (RkpA-like wcbR-like) {ECO:0000313|EMBL:ACS39663.1};
GN OrderedLocusNames=MexAM1_META1p1821 {ECO:0000313|EMBL:ACS39663.1};
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630 {ECO:0000313|EMBL:ACS39663.1, ECO:0000313|Proteomes:UP000009081};
RN [1] {ECO:0000313|EMBL:ACS39663.1, ECO:0000313|Proteomes:UP000009081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
RC {ECO:0000313|Proteomes:UP000009081};
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
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DR EMBL; CP001510; ACS39663.1; -; Genomic_DNA.
DR RefSeq; WP_012752635.1; NC_012808.1.
DR STRING; 272630.MexAM1_META1p1821; -.
DR KEGG; mea:Mex_1p1821; -.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_31_5_5; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000009081; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd05195; enoyl_red; 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; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; PF00107; ADH_zinc_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 SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 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; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000009081};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..426
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2345..2422
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2468 AA; 261020 MW; 76CBCD3CDA5305E9 CRC64;
MTHRKDIAIV GRACRLPGAQ NVEGLWQLLT EGRCAVSRIP EDRWSLQAFG HPRAQERGKS
YTWAAGVLDD IWSFDPGVFG ISPREAEQMD PQQRMLLELT WEAFEDAGLR PSAVAGSHIG
VFVGASALDY GNLRILDPSS GDAYAATGNT LSIISNRISY IYDLKGPSFT LDTACSSSLV
ALNAAIAAIE AGQVDTAVVA GANILASPFN FISFSNAQML SRTGLCQAFS SSADGYVRAE
GGVVLILQSA EAAARSGRAV RGVIAASGVN SDGRTTGISL PSGHAQGALL EQVYRDAEID
LDKLAFVEAH GTGTPVGDPI EAGAIGSKLG KPRQTPLPIG SIKTNIGHTE PTSGLAGLLK
ASLALEHDLL PPSLHAAELN PDIPFEAMKL AVNRAPLALA RTKAERFAGV NSFGFGGTNA
HVVLTDAGPV AAANDAGPAP EILLLSAQSR AALNDLALDY AARFDGAAPA EAARVTAAAF
HRRERLATRL ALPLTPETDV PAALRALAEG EESDAAIVGT AVERQAEVAF VYSGNGSQWV
GMGREAYEES KAFRARFDQT DKLFEKLSGW SLKEAMFAED LDARLSLTRV SQPLIFAIQS
ASTAALRAKG LAPRYVLGHS VGEIAAAEAA GILSLEQAVR VIFYRSKHQE STRGFGTMAV
LLGPAEEMEA FLADYPTLDI AAYNSPKAIT VAGPEADIEA AMKALARKRR RGRKLDLEYP
FHGRLMDPTE RPLLRDLDGL KASAGHTAMV STVTGTVLPG AQFGAGYWWR NIREPVRFCE
ALQEATRQGA RVFVEVGPRA TLLPHIGDAI EPLAIEVASV GVMHRKPIGG DPIAKAVAAA
LVAGAAVDEA RLFGADPAGI IALPLYPWQR RPFRLAETTE GAGAAPRPYH PLAGARLAPD
GLEWHGHLDA ALVPELDDHR IDGQVILPGA AFVEMALHVA RQALRTESVT ISDVEILSPM
VFAEDSLREV LVRLSGSGNQ IQILSRPRLT PTPWQLHASA KIIEGDFPVP ARRDLAVPAE
HAISGDGLYR RALASGLGFG ENFRQVAASA RIDETTIVSE LIPAESDDRY GLVPARLDSC
FHGLILLFAE LMGEGATKAY VPVRFGEVRL LRPGAAIARA EIRTRRCNER SILADFTLTD
AEGEVVATIR EGRFQALRAR SGSDLDAYAI TQGVERATEP TALPLERRPS VAERLRPSLA
AATAPDTADL GPGHLLLEGW ATALAYRLAD GLSEKGKVTL DRRLPAALHP WATNALYALE
SSGLATLEKG VWRLRRDVSL PAPEETMRWI AADHPELAAE LVLLADTTAL VGRIVAGDAP
ASASLPPAAL DAFHLRGATA RAAADVVARI VAEARGRMPS DRALRILQVG FGPLSARAAA
LAREADARLT VLDTDRRLAE RARLALPSTV EVIEDIDALP PAAFDLVLAS DVLHRADKAL
PGQLAAALAS GGLLVAVEPG ASLFRDLVFG LAPDWFEEAV AGMPLSRLDD VTGWQRRLSA
SGLVRVSADR AASANGDDLL LVAEAPVRSA VGHGQSFAFV VGSHDEFGAE TASSLATLLV
ASGVHVSIIL DSEQSLRELE RETPDTVVFL AGAFAGEGAA ATRLRDRCLS LKRCAEFLGS
RQTRLWVVAP GATRDAGGEA AAVEAGVWAF SRTLANETAT LDVRRIDLAP TLSSKDAAER
LRALILSGTD ETEIVLDADA TRVVRFHPGR AATTAGEAAP AARLERSNTG GLNEMVWGPA
ERAAPGPGEV EIAVAATGLN FRDVLWALSM LPEEILEDGF AGPRLGLEVS GQVTAIGQGV
VDFAVGDAVV AFAQSGFATH VVVPEMVVAP MPAGLDPAAA ATVPVAFLTA YYALCTCARL
RKGEWLLVHG GAGGVGLAAL QIAKWKGARV IATAGSREKR ALVAALGAEH VLDSRSLAFV
DDVRRITGDG VDVVLNSLFG EMMERSLNCL RPFGRFVELG KRDYVANTHI GLRPFRRNLS
YFGVDLDQVL QHQGEDGARM FREVMALFVE GGLRPLPYQP FAADETSDAF RLMQQSGHVG
KIVVTPPVPG SVARVQRNAF TVSAEGVHLV TGGLGGFGIE AARWLADRGA KRIVLVGRSG
KPNEEGRAVV AELAAQGVRV ETKACNITSR RAVEALIEGI EARGEKLAGV IHGAMVLQDG
LISAIEPETL EAVIAPKVIG AGHLDAATRG RKLDYFVLFS SATTFIGNPG QGSYVAANGF
MEGVARQRRR LGLPALAVAW GAIGDVGVLA RNKAVMETLA SRVGVTPMDA RLCLDLMAEA
LESQGKTSDE GVIAIAAMHW GKARERLATL RSPSYASLGG DQQAESGTVA AINIGALLRS
QDIDTVRKTV SDAIVEDIAR ILRLPKDDIS RVRQLSEIGL DSLMGVELGA SLQERFALDA
PPAGISSGLT VNELTETLIQ AVATPVDEAA GVTLSLATKH VGDLDAATLM PFNELVEKNV
SDIKEILP
//
