PHAS_MYCBP
ID PHAS_MYCBP Reviewed; 2126 AA.
AC A1KQG0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Phthioceranic/hydroxyphthioceranic acid synthase {ECO:0000250|UniProtKB:P9WQE9};
DE EC=2.3.1.287 {ECO:0000250|UniProtKB:P9WQE9};
DE AltName: Full=Polyketide synthase pks2 {ECO:0000250|UniProtKB:P9WQE9};
GN Name=pks2; OrderedLocusNames=BCG_3888c;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7 (S)-methylmalonyl-CoA + 21 H(+) + hexadecanoyl-
CC [(hydroxy)phthioceranic acid synthase] + 14 NADPH = C37-
CC phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 7 CO2 + 7 CoA
CC + 7 H2O + 14 NADP(+); Xref=Rhea:RHEA:58908, Rhea:RHEA-COMP:15244,
CC Rhea:RHEA-COMP:15246, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57327,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78483,
CC ChEBI:CHEBI:142473; EC=2.3.1.287;
CC Evidence={ECO:0000250|UniProtKB:P9WQE9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8 (S)-methylmalonyl-CoA + 24 H(+) + hexadecanoyl-
CC [(hydroxy)phthioceranic acid synthase] + 16 NADPH = C40-
CC phthioceranyl-[(hydroxy)phthioceranic acid synthase] + 8 CO2 + 8 CoA
CC + 8 H2O + 16 NADP(+); Xref=Rhea:RHEA:58904, Rhea:RHEA-COMP:15244,
CC Rhea:RHEA-COMP:15245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57327,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78483,
CC ChEBI:CHEBI:142472; EC=2.3.1.287;
CC Evidence={ECO:0000250|UniProtKB:P9WQE9};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250|UniProtKB:P96202};
CC Note=Binds 1 phosphopantetheine covalently.
CC {ECO:0000250|UniProtKB:P96202};
CC -!- MISCELLANEOUS: In strain BCG, the sulfolipid-1 (SL-1) is not
CC synthesized.
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DR EMBL; AM408590; CAL73878.1; -; Genomic_DNA.
DR RefSeq; WP_011799379.1; NC_008769.1.
DR AlphaFoldDB; A1KQG0; -.
DR SMR; A1KQG0; -.
DR PRIDE; A1KQG0; -.
DR KEGG; mbb:BCG_3888c; -.
DR HOGENOM; CLU_000022_31_5_11; -.
DR OMA; KDVQHYT; -.
DR Proteomes; UP000001472; 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:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 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; IPR013154; ADH_N.
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; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
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; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 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; 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; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 3.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Multifunctional enzyme; NADP;
KW Phosphopantetheine; Phosphoprotein; Transferase.
FT CHAIN 1..2126
FT /note="Phthioceranic/hydroxyphthioceranic acid synthase"
FT /id="PRO_0000329010"
FT DOMAIN 2040..2126
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..449
FT /note="Beta-ketoacyl synthase (KS)"
FT /evidence="ECO:0000250|UniProtKB:A0R1E8"
FT REGION 449..549
FT /note="Linker domain (LD)"
FT /evidence="ECO:0000250|UniProtKB:A0R1E8"
FT REGION 550..849
FT /note="Acyltransferase (AT)"
FT /evidence="ECO:0000250|UniProtKB:A0R1E8"
FT REGION 909..1191
FT /note="Dehydratase (DH)"
FT /evidence="ECO:0000250|UniProtKB:A0R1E8"
FT REGION 1227..1398
FT /note="Pseudo beta-ketoacyl reductase (PsiKR)"
FT /evidence="ECO:0000250|UniProtKB:A0R1E8"
FT REGION 1426..1750
FT /note="Enoylreductase (ER)"
FT /evidence="ECO:0000250|UniProtKB:A0R1E8"
FT REGION 1772..2019
FT /note="Beta-ketoacyl reductase (KR)"
FT /evidence="ECO:0000250|UniProtKB:A0R1E8"
FT ACT_SITE 196
FT /note="Acyl-thioester intermediate; for beta-ketoacyl
FT synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 641
FT /note="Acyl-ester intermediate; for acyltransferase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:A0R1E8"
FT ACT_SITE 947
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000250|UniProtKB:Q03132"
FT ACT_SITE 1115
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000250|UniProtKB:Q03132"
FT BINDING 1780..1783
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q03131"
FT BINDING 1803..1806
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q03131"
FT BINDING 1831..1832
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q03131"
FT BINDING 1904..1905
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q03131"
FT MOD_RES 2075
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2126 AA; 225734 MW; 0BF4B77F968CA3BA CRC64;
MGLGSAASGT GADRGAWTLA EPRVTPVAVI GMACRLPGGI DSPELLWKAL LRGDDLITEV
PPDRWDCDEF YDPQPGVPGR TVCKWGGFLD NPADFDCEFF GIGEREAIAI DPQQRLLLET
SWEAMEHAGL TQQTLAGSAT GVFAGVTHGD YTMVAADAKQ LEEPYGYLGN SFSMASGRVA
YAMRLHGPAI TVDTACSSGL TAVHMACRSL HEGESDVALA GGVALMLEPR KAAAGSALGM
LSPTGRCRAF DVAADGFVSG EGCAVVVLKR LPDALADGDR ILAVIRGTSA NQDGHTVNIA
TPSQPAQVAA YRAALAAGGV DAATVGMVEA HGPGTPIGDP IEYASVSEVY GVDGPCALAS
VKTNFGHTQS TAGVLGLIKV VLALKHGVVP RNLHFTRLPD EIAGITTNLF VPEVTTPWPT
NGRQVPRRAA VSSYGFSGTN VHAVVEQAPQ TEAQPHAAST PPTGTPALFT LSASSADALR
QTAQRLTDWI QQHADSLVLS DLAYTLARRR THRSVRTAVI ASSVDELIAG LGEVADGDTV
YQPAVGQDDR GPVWLFSGQG SQWAAMGADL LTNESVFAAT VAELEPLIAA ESGFSVTEAM
TAPETVTGID RVQPTIFAMQ VALAATMAAY GVRPGAVIGH SMGESAAAVV AGVLSAEDGV
RVICRRSKLM ATIAGSAAMA SVELPALAVQ SELTALGIDD VVVAVVTAPQ STVIAGGTES
VRKLVDIWER RDVLARAVAV DVASHSPQVD PILDELIAAL ADLNPKAPEI PYYSATLFDP
REAPACDARY WADNLRHTVR FSAAVRSALD DGYRVFAELS PHPLLTHAGD QIAGSVGMPV
AALAGMRREQ PLPLGLRRLL TDLHNAGAAV DFSVLCPQGR LVDAPLPAWS HRFLFYDREG
VDNRSPGGST VAVHPLLGAH VRLPEEPERH AWQADVGTAT LPWLGDHRIH NVAALPGAAY
CEMALSAARA VLGEQSEVRD MRFEAMLLLD DQTPVSTVAT VTSPGVVDFA VEALQEGVGH
HLRRASAVLQ QVSGECEPPA YDMASLLEAH PCRVDGEDLR RQFDKHGVQY GPAFTGLAVA
YVAEDATATM LAEVALPGSI RSQQGLYAIH PALLDACFQS VGAHPDSQSV GSGLLVPLGV
RRVRAYAPVR TARYCYTRVT KVELVGVEAD IDVLDAHGTV LLAVCGLRIG TGVSERDKHN
RVLNERLLTI EWHQRELPEM DPSGAGKWLL ISDCAASDVT ATRLADAFRE HSAACTTMRW
PLHDDQLAAA DQLRDQVGSD EFSGVVVLTG SNTGTPHQGS ADRGAEYVRR LVGIARELSD
LPGAVPRMYV VTRGAQRVLA DDCVNLEQGG LRGLLRTIGA EHPHLRATQI DVDEQTGVEQ
LARQLLATSE EDETAWRDNE WYVARLCPTP LRPQERRTIV ADHQQSGMRL QIRTPGDMQT
IELAAFHRVP PGPGQIEVAV RASSVNFADV LIAFGRYPSF EGHLPQLGTD FAGVVTAVGP
GVTDHKVGDH VGGMSPNGCW GTFVTCDARL AATLPPGLGD AQAAAVTTAH ATAWYGLHEL
ARIRAGDTVL IHSGTGGVGQ AAIAIARAAG AEIFATAGTP QRRELLRNMG IEHVYDSRSI
EFAEQIRRDT NGRGVDVVLN SVTGAAQLAG LKLLAFRGRF VEIGKRDIYG DTKLGLFPFR
RNLSFYAVDL GLLSATHPEE LRDLLGTVYR LTAAGELPMP QSTHYPLVEA ATAIRVMGNA
EHTGKLVLHI PQTGKSLVTL PPEQAQVFRP DGSYIITGGL GGLGLFLAEK MAAAGCGRIV
LNSRTQPTQK MRETIEAIAA MGSEVVVECG DIAQPGTAER LVATAVATGL PVRGVLHAAA
VVEDATLANI TDELLARDWA PKVHGAWELH EATSGQPLDW FCLFSSAAAL TGSPGQSAYS
AANSWLDAFA HWRQAQGLPA TAIAWGAWSD IGQLGWWSAS PARASALEES NYTAITPDEG
AYAFEALLRH NRVYTGYAPV IGAPWLVAFA ERSRFFEVFS SSNGSGTSKF RVELNELPRD
EWPARLRQLV AEQVSLILRR TVDPDRPLPE YGLDSLGALE LRTRIETETG IRLAPKNVSA
TVRGLADHLY EQLAPDDAPA AALSSQ
