ID B2HQ46_MYCMM Unreviewed; 2090 AA.
AC B2HQ46;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Probable polyketide synthase Pks5 {ECO:0000313|EMBL:ACC40789.1};
GN Name=pks5 {ECO:0000313|EMBL:ACC40789.1};
GN OrderedLocusNames=MMAR_2340 {ECO:0000313|EMBL:ACC40789.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC40789.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC40789.1, ECO:0000313|Proteomes:UP000001190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
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DR EMBL; CP000854; ACC40789.1; -; Genomic_DNA.
DR RefSeq; WP_012394090.1; NC_010612.1.
DR STRING; 216594.MMAR_2340; -.
DR KEGG; mmi:MMAR_2340; -.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_31_5_11; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000001190; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 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; 3.90.180.10; 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 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-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR016039; Thiolase-like.
DR NCBIfam; NF041183; Pks2_ls1_myc; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
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; 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; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 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:UP000001190};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..423
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2008..2088
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2090 AA; 222584 MW; 8BC1CFE9911C920C CRC64;
MTPVAVIGMA CRLPGGIGSP EELWEALLRG DDLVTEIPAD RWDADEYYDP EPGVPGRTVC
KWGAFLDNVG DFDPEFFGIT EKEAIAIDPQ HRMLLETAWE AMEHGGLTPE QMAESLTGVF
VGLNHGDYQF VHVDANTFDG PYGNTGTNSC FASGRISYAM RLHGPAVTVD TACSSSLYAT
HLACNSLSEG ESDLAFAAGV YVMLEPRRFA SGSAQNMLSP TGHCHAFDVD ADGFVSGEGS
VVLLLKRLAD AQRDGDRILA VMRGTAANQD GHTVNIATPS VEAQSAVYRA ALATAGVDGA
SVGLVEAHGT GTPVGDPIEF ESLARVYGID RPCALTSAKP NFGHMQAGAG VLGLMKAILA
LQHGVIPPNI HFSRLPDEMA QIKSGLFVPQ EITQWPTNGE QTRTAAVSSY GISGTNVHAI
LEQAPETATH DAEPVSPAIE GALIFPLSAT SADGLRQTAK RLADWVDAQG PELATSDLAY
TLARRRGHRP VRTAVLADNV SELSAGLHEI ADDETPYQAA VGRDDRGPVW VFSGQGSQWK
AMGADLLANE PVFAATVAEL EPLIAAESGF SVTEAMTAIE TVTGIDRVQP TIFTMQVALA
ATMKSYGVRP GAIIGHSLGE SAAAVAAGAL SLEDGAKVIC RRSRLMTRIS GSGAMASVEL
PAQQVLSELM ARGINDVVVA VVASPQSTVI GGATDTVREL VAAWEQREVM AREVAVDVAS
HSPQVDPILD DLYDVLADLE PLTPEVPYYS ATLFDPREEP YCDGSYWVDN LRHTVRFGAA
VQAALEDGYR VFAELAPHPL LTRAVEKTAE GLDMPVAALA GMRREQPLPH GLRGLLADLH
SAGAAVDFSV LYPAGELVDA PLPAWTHQSL LLNRAGQDHQ AQGGSSVVVH PLLGSHVLLP
EEPERHVWQS DVGTEALPWL ADHQIHSAPA LPGAAYCEMA LVAARTILGD AAEVRDVRFE
QMLLLDDETP LSAVGSVKSP GIVDFVVETF QDGGAVRRGG AVLHAVEDDD QLPAYDIPAL
LAEHSRTEDG EELRARFDEH GVQYGPAFTG LGNAHIADGA VSSVVAEVAL PGAMRSQQRA
YAIHPALLDA CFQAVGAHPD VQVAGNGGLM LPLGVRQIRA YASTRNAHYC YARVTSVDTS
AVEADLDVLD EHGTVLVAVR GLQLGTGVSE EGNRDRVLNE RLLTIEWQQR ELPEVDAAEA
GAWLLISTSD GADMLAAELT DALKLHSAQC ATTSWHENAA DHAASAERLR NQLNAGGFHN
AVILLKPDSG DRDENSGVEG VECVRHVVRV VRELPEIMGE APRLFVVTRG AQTVLGGESA
NLEQAGLRGL LRVIGAEYPH LHTTHVDVDE HSGSEVVARQ LLSGSEEDET AWRCGQWYTA
RLSPMPLRPE ERKTTVVEHD TEGMRLQIRT PGDLQTMEFV AFDRVAPGPG QIEVAVSTSS
INFADVLVSF GRYNSPDGQM PQLGTDFAGV VTAVGPDVTD HQVGDRVGGM SPHGCWATFV
TCDGALATPI PAGLTDAQAA AVTTAHATAW YGLHDLGRIR AGDKVLIHSG TGGVGQAAIA
IARAAGAEIY ATAGSPKRRQ VLRDMGIEHV YDSRSIEFAE AIRADTDGYG VDIVLNSLTG
AAQRAGLELL AWGGRFVEIG KRDIYGDTKM GLFPFRRNLS FYGVDLGMLS ITHPRLIREL
LTTVYQHTAE GVLPMPQDTH YPLAEAATAI RVMGAADHTG KLLLDIPRSG RSAVVLPPEQ
VPVLRADGSY IITGGLGGLG LFLAEKMATA GAGRIVLSSR SAPSQKALET IELIRSIGSD
VVVECGDIAQ PATAARLVAN ATATNLPLRG VLHAAAVVED ATLANITDEL LDRDWAPKVY
GAWHLHQATT DQPLDWFCSF SSAAAMLGSP GQGAYAAANS WLDAFTHWRH NQNQPATAIA
WGPWAEIGRA IALAESSDAA IAPDEGAYAF QTLLRHNRTY TGYAPIIGAP WVTAFAERSK
FAEAFKALEQ GRSGSSKFRS ELDALPLDEW PGQLRRMVAE QVSLILRRTI DPDRQLSEYG
LDSLGNLELR TRVQSETGIR ISSTDITTVR GLADHLFAQL APEEAAASSQ
//
