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Database: UniProt
Entry: A0A1H6Z6Y1_9ACTN
LinkDB: A0A1H6Z6Y1_9ACTN
Original site: A0A1H6Z6Y1_9ACTN 
ID   A0A1H6Z6Y1_9ACTN        Unreviewed;      3986 AA.
AC   A0A1H6Z6Y1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:SEJ45392.1};
GN   ORFNames=SAMN05443287_104486 {ECO:0000313|EMBL:SEJ45392.1};
OS   Micromonospora phaseoli.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1144548 {ECO:0000313|EMBL:SEJ45392.1, ECO:0000313|Proteomes:UP000198707};
RN   [1] {ECO:0000313|Proteomes:UP000198707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7038 {ECO:0000313|Proteomes:UP000198707};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC       family. {ECO:0000256|ARBA:ARBA00029443}.
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DR   EMBL; FNYV01000004; SEJ45392.1; -; Genomic_DNA.
DR   STRING; 1144548.SAMN05443287_104486; -.
DR   OrthoDB; 5478077at2; -.
DR   Proteomes; UP000198707; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.30.70.3290; -; 2.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
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; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
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   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 2.
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; 3.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 3.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 3.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 3.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   3: Inferred from homology;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          585..662
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          678..1089
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1941..2019
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          3017..3092
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          550..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1477..1497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1613..1635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1652..1677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1902..1944
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2604..2631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2990..3020
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3095..3134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3331..3359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3501..3520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3584..3604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1906..1925
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3004..3019
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3333..3352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3986 AA;  417046 MW;  6B849515B73A6C01 CRC64;
     MQTATGSGGQ RTLLDVLLDA ADRRPDQVVV HLREDGTERT VTVRELRDES LRVAGGCHAA
     GIAPGTPAIL LADAGDDFQP MFWGTLAAGL IPVPLPPEPS RVRAVRDLLT DAVVVTDDAT
     ATTVDGLPGP VLRLAALRAG TPPDELPRRT PDDVAFLQFS SGSTGAPRGV ELTHANVLSN
     VEQARLASGA RPDDVLVTWM PFFHDMGLIG THLTPLAIGC KQIRIPPLAF AKRPALWFTA
     AHRHRATLLS AANFALAMAV RRVPADTLAA LDLSRVRCLV VGAEPISAAV WRAFLDHTRA
     AGLDPAAPRP VYGLAEATLA VTFPPAGEVA APLVLDRAAL SLGRAVPTQP GGHAVELMDL
     GHPVHGCEIR VVDDRHRPVV ENRVGLIEVR GPNVARGYHR APQASRETFV DGWLRTGDLG
     FLRAGRLCVT GRAKDVVFVN GRTFHAPDLE AVAAATPGLP TGVTAVVGCT DPDSGGERIV
     VFVAWARPPA GAAGVLDATR ARVAEAAGHH DVRVLPLPPG AFARTTSGKL RRRRMRDRYL
     AGDFADREHR WHPPAPVTVP APASTAAEPP ATTPAGPPTG DPWRLPRREV ERIVRTVWAG
     VLDRPADTIG LDDRFLAIGG SSLKAMEVLA GLEDALSTTF APADLRDCPT VATLTDRILA
     GPGVAPTRPA AAPTGGYAAP MAVIGMACRF PGADDPDQFW RRLVDGVDEV RPVPAHRWTP
     QGDHPRWGSF LDDPMLFDAE FFGLTESEAR LTDPHARLFL EIGYEALERA GYAGPRRQGR
     RIGVFAAVGD SAYPELLAAD GPVAAPAALV GNLRNLVAAR LAQTLDLTGP AIAVDTACSS
     ALVALHLAAR SLAAGECDIA VVGGVNLNLT ETAYRLLDAA EALSPTGRCR AFDADADGFV
     PGEGGAALVL CRPADAHAAA DPVLALVTGT AVGNDGRSLS LLAPNPHRQW EVIARAYADA
     GIDPAAVSYI EAHGTGTGIG DPVEARSLAA AFPPRPDGTP RWLGSVKTNL GHLLNTAGMP
     ALLKVVLALR HRQLPPSLHH VRPSTRYDLD ATGFAVVTAT RPWSAPGPLV AGVNAFGFGG
     TNAHAVLSEA PRRPPTPAPA DGHVGGQLVT LTAHSAPALR RSARDLAQHL RAHPELAAAD
     VAASASTARD DAPYRLALVA TADLADRLEE AADTLADAPV RRRPRTVFVF PGDGTPVPAP
     VVRDLHARLP VFRGLLTDAC AAAGPLAGRP LLSWCLAEDT PADRDRPDRQ VTATVGVVVA
     LALAGQLTAW GVRPDAVLGH GVGELAAAAA SGTLSVAEAV RRTVALTGTE PGGPADETVR
     VEMRAALRRL LDDGYDTVVE LGPAGDAARS FDGRAAGPVR VVTLLDAPAH PADAGATSLL
     TAVGGLWSRG GPLDRLALHV GRRRVPVPTY PFERRAYPPP AAAEAAVPLY LPAWREVPPV
     AGDRPPTVRL RGPGVDGRFA AALTTALTAD GIEVHTGEPE TAVPPTGRGS ITARPGDGAS
     TAEVTVLLAG AAVDPPDATA LDAAVADQVR AVRALLDEGL DHPGRLLVVT EDVHVTGSAA
     ERPRPVQAVL AGLTTALADE RPGLLVRPVD LSSLDGEAAR VDAVRREVRG FVDSGTSDTG
     RRAGATGPQG APPGPVAAIG VAWRNGRRLA RFLDPAPTST DPTSDGPGMT GDARRPGAGG
     VHLIVGGAGG VGAALARTLA RADRPTLLLA GRSDRAPAEL LTELTELGAA VTYHRCDVTV
     AADVDALLAG APRLDTVFHA AGTVRVGTLR VKSTRDVLAV LAPKVRGSYL LTEALRRHRH
     DRAALVGFSS VSAVLPGLAG AIGDYAAANA FLDAFAAAHR AAGRRVQAVG FAAITDIGMA
     ARTGGTGTGA LPVRDALRAL ALARRLDAAH LVVADLRRRA DPHAPASTAP TSTAPTSTTP
     ASTAVAGRTA GRPRPDAAHD GPNRDEVARL LRRLLAEPLH RRPDEIADDA SFLALGLDSL
     AAVDLVKRLE EEIGRDLPVT LFFEYTTVAE LAAHLTATTD AASPPAACTV EQPAPVHEPG
     PRPSAHGEPF PLTAVQRAFH VNERLHPTVA SYAFVQQTIT GTIDATLLGR ALAHLETQHP
     MLRVRFVPGT GAGTPRQVIL PPTEQPAPAW YAVQPLTGPL GALAERLCNT PVDLTRQPPL
     RAVLVRETPD RAHLLLVQHH AAGDGFSLNL LSEELWSGYT ALCHGRTPPP SPAPGFDAYA
     RAVTPPTAQD LSYWQDRLSG DGWTLPLPYD GDRAAPPAPP YLTHQGDLDA DLVAALRDRA
     AAAGVSLFHL LLAGYVRCLS RWSGQQSVPV TVARAGRDAR LPAIGRIVGP FADTLPLRID
     TDPDEPTGQL ADRLRVAWSA AQRHGSVTSL DLARLLDRPG AGPRTASPAG FSFARFPVTR
     DPDCPVTVTP TAAGSASAAT RLSLLCWESG AGLGLSWNFP LRLFTRATVA RLAAEHRQEL
     VALAAGRRQP AQPGAAAGGD VTARIRAVCR RTPDAVAVDT GDGSLTYRAL DLAADRVAGL
     LTRQGVRPGD RVGLLTAPGP QTVVGVVGIL RAGAAWVPLD AAHPPARLTD HLVRAGAELL
     LHDDECAATA AGLVHAARPI RLAPPTSDSA ADATTDSGTG PQAPPPAPEH PAYVIFTSGS
     TGRPKGVPVT HRSMSTYLDW AIASFGYRPT DRLAQTSSSC FDASVRQILA PLLVGATVVT
     FTRSLLRDPQ ALLSRIERDR ITVWSSVPTL WERILHAAEE HVARHGVAPD LTALRWVHVG
     GEELSPVPVR RWFDLFGDDC RITNLYGPTE ATINATWHLI DRRPDDAVRR LPIGRPVGAA
     VVHVVDPAGR TCPPGVAGEL YLGGVGLTAG YLGEPELTDA AFVVREGQRF YRSGDRGRVA
     ADGTLEFLGR LDDQVKIHGY RVEPGEIEAV LRTHPAVAAA AVLHQADPHP RLHAFVLPTS
     QSTPTVADLR AHLAARLPEH MVPARLQLLD SLPLTATGKI DRARLLAHTG TRPATAREHA
     ATTTGPHPAT TTGPVTGPVS GTEASLARIW ADLLDVPAVG PDDDFFALGG DSILILEVFA
     QLRERFPTAL RPTAIYEHRT LAALAAAIDT AADPASGSAG PAAGLSPAPA TPGPSFCAPA
     AGQPAPDTSP AGPFPVTATQ RGFLLADAVV PGAGTAWLAR LRLHGRLRRD IFQRAVDLLV
     ARHPMLRTVF PAGARPPVQQ ELPVSMRLPV EYETLAQHSD VAARVAEERR RRFEPWAWPL
     LRLRLLTVTP DEHVLLVHAH HLIGDGYSAA LLGHELLAAY HRQADGSPDP LPPLRTSFRD
     YVTLLERRST AAPDPAARAW WARRFGPPYR PPVRRADTDR SPDADRPEAD GAPGQRTRSA
     PVRGFTLDLT VVAGLRRLAA EAASTLYAPV LTAYHRALAR LTSQDDLVVG LAVTGRDHPL
     PDLHRVFGPC AAMLPLRLTG TAAFPTHLAH VAAEVAAARQ HADPPSIAAA VPTGRPDGAP
     TGAQFFFSFL DFDALDPVLA LGSADDPPPA APSGHTGSAA PTRLRLTWDE ETELAPPPIG
     TDLFLTARPG PDGLRVTLRG SPTAVSPTDL DRLVDWLRTD LTTAAAEQSR RGTPERPDPN
     LATAPAVVPS TRLTAAIVGY LPPPAQLAAI AGLPAGSLPR EQLRELLFPA GRPRLLEELT
     TPLGTSGFVC LPRFSDELTA AGETLAAETA AAVDLAATLG AACVSLAGLI PAHTGYGIGV
     LRRTRTATAI TTGHAATVVS VVLTVEAALA ASGRHLAGST LAVVGLGSIG FSSLRLLLAR
     APRPPARLVL CDIPSAAPRL RDQANRLRSD GFAGTVEICA TTSTVPDPGY AADLIIGATS
     AATEPLDVDR LRPGTIVVDD SFPHALNPVR ALARMRHDRD VLVVGGGLLH VAETTRTVPA
     DLPPAAIAGH AAGFGLPGAV ASCQLESLLR AASPTLPVVH GLVDDSTAAT YAQALTEAGI
     GAAPLHLLHQ LVDADLPAAL PAGPPA
//
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