UniProt: H2JGN2

Database: UniProt
Entry: H2JGN2_9CLOT

LinkDB:  H2JGN2_9CLOT 
Original site:  H2JGN2_9CLOT

All links

Ontology (5)   
   GO (5)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (44)   
   InterPro (25)   
   Pfam (11)   
   PROSITE (4)   
   SMART (4)   
Literature (1)   
   PubMed (1)   
All databases (53)   

Download RDF

ID   H2JGN2_9CLOT            Unreviewed;      2796 AA.
AC   H2JGN2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Amino acid adenylation enzyme/thioester reductase family protein {ECO:0000313|EMBL:AEY66795.1};
GN   ORFNames=Clo1100_2632 {ECO:0000313|EMBL:AEY66795.1};
OS   Clostridium sp. BNL1100.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=755731 {ECO:0000313|EMBL:AEY66795.1, ECO:0000313|Proteomes:UP000007324};
RN   [1] {ECO:0000313|EMBL:AEY66795.1, ECO:0000313|Proteomes:UP000007324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BNL1100 {ECO:0000313|EMBL:AEY66795.1,
RC   ECO:0000313|Proteomes:UP000007324};
RX   PubMed=23209234; DOI=10.1128/JB.01908-12;
RA   Li L.L., Taghavi S., Izquierdo J.A., van der Lelie D.;
RT   "Complete Genome Sequence of Clostridium sp. Strain BNL1100, a Cellulolytic
RT   Mesophile Isolated from Corn Stover.";
RL   J. Bacteriol. 194:6982-6983(2012).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004789}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC       family. {ECO:0000256|ARBA:ARBA00029443}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003259; AEY66795.1; -; Genomic_DNA.
DR   RefSeq; WP_014314156.1; NC_016791.1.
DR   STRING; 755731.Clo1100_2632; -.
DR   KEGG; clb:Clo1100_2632; -.
DR   PATRIC; fig|755731.4.peg.2621; -.
DR   eggNOG; COG1020; Bacteria.
DR   eggNOG; COG3321; Bacteria.
DR   HOGENOM; CLU_000022_35_4_9; -.
DR   OrthoDB; 9765680at2; -.
DR   Proteomes; UP000007324; Chromosome.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; 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   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd08953; KR_2_SDR_x; 1.
DR   CDD; cd19531; LCL_NRPS-like; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 1.10.1240.100; -; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
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; 1.
DR   Gene3D; 1.10.287.490; Helix hairpin bin; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
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; IPR049490; C883_1060-like_KR_N.
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; 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; IPR013968; PKS_KR.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 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; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF21394; Beta-ketacyl_N; 1.
DR   Pfam; PF00668; Condensation; 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; 2.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..432
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1449..1524
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          2474..2549
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2796 AA;  315818 MW;  EA64AC91CBA4F426 CRC64;
     MEEINNKNGL EVAVIGLAGR FPGANNINEF WSNLKNGIES ISFFSDSELI ENGVDINCLN
     DPEYVKAKGM VSNAEYFDPY FFGYTPSEAE VMDPQIRVFF ECVWEALENA GYDPFSYKKP
     IGLYAGAFDN ESWRQKVSLF GNSDVDMLTK TLLSSRDCLS TLISYKLNLK GPSITVQTAC
     STSLVAIHLA CQSLLNGECS IALAGGVSIM LPQITGYKYE DGMMLSPDGH CRTFDEKSKG
     TVMSNGAGVV VLKTLEDAIN DGDHIYAVVK GSAINNDGNR KVGFTAPSVL GQAEVIRDSL
     MMAEVEEESI SYIETHGTGT PVGDPIEIEA LKLAFNTDMK QYCALGSLKT NVGHLDAASG
     VAGFIKTVLS LKNREIPPNL HYKNPNPSID FDNSPFFVNT HLNKWENKKY PLRAGVSSFG
     IGGTNAHIIL EEAPTLDESV SNNSWYMIPL SAKTQNALDK LSKNFAYYLE QNPDISLPDL
     AYTMQIGRAQ FKYRRAVVFQ NVKGAISELN KTYTAEIAKV DQNTVVFMFP GQGYQYVNIG
     LELYQSDPYF RKEMDHCFDI LKPMLHFDIK NILFPMDNIN NISITDTLVA QPLNFILEYS
     LAKSLINWGV KPDALIGHSM GEYVAACLAE VFTLEDALGL IVLRGKLMQE QPAGIMLSVM
     ISEEELRPLL TEELSLAAVN SSSVCVVSGS QQAIDTLEKH LNEIGHQGIR LPVSHAFHSS
     AMKSMIQTFL NKLERIELNK PKIPYISNVT GTWITAKEAT TPEYWAEHIL GTVRFADGIT
     ELLKKNNPVF IEVGAGWTLN TSVSLHEDYT PQIPVVNLLR HFREDAEKQS PRNQIMNLFN
     SIQEAPSDMA FLLNQLGMLW CAGIKIDWNQ FYKNEKRRRI PLPTYPFERK RYWIDMDYNK
     SLETLAQTYK KKDIKNWFSI PSWERTDLPY SDISVDAGKS ILVFTNTLEF SSKLIESMEF
     SNYNLTFVRM GAEFYKETRC SYFINPGKDK DYKSLFNDLN KSKFTPDVIL YLWTLTDDNS
     CKLDKSKVKT AVDIGLYGII YIAQAIGELN FLEKVSIKVV TNNMHIVTGE ESINPEKSVV
     IGSIKTIPRE YHNIKCTGID IDLPQTDKIK ERQLINCLLS ELAASPDDSL VAYRGKYRWV
     QNFKQIQLKE CHGIPSRLRE NGVYMITGGL GGIGLAISEY LAKTVRAKLV LIGRSEIPPS
     EKWDDYINSS EKDCKLSDKI MKIKGLQESG AEVLLINADV ADAEQMSRAM SIIHERFGEV
     NGIIHGAGLP DGGMIQLRNR ATTDCVIAPK IYGTLEINKF IENNKLDFLI LCSSLNSIIA
     PYGQIGYSSA NSFLDAFSQY QSNQTGIYSV SINWDSWKEV GMAVDSVNTG NSLVSLETGM
     LTSEGIEVLK RILDSNLPDY ILSQLIVSTY SLELYLKGMP ELENKESMFY GGENQNCGEE
     LNRNIQHAIS KDEIELILVK IFQKLLGIEE IDKYDDFFEL GGDSLKATVL MTKIYNELSA
     KISLKEIFNL RNIESISDFI ASGEKHTYEK IKKVEEKEYY EASSAQKRMY ILQQVEKDST
     AYNMPSALFI EGELEIGRVE RALKKLIERH ETLRTSFETI DKIIIQRVHN IDTIDFSIKK
     ISVNSEIEVK EKINSFLEPF ELGKAPLLRV GVIELSETRH ILLFDMHHII SDGVSMDILT
     GEFAALYEGR GLPDLKIQYK DYSAWQNRMK ADDRMQKQEE YWLKVFQGEI PVLNLPEDFP
     RPRVQSFEGD SITFDIVPEV AKGLEKLAGD TGATLYMVLL AAYNVLLSKY TGQEDIIVGT
     PIAGRPHTDL ENLIGMFVNT LAMRNYPESS KTFKEFVEEV RENALRAYEN QNFQFEELVE
     KLDIRRDISR NPLFDTMFTL QSAGATLEKE TGLRLKPYET VDKTAKFDLS LLAAFSGDKI
     SFLINYCTKL FKKETVERIV GHFQNLLHEI VKNPEKKLQE LDMMSDKEKE SILYGFNNTK
     VEYPRDKTIH ELFEEQVWKT PENIAVVHRE EKISYRELDR RAEAVSQNIM EKGIDCDEVV
     GILLNPSIDM FAAILGVLKA GAAYLPIDVD YPKQRIEYML KDSCAKLLIS TEKISSGIEF
     GDEILEIRDT QASAERRAVG KTNSKPEHMA YVIYTSGSTG MPKGVMVEHR ALVNLCSWHI
     ERYEVTSRDR ATKYAGTGFD ASVWEIFPYL IQGAAIHVID EEIRLNVNKV NEYYEKNGIS
     ISFLPTQICE KFIQLENRSL RCLLTGGDKL KYFNKQRYKI VNNYGPTENT VVTTCYMVKE
     SSANIPIGKP ISNTKVYILN GNKAQPVGVA GELCISGESL ARGYINHEEL TQEKFTENPF
     VPGERMYRTG DLARWLPDGN IEFLGRIDDQ VKIRGYRIEL AEIENVLRKL DKIDDAAIVV
     SEDKSGDKCI YAYIVSKYEI MPDKVREILS VKLPLYMIPT YIMQIDSIPI TENGKIDKKK
     LPEIELSVKT KYVAPENEIQ EKLCRVVCEV LGLERVGIND DLFELGANSL SIMSFLSMVH
     SEFGIELAFR DVFKDPTVRG CSDIVSTSQD VSKNYLNDCI QLSSNKQGGK TVFCLPSLGA
     VGILYMQLAE ELGSNCLYSF NFIEDENLIE EYVKVIIKVQ SEGPYILLGY SAGGNLAFEV
     AKELERQGYE VSKIIMIDSY YRSEITNLTE EEREKMINEL IDSYFKHNRT QDEIIKRHND
     KRTLTDYVGK KIIAYSRYLD SLITLGQVDA NIILIKSLEE GNVKVSPRER NLWSNSTSKR
     FKSIQGFGAH IEMLSPEFIK QNSEIIERIL NEDGSL
//

DBGET integrated database retrieval system