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Database: UniProt
Entry: C5CUE5_VARPS
LinkDB: C5CUE5_VARPS
Original site: C5CUE5_VARPS 
ID   C5CUE5_VARPS            Unreviewed;      1358 AA.
AC   C5CUE5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:ACS20358.1};
GN   OrderedLocusNames=Vapar_3742 {ECO:0000313|EMBL:ACS20358.1};
OS   Variovorax paradoxus (strain S110).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=543728 {ECO:0000313|EMBL:ACS20358.1};
RN   [1] {ECO:0000313|EMBL:ACS20358.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S110 {ECO:0000313|EMBL:ACS20358.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Orwin P.,
RA   Leadbetter J.R., Spain J.C., Han J.I.;
RT   "Complete sequence of chromosome 1 of Variovorax paradoxus S110.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR   EMBL; CP001635; ACS20358.1; -; Genomic_DNA.
DR   STRING; 543728.Vapar_3742; -.
DR   KEGG; vap:Vapar_3742; -.
DR   eggNOG; COG1020; Bacteria.
DR   eggNOG; COG3319; Bacteria.
DR   HOGENOM; CLU_000022_2_13_4; -.
DR   OrthoDB; 6297021at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic 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:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd19531; LCL_NRPS-like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-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; IPR036736; ACP-like_sf.
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; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          995..1072
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1358 AA;  144985 MW;  8CA9A20DB3723AFF CRC64;
     MSLEMTALSR RFAALPAAKQ RVFLEKLRAS GVGFDALPIV PRDPAAPVPM AYAQRALWLV
     WQRAPQSPAY NLSGRLALPL SCTPQQVQAC LAQLVARHEV LCTTYPAGAE GQPLQHIDPG
     HRFGWAVREW TGSRADSERE LAAAATGFGA RPFDLERGPV FRGELNLFAD GAPELFLAVH
     HIAADGQSVA LLVAELQALL AAPAASTQPA APALQYADYA VWQRQWLEAG ELERQTAYWR
     EQLRGAPQST PLPLDRPRQK ARDARGGQIN FALPPDVSQR LKELARKHAA SPYMVAIALL
     GLLVYRYCGE RDVCIGSPSA TRDRPELAAL VGHFTNVLVL RMKVDPAAGF VALLSQVRER
     VLEAKSHQDL PLDMLVEALA LERTPGLHPL FQIKSTQQAA GAVPADPAAA AHGIGVDEVH
     FDLSFDLVDT GSALSFVLAY AADIFDHATI ERLADALRSL AGQVAADPAR ALAATQLAGD
     SSLRGECASS PADNVLSLFD QAAARRGGAT ALSFGDRAHS FDELARAAGH WAAELESRGI
     GAEQRVAVCM ERTPEFVLAV LSVLKAGGAY VPIDPTLPQQ RIDELLADCG AALVLVSGGK
     PRQAALPCMR VGFDVPGGFL PHRARAMHPA QAAYLIYTSG STGRPKGVVV HHGALANYVQ
     GVLARLALPE GESFAMVSTV AADLGHTSLF GALCSGGALH LVSSEAAFDP DAFADRMAKT
     RAGVLKIVPS HLKGLLNAQR AAAVLPSHAL VLGGEATDAA TLQAIRALRP DLRIFNHYGP
     TETAVGMLTH AAPAQAGDTG NLPLGKPIAN MDAWVLDDAL QPVQPGMAGE LYIGGAGVAR
     GYLSRAGLCA DRFVASPFGD GQRIYRAGDR VRQRSDGTLE FLGRSDDQVK IRGYRVEPGE
     VAGRIRELDG VADAVVVAEQ GAQESAVLRA YVVARPGTSL DVEELRHALA DSLPAWMVPE
     RIVLLDALPL TANGKIDRKA LPRPAQPEPA RGFDAPQGPT EEALARIWSQ VLGVDRIARG
     DNFFALGGDS ILSLKLVARI RKQLPGGGQL SLPDVMQASS LGSLAERLRQ KFEGSHDAVC
     LSASGTGVPL FCLPGLIVNT REFLPLAEAL QGERVVYGFV SHVYTRKRWR GFDLQALAAE
     YASFILATAT EGRCALLGWS SGGDLAFELA RQLQGRIEIV FTGMLDVFET PPLRASAPLG
     AARRAQADEV LAQWLGRSEM AAHWKALFAR MDGEELAWVA EQVLNPAQPL PLDGTGDEAA
     EYLLWATIDK RVQAARYTCA RSPLPLHVFL ADSSLRREET LRNWADHAPV VSAEVLPQAD
     HLDIVRHPAL CASLKGLLRG ADAAHGAVQA AQSAAYQR
//
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