ID H1SA26_9BURK Unreviewed; 1463 AA.
AC H1SA26;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Amino acid adenylation protein {ECO:0000313|EMBL:EHP40575.1};
GN ORFNames=OR16_24725 {ECO:0000313|EMBL:EHP40575.1};
OS Cupriavidus basilensis OR16.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP40575.1, ECO:0000313|Proteomes:UP000005808};
RN [1] {ECO:0000313|EMBL:EHP40575.1, ECO:0000313|Proteomes:UP000005808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR16 {ECO:0000313|EMBL:EHP40575.1,
RC ECO:0000313|Proteomes:UP000005808};
RX PubMed=22461549; DOI=10.1128/JB.06752-11;
RA Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
RA Nagy I., Horvath B., Nagy I., Kukolya J.;
RT "De Novo Genome Project of Cupriavidus basilensis OR16.";
RL J. Bacteriol. 194:2109-2110(2012).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHP40575.1}.
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DR EMBL; AHJE01000062; EHP40575.1; -; Genomic_DNA.
DR RefSeq; WP_006160291.1; NZ_AHJE01000062.1.
DR PATRIC; fig|1127483.3.peg.4942; -.
DR OrthoDB; 9154499at2; -.
DR Proteomes; UP000005808; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd05235; SDR_e1; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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; IPR036736; ACP-like_sf.
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; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR010080; Thioester_reductase-like_dom.
DR NCBIfam; TIGR01746; Thioester-redct; 1.
DR PANTHER; PTHR45398; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR45398:SF1; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 972..1047
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1463 AA; 161514 MW; 058C2A28B68BB5EB CRC64;
MNLDKHNVAD VVPATPLQQG MLYHALAAQD PAMYLEQYGF SVHGDLDIER YRTAWQQVLD
HQPMLRTSFH WEGLGKAYQV VHKRLEVSFE HIELSHLAGP QHSVVQDKLR AERRAAGFSL
NRAPLFTVTV VTLAKSLHKI WLTLHHLLAD GWSLYLLLAE VGQLYQHPLG LPAPAVPFRR
YCEWLQAQDQ DSARRWWQDR LGAGGFTGKA PLVEQSRTGS STAVDYKLNE AESARLQQGS
RRQGLTESTL FNAAWSILLR RYLRQDRLVF GYTVSTRPAE IDGIERMLGL LLNVLPVTVD
LNPEQEIEPW LQALQQQLIA DRQHDYLPLS ELQRLAGTAA NQGLFQTLLV WENQPGSSVE
EGSADSLRVV HDESYELNHY PLMLAGYPGS VVRLRLNFRE RALSHARALD LLQQMADIML
VLAEGGPRKL GDLIADRIMQ PLPTLSLDAV PTAIAPSLWQ RILELATANP SAPQLDQAQP
AQSFTRNDLV LRAQSLARRL AASLPADRSA PLALLLWPGI DYVSAILAAL YLGRPWLALD
PRRPVEGLGE QLAYIQPAAL LSEPSLWPEP HRWEGPTIVD LSAAETGPVT ACVPPVVMDE
VDCVCMVLTS GSTGRPKCVS LPLRALRQRL GWMQSFLPAS PEDSILLKTS PAFVDAICEV
LGPLISGYRM VAPTPEQSHD LGQWPALLTE QAITRLVITP SVLEGLLRVL AEPVPSVHLL
QVSGERFPSD LLERGKQRFP NARILNLYGS SEVMADACAF DCSAWQPAHC ATVPLGKLLP
GALGAILDEG RHPLPEGAIG ELFLGGDCLA IGYHANPDAT DAKFREMDGL PGRPRMYATG
DLVALGEDGQ LHYHGRADHQ IKLNGMRIEP GEIESLLKSR KGVDDAALAC HHNAVGQAIL
TAHIASQCYH KDPEALVADL QVLLSRQLPS GQMPRHWQVT TDLPRNASGK LDRRALRYLD
AAVAVHSIER VAPHTDRQQR LHAVWQQVLG QDAFGIDDDF FALGGSSISM TQLCFAVRKA
FHVPFPIRGA FEAPSIRQQA DLIQQYQDGA QPVADRGTGR PQHHDLHIDA ASADHVLPLA
GEITPWPQGA VHVFLSGAQG FINAWLLARL LDDPTLTVSC LAPGSDAQSA WAGLVEHLSQ
FGLWSGERGS RLRIVAGDLG QPRFGLSEQD WQALAEQCQV LFHTGVAINF VAPYAQLRAT
NALSTATMLD LATTARAKPL HFVGSLGVVD HSRAAGDSAR VREDDALLTW RGLPTGYLQA
RWVSDTMIRR AIERGVPCSV MRMTTVSGDT DRHQANSQDM MWQLIKLAMT VGIIPDTPRP
IDLVPVDRAV EAVIALARSA STLGQAWHVS NPRIWKWAEV AALLRSKGYP VHLLSGEEWS
QRFGRVAMQL GEQPEWQKVL PLLGDAWQEH KHFFELDKHK TLERLRQLDS ALPPMDEQLL
WQTVERFFES GFLPRTGVAA AYG
//
