ID U5DK84_9CHRO Unreviewed; 1461 AA.
AC U5DK84;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Amino acid adenylation domain protein/thioester reductase domain protein {ECO:0000313|EMBL:ERN42081.1};
GN ORFNames=KR51_00012530 {ECO:0000313|EMBL:ERN42081.1};
OS Rubidibacter lacunae KORDI 51-2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Rubidibacter.
OX NCBI_TaxID=582515 {ECO:0000313|EMBL:ERN42081.1, ECO:0000313|Proteomes:UP000016960};
RN [1] {ECO:0000313|EMBL:ERN42081.1, ECO:0000313|Proteomes:UP000016960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI 51-2 {ECO:0000313|EMBL:ERN42081.1,
RC ECO:0000313|Proteomes:UP000016960};
RA Choi D.H., Noh J.H., Kwon K.-K., Lee J.-H., Ryu J.-Y.;
RT "Draft genome sequence of Rubidibacter lacunae KORDI 51-2.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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:ERN42081.1}.
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; ASSJ01000034; ERN42081.1; -; Genomic_DNA.
DR RefSeq; WP_022605746.1; NZ_ASSJ01000034.1.
DR STRING; 582515.KR51_00012530; -.
DR PATRIC; fig|582515.4.peg.1402; -.
DR eggNOG; COG1020; Bacteria.
DR InParanoid; U5DK84; -.
DR OrthoDB; 473401at2; -.
DR Proteomes; UP000016960; 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; cd05930; A_NRPS; 1.
DR CDD; cd19543; DCL_NRPS; 1.
DR CDD; cd05235; SDR_e1; 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; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; 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; 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; TIGR01733; AA-adenyl-dom; 1.
DR NCBIfam; TIGR01746; Thioester-redct; 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; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PIRSF; PIRSF001617; Alpha-AR; 3.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000016960}.
FT DOMAIN 973..1050
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1461 AA; 162335 MW; 3272BA836726604D CRC64;
MKAKNIADIY DLSPLQQGLL FHALYEPESG AYLDQHSICI RGPLQLDCFR QAWQQALERH
AILRTSFHWE NLKQPVQVVR KDLTLPWHTE DWSEVAPGDR AAKLHAWLQA DRARGFDLGQ
APLFRIVAIR LAADTTQIIF SRHHILIDGW SRMLLYQEIF ATYQALASDR VAPPLESPPF
RTYIHWLRQQ DPQQAKSYWQ QQLQGIVAPT RLSGDLAAGT ERNSFQQQHR HLSVAQTNAL
QTFARKHNLT LNTLVMATWG MLLGKFAGET DVIFGVTSSG RPPQLPQSGR IIGPLINTLP
LRVKLPGQQP LLDWLQALQA QQVAMRQYEH CALTEIQSWS DVPAGTPLFE SLAIFENYPA
ERADTEGEQS LEILDSDAIG YSHYPLNLLA IDGECLRLDL NYCSDRYSAA QIEQYLDVFT
ELLAQLPTAA ERPLSCWTGL SPNTRDRILQ KWNQTQRSFP EGCIHEQFAA QAARTPEAIA
VSDPNGSLTY GELNARANQL ACYLQTRGLG PEVAIGLALT RSNDLVVALL AILKAGGAYV
PLDPSYPQAR LDFILNDAKA ALLLTDSPTS QKFTNFSSTT ICFDTAAPEI ATQSDRNLET
PLTAQNLAYI IYTSGSTGQP KGVMIPHGAL NNHMAWFQGA FPLTSEDRIL QKTPFSFDAS
VWEFYVPLLV GAQLEMAAPD GHQDMDYLVR TIRDREVTIL QLVPSLLRAL LEHPEISTCR
TLRQVFCGGE ALPTDLVKRF FTCLVNAELH NLYGPTETCI DATAWTCGRE PIGLSIPIGQ
PIANLQAYVL DSHLHHVPVG VPGELYLGGR GLARGYLQRP DLTAERFIPN PYSTRPGERL
YKTGDLVKYL PTGVLEYLDR SDSQVKLRGF RIELGEIETK LQTHPDLQQA AVAVRATTAG
DRLVAYGVLA GENEPTLASL RDWLQTRIPD YMLPGAFVRL ERLPFTPSGK VDRRALPTPD
VHPSLARTTP YLAPQTDTER QLAKLWAALL SVELDTVGRN DNFFDLGGHS LVLIRLLTQV
RDTYKVSIPL RSLFNRATLQ AQGELLDAAQ QSIDLDLGNR PDLVREAVLA PEISPPATSP
VDISERIFLT GATGFLGAFL LADLLAKTNA RVYCLVRADS MERGAAKLKA NLETYNLWDR
DRGTRIIPVL GDLAKPLLGL SQDEFDTLAR EIQVIYHNGA WVNFLADYQT LKEANVLGTQ
EVLRLACSGE IAKPVHLIST VAVFSSGDRR DKVTVYETDP PEQSHLLQSG YSQSKWVAEQ
LALQARDRGL PVAIYRPGRV TGHSQTGQAN AGDFITSMLK GCIQLGNIYE PQNASDPVDL
TPVDYVSQGI VEISLQPDAM GQIFHLINPA PMSVAQLSHW LMEKSGYEIQ TVNYDLWRQK
LVQAATDAEA NALYPFLTRF PEQMPSATKA VRLAQQFDCS NASQALEQTT VRCSPVNSKL
LEAYFHYFVE SGFLPTPVSM L
//
