ID H5X7S1_9PSEU Unreviewed; 2067 AA.
AC H5X7S1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Amino acid adenylation enzyme/thioester reductase family protein {ECO:0000313|EMBL:EHR51364.1};
GN ORFNames=SacmaDRAFT_3133 {ECO:0000313|EMBL:EHR51364.1};
OS Saccharomonospora marina XMU15.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR51364.1, ECO:0000313|Proteomes:UP000004926};
RN [1] {ECO:0000313|EMBL:EHR51364.1, ECO:0000313|Proteomes:UP000004926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XMU15 {ECO:0000313|EMBL:EHR51364.1,
RC ECO:0000313|Proteomes:UP000004926};
RX PubMed=22768369; DOI=10.4056/sigs.2655905;
RA Klenk H.P., Lu M., Lucas S., Lapidus A., Copeland A., Pitluck S.,
RA Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., Land M.,
RA Ivanova N., Rohde M., Goker M., Detter J.C., Li W.J., Kyrpides N.C.,
RA Woyke T.;
RT "Genome sequence of the ocean sediment bacterium Saccharomonospora marina
RT type strain (XMU15(T)).";
RL Stand. Genomic Sci. 6:265-275(2012).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; CM001439; EHR51364.1; -; Genomic_DNA.
DR STRING; 882083.SacmaDRAFT_3133; -.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_0_3_11; -.
DR OrthoDB; 2472181at2; -.
DR Proteomes; UP000004926; Chromosome.
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:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd12117; A_NRPS_Srf_like; 2.
DR CDD; cd19540; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.980; -; 4.
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; 2.
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; 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; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 2.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 2.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000004926}.
FT DOMAIN 917..992
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1975..2050
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2046..2067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2067 AA; 221878 MW; 53AA5AAAF13EA56C CRC64;
MSQQLPAQTC ELTSAQEGLL RPDQYDPHAR TFDVVQAVVA LPPGLSADDL RKAAAGLMAE
RPELFARLGH DTTGRPVRGV VPGAPLPWTE HPEVDVDEVA AVEWERGFDV EVGGEPLLRF
ALARAEGDGS ALILTAHRAV LDTVGLHCLL TGLLAGDPGA SAAPPDTVVA RTAADADADV
DVWRSELAGP PEPCFLGRHV DAAARHSEAL PICLTSDTAE RLAALAAGLS TSTSAVYQGI
WAVVCARLTG RQDVVIGMGD NDLPLRVTVG AQSGASEVIH SVARFHERVA GHLDISGPAL
RRVTGVQSEL FDTAVVVDDC RWDEGVRLRQ STHHAITVIA RTGRATPVLE LVYRTDRFTA
SEARAAADLL ARAVQAVTDE PGVLVCDIDW LGDELRRELV VDYNETTASL PEGTLHSLFA
AQAARTPDAV ALHCEGRTLT YAALDAAANG LAHTLTQLGV RPGDSVALYQ GRSLEYVMAV
LAVLKCGAAY VPLDPRQPAD RLRWMIEDTG VGIVLTDPDT DEVPFAGVTR VLAVQDVVTT
AAHGQRTGPE LEVHPDEVAY VMYTSGSSGR PKGVATTHRN VVELALDPCW AGGRHSTVLA
YSPLAFDSST YELWVPLLRG GRAIILPSQE IDSRELARTI EQQGVTALYF TTALFDAIAQ
ESPHSLATVQ EVWTGGDVLS TVALRRVLDA CPDTTVVHVY GPTETTVFCS YESFGPDRRT
ATELTLGVPM ANTAMYVLDA ELRPAPPGVV AELYVAGTHL ARGYVNRPGL TAERFVANPF
GPPGSRMYRT GDLVRWRRDG LFEFVGRADQ QVKLRGFRIE PGEIEAALLG ADGVGQAVVV
VREDRPGDKR LVGYVVGTEG ASVDAGALRR AVAMALPDYM VPSAVVVLDC LPLTAHGKLD
RAALPVPRLE GEEDGRVPRT ATEETLCSLF ADVLDVGRVS IDDDFFHLGG HSLLATRLVS
RIRKALDTDV TMRDVFAHTT VAEIAAVIAE RASSRRPELV AMRRPKRIPL SFAQRRLWFL
GELEGASATY NIPLSIRLRG GLDPQALRLA LQDVLGRHEC LRTVYRLDEQ EPYQYVRPVA
DVALTLPVVA VGEGVLAARL AELAACTFDL ANDLPVRAHL LRVAEDDHVL LLVVHHIASD
GWSNGPLLRD LALAYEARLE GRAADWEPLP VQYVDYTLWQ RELLGAVKDP QSLAARQLGY
WRDVLAGLPE EVTLQSARPS PATASYRGAR VSAQLSAQVH EQLQSLARES GASLFMAVHA
ATAAVLTRSG AGTDVPVGSP VTGRTDPALD DMVGFFVNTL VLRTDTSGDP SFLELLARVR
ETDLGAWAHQ DLPFDLLVEE LNPQRSAARH PFFQIMLTLG DSITPAPELV GMTAEVTEAP
LDTARFDLTV NFLERRTPGG PGGVELRIDY AADRYDAETV QAFADRIIRF LEAAVADPSR
PIGDLDILDA AEWRRVIEPV TGDLSPRSHT TLPAVISGHA ATIPDAAAVV LGERCLSYAE
LEEYANRFAH RLVEVGVGSE TRVALLLGRS LEVPVSILAI LKAGGAYVPV DTDYPKARIQ
QILTAASASI VVTARDMTGL DLPEGITALP APELNGFSPG GTQTPAPDVD IHPDQLACTV
FTSGSTGIPK GVGNTHRNIV DLSLDQAFAT GAHDRMLQHS PLTFDVLAYE MWVPLLVGGT
VIVAPPGDLD AISVEQLIAE FRVRSLWLTA GLFHVMAEEN PSGFAGLQEV WTGGDVVAPA
AARRVMEHCP GTTVVNGYGP TETTVFATCY PLPRNTVYQG SLPIGLPLDN TGTYTLDDAL
RPVPAGVVGE LYIGGPGLAR GYVNRPGLTA ERFVANPFGP PGSRMYRTGD LVRWRRDGLF
EFVGRADQQV KLRGFRIEPG EIEAALLGAD GVGQAVVVVR EDRPGDKRLV GYVVGTEGAS
VDAGALRRAV AMALPDYMVP SAVVVLDCLP LTAHGKLDRA ALPVPRLEGE EDGRVPRTAT
EETLCSLFAD VLDVGRVSID DDFFHLGGHS LLATRLVSRI RKALDTDVTV RDIFEAPTVA
ELAERVSRAK PSRRPKLASL RRTGASS
//
