ID A0A1L9QU94_9CYAN Unreviewed; 1650 AA.
AC A0A1L9QU94;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Short-chain dehydrogenase {ECO:0000313|EMBL:OJJ26260.1};
GN ORFNames=BI308_07415 {ECO:0000313|EMBL:OJJ26260.1};
OS Roseofilum reptotaenium AO1-A.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Desertifilales; Desertifilaceae;
OC Roseofilum.
OX NCBI_TaxID=1925591 {ECO:0000313|EMBL:OJJ26260.1, ECO:0000313|Proteomes:UP000183940};
RN [1] {ECO:0000313|EMBL:OJJ26260.1, ECO:0000313|Proteomes:UP000183940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AO1-A {ECO:0000313|EMBL:OJJ26260.1};
RA Buerger P., Wood-Charlson E.M., Weynberg K.D., Willis B., Van Oppen M.J.;
RT "CRISPR-Cas defence system in Roseofilum reptotaenium: evidence of a
RT bacteriophage-cyanobacterium arms race in the coral black band disease.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OJJ26260.1}.
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DR EMBL; MLAW01000009; OJJ26260.1; -; Genomic_DNA.
DR STRING; 1925591.BI308_07415; -.
DR Proteomes; UP000183940; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 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 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; IPR049490; C883_1060-like_KR_N.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF21394; Beta-ketacyl_N; 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; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
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; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000183940};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..435
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1522..1597
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 437..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1650 AA; 180857 MW; 8679085987AD0FC3 CRC64;
MRGKLEAVNK AKTEPIAIVG MACRFPGGAT DPSKYWSLLH DGIDAITPVP GDRWDVSAYY
DPDPEVLGKT YTKEGGFIEQ VDQFDPLFFG ISPREAASLD PQYRLLLEVT WEALENSGQT
WTNLKNSQTS VFMGISTDDY SSVIFNEAKS YPTLGSNRSI GVGRISHLLG LQGSNIQVDT
ACSSSLVAAH LACQSLRSGE SNLALVGGVN LILSPFSTIG RCQLRALAPD GRCKTFDASA
NGYGQGEGCG VLVLKRLSDA VSDGDLISAV IRGSAVNHDG PSSGMTVPNR MAQKKVIQQA
LSNAKLEPDQ ISYLEAHGTG TSLGDPIEIE ALAEVYGKKR PVDDPLIVGS VKTNLGHLEA
AAGVSSLMKV ILALKHQEIP PHLHLKEPNP HVDWDRLPIK IPTSLMPWSD EGKPRIAGVS
SFGMGGTNAH IVLEEAPREG NRHTSTALSD QTSTALSDQG NSEDQLERSL HILTLSGKTE
KALEDLVSRY QKHLETNPDV AIAEVCYTAN TGRQHFQHRL AVIASDPKEL AEKLLGWKRG
QEVVGLSCGQ FDRGSASSKI AFLFTGQASQ YVDMGKQLYE SQPTFRQALD RCDQILQPYL
DYPLLEVLYP KEEQKSSSSL LDQTAYTQPA LFAVEYALFK LWESWGIKPN VVMGHSVGEY
VAATVAGVFS LEEGLKLVAA RGRLMQQLPP GGEMVAAIAS ESVVQEEIGD DASKVTIAAI
NGPESTVISG ESGAIASICT KLEAQGIKTK PLQVSHAFHS PLMEPMLAEF AAVAQEVTYR
QPKIKFVSNV TGQKAGNEVT KAEYWVNHIR QPVQFYQSIK TLHEQGNELF LEIGPKPILL
GMGSRCLPDV GVWLPSLRPG VAEWQPMLSS LGQLYVKGIT VNWSGFDQDY TRQKVALPTY
PFQRECCWVE INKQKEPQTS GGITETSIVK LLSQGKTEAI AQQLERSVNL SPEQRKLLPE
LLEALAKQHQ EQLAAAAIAN WFYEIQWKPL NRSGSPNNMQ PSHWLIFADR TGIAEKFAQK
LQQQGHQYSL VYRGKSYQKP EAGKYQLNPS IPEEFDQLYQ EIQDGNQLPL SRLIHLWSLD
APESKDLTLD ALQETQLWGC GSVMHLVQTL LKNASLSPLW LVTRGSQSVL SQEKNIPGLA
ASTLWGLGRA ISLEHPQLWG GLVDLDPQAS VEDEIEMLWQ LLGNEQEEDN LALRGEQSYV
ARLANQEPPE FPQSLSLSSD GSYLITGGLG ALGLHTAEWL VEKGAKNIIL TGRRPPSEKV
QESIQQLEQA GCQVKVLLGD VSIEEQIAQI LEQIQTSMPG LKGIIHTAGV LDDGTLQQMN
WERFSQVMSP KVTGTWNLHQ LTQNLPLDFF VCFSSIASLI GSPGQGNYAA ANAFMDAFAG
YRRSIGLSGL AINWGAWASE GMAARLAVEH QNRIQSSGVS EIALKEGMYA LELLLGNQIA
DPPPVPLRKG EVRECCAVPG QVGVIPVEWS VLAEHWSGLQ KSSLLRELLE QEELAERDTL
KQKVKAEILA KLEAASPEER QEILIEHIRG QVVQVLGLSS SQLPEMNVGF MEMGMDSLMA
VELKNRLQNQ LGTHLPETLA MEYPTIAKLS LYVEELMEWK TTENGTFSDK LSPTDESEIE
GDILPDIEDI SEEDFEALAA QQLEKLKNML
//
