ID C7Q564_CATAD Unreviewed; 1837 AA.
AC C7Q564;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Short-chain dehydrogenase/reductase SDR {ECO:0000313|EMBL:ACU75833.1};
GN OrderedLocusNames=Caci_7003 {ECO:0000313|EMBL:ACU75833.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU75833.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU75833.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
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DR EMBL; CP001700; ACU75833.1; -; Genomic_DNA.
DR RefSeq; WP_015795561.1; NC_013131.1.
DR STRING; 479433.Caci_7003; -.
DR KEGG; cai:Caci_7003; -.
DR eggNOG; COG0236; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_2_11; -.
DR InParanoid; C7Q564; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000000851; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR CDD; cd08956; KR_3_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 Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR018201; Ketoacyl_synth_AS.
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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR015083; Polyketide_synth_docking.
DR InterPro; IPR036299; Polyketide_synth_docking_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08990; Docking; 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; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 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; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 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; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 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:UP000000851};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 34..461
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1692..1767
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1566..1585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1567..1585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1837 AA; 192073 MW; 201E30E4808EF4AF CRC64;
MATTEDKLRD YLKRVTVDLT EARRRLEESE NARREPIAII GAGCRFPGGV STLEGLWETV
RSGTDTITGF PTNRGWDTDG LYDPDPEAPG RTYTRHGGFL HDAADFDAEF FGMNPRSALA
TDPQHRLFLE TAWESFERAG IVPGSLRGSK TGVFAGTMHN DYAMRYINAH PAELEGAFLL
ANAPSVLAGR LSYTFGLEGP ALTLDTACSS SLVAVHLAMR ALRDGECSLA LAGGSTVMST
TDSFIEFCRQ RALSADGRCR PFSADAAGAA WSEGVGVLLL ERLSDAQRNG RRILAVIRGS
AVNQDGRSNG MTAPNGPAQE RVILAALADA GLDTADVDAV EAHGTGTPLG DPIEARALVA
TYGRGRKTDD PLWLGASKSI FGHTQAAAGL AGILKMVMAM RHGVLPPTLH AEVLSPHVDW
DAEALSLVTA EQEWTRRGGP RRCGVSAFGL SGTNAHVVLE EAPDAAASAA LVSGHGGPLA
WVISARTPAA LRGQAERLRS FEDTEPHDAG DVARALVSTR ALFSHRAVLL GDDRDALLSA
LDDYVAGRPN RDVVTGVAPD HAPRAFLFTG QGGQRAGMGR ELHAAFPVFA AAFDEVCDAL
DPHLDRPLKD VVFAAPDSPD AALIDQTRYT QPALFAYEVA AFRLLESFGI APDFVAGHSI
GEFAAAFVAG VWSLADAARL VVVRAALMQG LDAAGAMVAV EASFDEVAAS LVGLEDAVAV
AAVNSPTSVV LSGEEKACLR LAEQWQTAGR RTRRLAVSHA FHSPLMAPML DAFRAELARV
EFAAPRLAHA TNLGPDGSGG PDWDEPEYWV RQVRETVRFE ETVDALVAQG AAVLMEVGPD
AVLAGLAQGC PSAADVRVVA LQHRKRAEVE ALVGALAQGC VAGVGVAWDA LFGPVSGVPS
FDLPLYAFDR TRYWLPPRPR EAQVESVGQR ALTHPLLGAA VEVGDDGALV LTGRLAAAEL
PWLADHRVAG AELVPGTAVL DAVLVAAERA GCERVEELVF EAPIVLPPSG VLFVQIAVDA
ERGVRVYTRG AEDEVWTRRA SGRLGSSGTG VAEVCDWAVS WPPSGASEID AERGYDRLAD
LGYEYGPAFR GAVRVWRRET ELFAEVAAPE GLDLSGFGLH PALLDAAFHP MLLTADETEP
RVPFLFRGAR LTATGASALR VRLTVAGDEV TVAVADLSGN PVFGIDAVVV RAAPASAMAA
AGPTPYVVEW IDATPTARST PDPTTLVIPA VIAPDTDPML AVREATTSAL ATIHQTIESS
SRAVFLTHNA FNGSLADAAV WGLIRTAQAE NPGRFVLADV PLGFDDWGLL AACDEPQVRI
ADGRVSVPRL VRHTRTDADT DTGTASLPDG PILITGGTGG LGALIARHLV EHHGVSELIL
VSRSGTDAPS APALRELGAQ VTITACDVAN REALTKLLAE HPHLAAIIHT AGILDDATLT
TLTPTRIDAV LQPKLNAAWH LHQLRPHTPL ILFSSLAGTL ANPGQANYAA ANAALDALAT
HRRTQSQPAT SIAWGLWPTP TGMTTTLTPT EQTRLTQSGL TPLTTPEALT LFDTALAEAC
ALAPSATQAT EPGSPSASMA SAPSAPAEAT VLSSSAAPSA HTPGAASASS APSAFAEAAT
AAASGADVSA SHTATLIAAT FHLPGLRARA EAGTLPPILQ ALVPARRKPA TATAAPALRT
RLAALPEPQA KQALVDLVRA HVAAVLGYAG PASVDPDRAF AELGFDSLTA VELRNRLEAD
TGLSLPPALA FDHPTVAAVG AHLFVELAPA APDPHQALRA ALAEVEDLVL ARPDPALAEL
VAATLARLTA GSAGDGVEQR INDASDEEIF AFIDNEL
//
