ID B3PCU1_CELJU Unreviewed; 1721 AA.
AC B3PCU1;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Oxidoreductase, zinc-binding dehydrogenase family {ECO:0000313|EMBL:ACE83632.1};
GN OrderedLocusNames=CJA_3002 {ECO:0000313|EMBL:ACE83632.1};
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE83632.1, ECO:0000313|Proteomes:UP000001036};
RN [1] {ECO:0000313|EMBL:ACE83632.1, ECO:0000313|Proteomes:UP000001036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE83632.1,
RC ECO:0000313|Proteomes:UP000001036};
RX PubMed=18556790; DOI=10.1128/JB.01701-07;
RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467}.
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DR EMBL; CP000934; ACE83632.1; -; Genomic_DNA.
DR RefSeq; WP_012488581.1; NC_010995.1.
DR STRING; 498211.CJA_3002; -.
DR KEGG; cja:CJA_3002; -.
DR eggNOG; COG0236; Bacteria.
DR eggNOG; COG0451; Bacteria.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_2_6; -.
DR OrthoDB; 9778690at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001036; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
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:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 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; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001036};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 37..464
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1590..1668
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1554..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1721 AA; 187867 MW; D442E2498E732A96 CRC64;
MTDNKPWRHD THNQQKRALL KIRELKQALS QQQQAQRAPI AVIGIGCRFP GSINSPESFW
STLAAGKDCI GDIPDHRWNH KQYFSEYPAK KGRIYVNQGG FIDGVDQFDA GFFNISEREA
AAMDPQQRLL LEVSWEALEN AGRDPAGLRG QRVGVYNGVC TQDYARFSLH SHNPDNIDIY
SFTGTAPSIA SGRISHVLDF QGPNITVDTA CSSSLVALHL AVQSLRHGEV DLALAGGVNI
ILSPENYIYF CHVNALSPEA RCKTFADDAN GYVRSEGCGV VALKLLDQAL ADGDPVWGVI
RGSAINQDGQ SFDLTAPNGT AQRQLIEQAL QNAGVGAGEV NYVEAHGTGT PLGDPIEIGA
LGAIYGAGRS ADKPLWIGAL KSTIGHTEAA SGIAGFIKTL LCLTRGKIPA NLHCTTKNTR
IPWADFPAIL PTELAEWPAC GERRLAGISA FGFSGTNAHI IVEAAPECAT VAPRWQLPPN
RFQRKSLWLT SKPLIAAQGA ELHPFLQRRL KSPAWTGVCY EADLSLARFG FLRSHPVWGK
VVAPGAVYIE AAFAAARDIF ASSQIVLKDC IYHEVFVLEE GLVATMQLTL TDLTDDSAAF
HIYSQAGAQE GDWRLHAEGS IHRNLDGGDS PPLALQSVKS RCRHTFDEGH FYQTLDERGY
YYGADHRGVR EAWVGEGEAL AQIAVPRSMV AEEAQMLGDY YFHPAILDSA FQLLLMLLPD
VGKDEMYVTL GKQSTTFCAP CQSSLWVHTR RLPGSDERNT TVRGDVRVYD QDGNIVMETL
GYIMKRTVKR GQSHLPPAEV GIYHTLRQPL NLPAKPLATT DDVALLGDPQ TPQWQVVTDA
LQRQGVTVAP VNPDDPVQPS SRPLVYLWPS WSPEDDGSAR LTQTLTQLTR IINALAQLSA
EEQSPFVILV QANNPVVEAL AGLLYSARDA YHHCALYLMA WSDTADLANL LPYLTQPRLL
GDECHLVCEA GLIQVPRLSL LRDVRQVWHS KLTLRERGNL SSLEWAMRPS QSLGANDVDI
RVEACGLNLR DVFDALGLHP RQLHEWGLEC TGVVVNIGSQ VTAFKPGDSV LAFGTGCLAH
RIVVPVNRVV HLPELLDFAE GATIPIAFLT AYEGLVLAGN LRAGQRVLIH GAAGGVGMAA
VQIAHAIGAE VYGSCSPDKT PVLQQMGVAH VLNSRDIGFA RQIPPASIDL VFNSLSREFI
DVSVPLIREG GCFIEIGLNG WPVEMMQAQR PDIRYHLINL MATWEQHPEL VKARLEDILQ
HIQTRRYSPL PLTRFSQQQT EQAFRQMQQG KHIGKVVILP ETGVAPARNG VQVITGGTGA
LGIKLAHWLL QQGFSKLALL SRHQSESLAL EKWPEPADVR HYVADVADAV AVEGALQRVR
TDLGEITGVF HVAGATCDAP MAELGETHFE RSLQSKVQGV LHLHSATQQD PIQRFVMFSS
LAAVIGSAGA ANYAAANGFL NGFCTYRQSL GLPALSIAWG PWRAGGLFDN LDKRTQDYLQ
KRGITPVGDA NYFAALEALL DCEGNYPVMA MDWSKWVAEA APRDAFFHSV SNSPGRVLPR
NSSLSPANNP GSARPASRLL QDLAGTRGAS RNRVLQQHLW AQLVDILGMA PGTPVDTRTG
FFDLGLDSLT SVELRNRLQN DLQCQLSSTI TFDYPNLDAL LAHLLELTAA QLQTIAAAPE
LPPVIPLIEH QECDPFIRLD SMSDDELYRA LLQPTSMETD V
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