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Database: UniProt
Entry: R6P1U4_9BIFI
LinkDB: R6P1U4_9BIFI
Original site: R6P1U4_9BIFI 
ID   R6P1U4_9BIFI            Unreviewed;      2300 AA.
AC   R6P1U4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Ketosynthase family 3 (KS3) domain-containing protein {ECO:0000259|PROSITE:PS52004};
GN   ORFNames=BN571_01066 {ECO:0000313|EMBL:CDC14654.1};
OS   Bifidobacterium pseudocatenulatum CAG:263.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1263060 {ECO:0000313|EMBL:CDC14654.1, ECO:0000313|Proteomes:UP000018036};
RN   [1] {ECO:0000313|EMBL:CDC14654.1, ECO:0000313|Proteomes:UP000018036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:263 {ECO:0000313|Proteomes:UP000018036};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000256|ARBA:ARBA00005254}.
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:CDC14654.1}.
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DR   EMBL; CBEV010000022; CDC14654.1; -; Genomic_DNA.
DR   Proteomes; UP000018036; Unassembled WGS sequence.
DR   GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:InterPro.
DR   GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd00828; elong_cond_enzymes; 1.
DR   CDD; cd03447; FAS_MaoC; 1.
DR   Gene3D; 3.30.70.2430; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.90.25.70; -; 1.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 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; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR013565; Fas1/AflB-like_central.
DR   InterPro; IPR047224; FAS_alpha_su_C.
DR   InterPro; IPR003965; Fatty_acid_synthase.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR002539; MaoC-like_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR10982:SF23; FATTY ACID SYNTHASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF18094; DNA_pol_B_N; 1.
DR   Pfam; PF08354; Fas1-AflB-like_hel; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF01575; MaoC_dehydratas; 1.
DR   PRINTS; PR01483; FASYNTHASE.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          1766..2214
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   2300 AA;  244224 MW;  8D3499D14A83F3F6 CRC64;
     MDEAWFPVLV REYPKPMPFV PVIDNDLLRW WGQDQLWQSE DSRYSADSVR IIPGPISVAG
     ITTVDEPVAD ILGRFEEAMV KRVSAESPSA DKTAFAQLGA ASSAEEFIRK SPNISWVGHL
     MANPAYGTSN GDANYEIRKI SSEGSIEKYD LDIHLDTYWD NDPDGGASKH AVRDIVIPLN
     VDGNESGLFP VVDRDRLPEH VYRMLADTAG IGNTAITGDK LTAMPVIEQV ADKAAHPFGQ
     AHTSYTLSAN LGFDHEAATG GALPSNLVPS RIAPDALVGP AWPAIYAALG SVYVNGFPVI
     EGLLNAVHLD HLIELEVSED ELLKHTGEQI ALTSWAENYF ESASGRVVTI HVTHSAQDGT
     VLANETERFA IRGRAYSDAL PPEAPDYGGI EAEIESTPRR LLRRVKVTAP HEMTAFARTS
     GDFNPIHTSH RGAAVSGLAA PLVHGMWLSA TAQYAVQALD GKGAHYEIAG WTYNMYGMVQ
     LDDEVEISVE RVGRVAHSGM VLEVTSRIDG NIVSRGTAIV RAPKSAFVYP GQGIQQQGMV
     LDERAKSPAA RDVWERADKV TCEKLGFSIL AVVRDNPKEL TANGVTYRHP EGLLNLTQFT
     QVALATVAFA QTARLREAGA DIWPAYFAGH SLGEYNALSS FAGVIPLETV IELVFHRGST
     MHHLIPRDAK GRSNYRMGAL RPNQFGVGDD GVREYVESVS KASGEFLQIV NYNLAGQQYA
     VAGTIAGLKA LKADSARRVA EYGGKPAFML VPGIDVPFHS TLLRKGVPEF RDKLDALLPQ
     TIDYRGRLVG RYIPNLVAAP FEMTKEFAAK ILEVVPSERI QAALDDPQIW DSYAADDQKL
     GRLLLTELLS WQFASPVRWI ETQALLFGSA EQGGLGVEEY VEVGLGNAPT LANLGAKTLR
     LPQFAGRDVT VYNVGRDEGR VYMTDSDSLV PEEDADDSAV AAAASSAAAA PAVASAPAAA
     PAAVAEVPVA AASAGAPSGA AVADIPFKAS DAIATLLAYS AKVRPDQIGE SDTTDTLTNG
     VSSRRNQLLM DISSELGVAS VDGAAEATVK ALSALVNKVA PNYKAFGPVL SDIVRDRVRG
     MFGAAGVKLG QITKRVTDTW QLGEGWTSHV VAALVLETRE GASSRGGDLA SLSTDAASNA
     AAANALIDAA VQKVAADKGI AVAMPSAGGA AGGAVVDSAA LDAFAAKVTG ADGVLASTAK
     FVLNQLGVAA PVAEETADEN AAVVAAVEAE LGADWPKQVE PRFDERKAIL FDDRWASARE
     DLARAYYNND ESALNGSFIG LGKTIADEAA WYAGKSDNAD LKAAFNRVAA EAGENASESA
     ETSRFAGDIA VVTGVAPNSI AAQVVNGLLA GGATVVATSH SFKPSVKAWA KQTYREHAAG
     DAKLWLVPAN LSSYRDVDAL VTWVGNVQKK TSGATTTILK PAYEPSLFFP FAAPPVHGSL
     ADSGELFESQ ARLMLWGVER AIAGLAKIGA DTDVQHKLHV VLPGSPNRGI FGGDGAYGEV
     KSAFDAIVNR ARAEKVWSSR VTFAHPKIGW VRGTGLMGGN DPLVEVVERH GLKTYSTAEI
     AVELLNLSTR ESRIEAAKAP LDVDLTGGLG NEPIDIKALR AEAMEDAAQA EAANAKNAIA
     GNESDTAAKT LIKALPSPRA PRQAKVDLAD WQNVSARPED EIVIVSVGEL GPWGSGRTRF
     EAELGIHSDG QVDLSAGAVL ELAWNMGLLT WNDSPKPGWY DVDGNLVPEE DIAERYHDEV
     VARSGVRPFD EGMGNDYKDG TDEEEAEVFL DHDVTFSVPT REIAEEYVKL DEAHTSFAAD
     AESGEWNVTR HAGSMIRVPR RAAMTRTVGG QFPKGFDPVK WGIPASMVGD VDKIALWNIV
     TTVDAYLSAG FTPTEILEAV HPSMVASTQG TGFGGMASMR KLYLDRFLNH EIPTDILQEA
     LPNVVAAHVM QSYIGGYGNM VQPVSACATA AVSLEEGADK IALGKADFVV TGAIDDIGVE
     SVIGFGNMNA TANSEEMYAK GIDARFFSRA NDRRRGGFVE SQGGGTILLT RGDIALKLGL
     PVAGVIGFVH SYADGAHTSI PAPGLGALAA GMGGKDSKLV RDLARLGVTP DDIAVVSKHD
     TSTNANDPNE SELHNTLAHA IGRADGNPLF VISQKTLTGH AKGGACIFQV NGLTQLFKSG
     VIPANAALDC VDPKLMRDDH MVWLREPLKV GSVKAGLATS LGFGHVSGFA AIVNPGAFEA
     AVANTAGVEA LNAWRDRANE RLAAGQRRLE EGMMGRAALY EPIDNRRFHE DGRGYNAHEV
     EKAMLLDPNA RLGASGYFEA
//
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