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Database: UniProt
Entry: B3DPT9_BIFLD
LinkDB: B3DPT9_BIFLD
Original site: B3DPT9_BIFLD 
ID   B3DPT9_BIFLD            Unreviewed;      3172 AA.
AC   B3DPT9;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   SubName: Full=(Acyl-carrier-protein) S-malonyltransferase {ECO:0000313|EMBL:ACD99078.1};
GN   Name=fabD {ECO:0000313|EMBL:ACD99078.1};
GN   OrderedLocusNames=BLD_1633 {ECO:0000313|EMBL:ACD99078.1};
OS   Bifidobacterium longum (strain DJO10A).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=205913 {ECO:0000313|EMBL:ACD99078.1, ECO:0000313|Proteomes:UP000002419};
RN   [1] {ECO:0000313|EMBL:ACD99078.1, ECO:0000313|Proteomes:UP000002419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJO10A {ECO:0000313|EMBL:ACD99078.1,
RC   ECO:0000313|Proteomes:UP000002419};
RX   PubMed=16391088; DOI=10.1128/AEM.72.1.527-535.2006;
RA   Lee J.H., O'Sullivan D.J.;
RT   "Sequence analysis of two cryptic plasmids from Bifidobacterium longum
RT   DJO10A and construction of a shuttle cloning vector.";
RL   Appl. Environ. Microbiol. 72:527-535(2006).
RN   [2] {ECO:0000313|EMBL:ACD99078.1, ECO:0000313|Proteomes:UP000002419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJO10A {ECO:0000313|EMBL:ACD99078.1,
RC   ECO:0000313|Proteomes:UP000002419};
RX   PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA   Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA   Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA   Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT   "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT   reveals loci susceptible to deletion during pure culture growth.";
RL   BMC Genomics 9:247-247(2008).
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000256|ARBA:ARBA00005254}.
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DR   EMBL; CP000605; ACD99078.1; -; Genomic_DNA.
DR   RefSeq; WP_010081377.1; NZ_AABM02000013.1.
DR   KEGG; blj:BLD_1633; -.
DR   HOGENOM; CLU_000114_7_0_11; -.
DR   OMA; APLVHGM; -.
DR   Proteomes; UP000002419; Chromosome.
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:0008897; F:holo-[acyl-carrier-protein] 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; 1.20.930.70; -; 1.
DR   Gene3D; 3.30.70.2430; -; 1.
DR   Gene3D; 3.30.70.3320; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.90.25.70; -; 1.
DR   Gene3D; 6.10.140.1400; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
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; IPR013785; Aldolase_TIM.
DR   InterPro; IPR013565; Fas1/AflB-like_central.
DR   InterPro; IPR040899; Fas_alpha_ACP.
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; IPR016036; Malonyl_transacylase_ACP-bd.
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; PF18325; Fas_alpha_ACP; 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; 2.
DR   SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 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   Transferase {ECO:0000313|EMBL:ACD99078.1}.
FT   DOMAIN          2621..3086
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   REGION          1752..1825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2461..2491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1793..1823
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2467..2491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3172 AA;  338288 MW;  8D8D8B70D812B516 CRC64;
     MTTFFLNRLA TEPHALAFAG QSTPWPVALA DQTTDPSLDE ALRGHVAAAG RLLTPVAADL
     LATTGRPVDL FGFAPNPARL GAAADATASV EGVALTQLGA LLDLEHLGYS VAQAKPLAVL
     GHSQGVLAVH MTRAIEAAGS IEAAGKTLNE ILAVAALIGA AGTRRVRELG LNPKYGEASP
     MLSVKGATRE QVEALVARVN NARGPISIAV TNSDNHHVLS GYPEDLAAFA LEAEREHQHQ
     AKLREQKLHG GTVFNPTLEY LEVTLPFHSP LMADAVEQTV AWAGACGFDQ KRTRALAEEV
     LLNHVDWNAR VKALFDDADP SKLWIVDLGP GNTLGKLIGN VVQGTGIGVV EATTLAERST
     LSMLESEPER TQNWKAFAPR VINTPAGAKL VTKFSKLTGK PPVLLPGMTP TTVEPEIVAA
     AANAGYWAEL AGGGQVTAEV FDRHIAALED ELEEGRTVEF NAMFMDRYLW NLQFGSSRIV
     PKKRTSGAPI DGVVVSAGIP ELDEAVELIK NLQADGLPYV SFKPGTVDQI RQVVRIAKAV
     SPTTIMVQVE GGEAGGHHSW EALDDLLAAT YAEVRACDNL VLVAGGGIGT PERAADYISG
     QWAHAYGLPD MPVDGVLIGT AAMTAKEAHT SPEVKQLLVK TPGIPADAKS DDVFAPQAAH
     WVPSGKSVGG MSSGLSHLHA DIYELENDSA ECGRLLVRVM KHPEELDSRR KEIIEALNKT
     AKPYFGDLAS MTYLEWARRF AELAFPWVDP TYADRFQHLL QRIEARVNDT DSGEFTSKLF
     AADGVSAEEA AAAGLLTHDD ILADPAPALE KLALAYPQTA ELKVVPTDVA WFPVLVREYP
     KPMPFVPVID NDLLRWWGQD QLWQSEDQRY SADSVRAIPG PISVAGITTI DEPIADILGR
     FETAAIKRVQ DEQQAADAAE NDDFAALGEA TSAEDFIRKS PNISWVGHIT DNPAYGTALG
     DQYYEIRAFD AAAGKYDLDI HLDTYWDNDP DGGTSKHAVR DIVIPLIVEG TEPGRVPVVD
     RERLIPDVYA MLAATAGIGN TAITGDKLTE MPQLDGKTSD ERPFATATAA YTLSANLGFD
     HEAATGAALP TTLQPSRIAP DALVGPAWPA IYTALGSVYV KGYPVIEGLL NAVHLDHLIE
     LEVNEEDLLK HTGETITLKS WAEDYFESAS GRVVTIHVTH TAADGTLLAR ETERFAIRGR
     VYSDALPADA PEFGDAEHEE IAPTPRRLLR RVKVVAPHDM TAFARTSGDF NPIHTSTRGA
     RISGLAAPLV HGMWLSATAQ HAVQALDEKG AHYEIAGWTY NMYGMVQLDD TVEISVERVG
     KVRHGGMTLE VTCRIDGQLV SRGTALVRAP RAAFVYPGQG IQKQGMVLDE RAKSAAARDV
     WERADKLTRS KLGFSILGLV RDNPKELTAN GVTYRHPEGL LNLTQFTQVA LATVAFAQTA
     RLREAGADIW PAYFAGHSLG EYNALSAFAD VIPLETVLEL VFHRGSTMHH LIERDAQGRS
     NYRMGALRPN QFGVDDAHVK EYVESVAKAS GEFLEIVNYN LAGQQYAIAG TIAGLKALKA
     DSARRVAAFG GKPAFMLVPG IDVPFHSTLL RKGVPEFRDK LDALLPAYID YRGRLVDRYI
     PNLVATPFEM TKEFAAKILE VVPSERIKAV LDDPAVWDSY ADDDQKLGRL LLTELLSWQF
     ASPVRWIETQ ALLFGQREQG GLGVEEYVEV GLGNAPTLAN LGAKTLRLPE FAGNDTVVYN
     VGRDEGRVYM TDTDSLVPDD EPEEAAASAP VETAPAGGSA VAKLGSGAAP ANAVTEAAQT
     TDGSVAGQST GLSDSSRGLQ SGQAAAGAPS GAAVADLPFK ASDAIGVLMA YSAKVRIDQI
     GSNDTTDTLT NGVSSRRNQL LMDISSELGV ASVDGAAEAT LDKLAQIVNK AAPNYKPFGA
     VLSEALRDRL RSLFGAAGVK QQYIRDRVTN VWQLGEGWVA SVLATLLLDT REGASSRGGD
     LAKLPTAAVQ NKPEADKLID AAVEVVAQLK GVAVALPSAG GAAGGAVVDS AALDAFAEKV
     TGSNGVLAAT ARFVLNELGV AAPAPEESED ENAAVVAAVE AELGSDWPKQ VAPRFDANKA
     ILFDDRWASA REDLARAYYD NDPAALNGSF IGLGKTIAAE AQWFANESES EELKAAFQKA
     GSEALEQVAS NKNASRYAND IAIVTGVSPN SIAAQVVEGL LAGGATVVAT SHSFKPSIKA
     WAKQAYREHA TGNAKLWLVP ANLSSYRDVD ALVGWVGHEQ KKTSGATTTI LKPAWEPTLF
     FPFAAPPVHG TLADSGDLFE SQARLMLWGV ERAIAGFSHI GADTNVQHKL HVVLPGSPNR
     GVFGGDGAYG EVKSAFDAIV NRARAEKVWS SRVTFAHPKI GWVRGTGLMG GNDPLVAVVE
     RHGIRTYSTA QIAAKLLDLC TAESREQALK APLDVDLTGG LGSEPIDIKA LRAEAMADAE
     KEAAAASSQE TDGSVAGKST GLSDSSRGQQ IKALPTPIVT KQASVDLNDW TNVTAKPEDE
     IVIVSVGELG PWGSGRTRAQ AELGIHSDGT VDLSAGAVLE LAWNMGLLTW ADSPKPGWYD
     TDGNLVPEED IAERYHDEVV ARSGIRPFEE GMGNDYKDGA DEEEAEVFLD HDVTFSVPTR
     EVATEYVKLD EAHTTIAPDE ESGEWNVTRH AGSMIRVPRR ATMTRTVGGQ FPKGFDPTRW
     GIPASMVGDV DKIALWNIVT TVDAYLGAGF TPAEILESIH PSLVASTQGT GFGGMMSMRK
     LYLDRFLNHE IPTDILQEAL PNVVAAHVMQ SYIGGYGNMI QPVSACATAA VSLEEGVDKI
     ALGKADFVVT GAIDDIGVES VIGFGNMNAT ANSEEMYGKG IDARFFSRAN DRRRGGFLES
     QGGGTILVTR GDIAEKLGLP VAAVVGFIHS YADGAHTSIP APGLGALAAG LGGKDSKLVH
     DLAKLGVSAD DIAVVSKHDT STNANDPNES ELHNTLAHAI GRTDGNPLFV ISQKTLTGHA
     KGGACIFQVN GLTQLFKSGV IPANAALDCV DPKLQRDDHM VWVRKPLRIG GGEDEFGRET
     AGRPVKAGLA TSLGFGHVSG FVALVHPGAF EAAVAKADGE AALEAWRERA NARLAAGQRH
     LEEGMMGRAA LYEPIDNRRF REDHRGYDHH EVEKAMLLNP DARLDADGYY EA
//
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