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
//