ID D0KZC3_HALNC Unreviewed; 2134 AA.
AC D0KZC3;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE SubName: Full=KR domain protein {ECO:0000313|EMBL:ACX95796.1};
GN OrderedLocusNames=Hneap_0958 {ECO:0000313|EMBL:ACX95796.1};
OS Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus
OS neapolitanus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Halothiobacillaceae; Halothiobacillus.
OX NCBI_TaxID=555778 {ECO:0000313|EMBL:ACX95796.1, ECO:0000313|Proteomes:UP000009102};
RN [1] {ECO:0000313|EMBL:ACX95796.1, ECO:0000313|Proteomes:UP000009102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23641 / c2 {ECO:0000313|Proteomes:UP000009102};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Kerfeld C., Cannon G., Heinhort S.;
RT "Complete sequence of Halothiobacillus neapolitanus c2.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001801; ACX95796.1; -; Genomic_DNA.
DR RefSeq; WP_012823832.1; NC_013422.1.
DR STRING; 555778.Hneap_0958; -.
DR KEGG; hna:Hneap_0958; -.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_2_6; -.
DR OMA; DEANYHI; -.
DR OrthoDB; 9778690at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000009102; 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:0008270; F:zinc ion 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; 3.30.70.3290; -; 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; 3.90.180.10; 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; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
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; 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; 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; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; 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; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
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.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00023160};
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:UP000009102};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 20..444
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2024..2099
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2107..2134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2114..2128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2134 AA; 233315 MW; F1EE40A379ACD51C CRC64;
MEQPTINSET MVKQLLSEKH EPIAIVGLSL RLSDGISDLN GFHHLLLDGR DNIVDIPESR
WDNKKYFSSA NDSGNAICTN RGGYLNDIDK FDPAFFSISP KEARYMDPQQ RIMLELCWEA
LENAGLNPEE LRGSDGAVYL GSSSLDYARD MMGLGEKQLV SQLGTGTANS AISGRISYFL
GWRGPSMTVD TACSSSLVAI HLASSALRNK ETSFAIAGGI NIVHNPVSHI IFTRANMLAP
DGRCKTFDES ADGYGRSEGA AVLVLRRLSS AIADGNRILG VIRGSAVRQD GESGGLTVPN
GVAQEAVMRD ALRRSLVKPA DISYVEAHGT GTPLGDPIEI HSINSLFSER PNIDEKVYVA
SSKTNLGHME AAAGVGGILK CLAQLNSKLI YQHINFNNPS SKIDWGALSV TVPTEVQPWE
QPVRRAMVNS FGFAGTIASL VLEEAPVMNA PPRVDKKGTS GASDDPFIFT VSAKSSSALL
RNMRAYLETL IKSSADDMDS IIWTSSVGRQ HHPYRWAASA RNNDELMQLM RSSLDESEEL
MADTERMLQF SEARVAFLLT GQGAQYPGMG AGLYKKNRVF RRALDEVSHH FDSVLDVKLK
ELMFDQGAIA KERLVQTKYT QPALFAFNYA VAKMWMEYGI EPAVMLGHSV GEIVSACLSG
LFTLKDAVRM TARRAEVMQS VKLDGAMLAV KATKEQVSNF IESFDDVGFA GFNGPKQTVI
SGGILSLDMI ADRLSEEEIP HRRLEVSHAF HSAHMNEAAE IFRDYMTTVT FHPLQREFIS
NVTGKVATYD LVASPDYWAR HICQPVNFAA GMETIATRSS YLFLETGPSP HLTAMGRGCI
KASDHYWVET VKPSLVEEDS LDEAILSLYK AGQKLDWRIV HAGVSNNMCE LPPYSFDHES
YWLPVATSGV DRGSDFHPLL GQLAARQHSQ WTFTAFVAPS SPAYLADHVV MGRTIFPGTG
YVEVVLALQD AVFGHTGMVM EDLEIHAPLI LADEASTELS TQLTYQKDGV YSVEISSVAQ
GENTVHFTCR MLEDPTLVSI VDLPDGSRDD EQSTFDKTIL YNRLASLGLQ YGEQFQRVRS
IRKDGVRRVF GTLSTENINS WEFVNPGLFD GVLHTLEPIL GADRTLVPVG WSKIRVYRKP
RGNVECVAEL RVDSDPFSSE VLADLTLYGD GLLVLRAEGL RLREVKSRER SSLPFFHRIV
WKEQPLDLQA FRAVRLIGIN CPDALKPHLS SHFELVADID KALDAIHTSQ GKPTKFVCFW
NGKELPADAD ADAIMAASQS FYEPLLAFIK ALAKLALKET VELVFVTKGV QTTGREDARA
GTEEPLSLNT QLQATISGFC SVLNSEFSRI RAKVVDLPCM GEDQDDVYSL LNELHLGNSR
SDFQVAYRCN SRMVKHLEVA KVIESEENYQ IVVADDGLLS GLGRKPLPRI VPSGDEIEVC
VEAAGLNFKD VLNALGLLKE HSKSEGLTHK ELPLGFECAG VVTAAGDDAE FMVGESVMIS
HLGCMQRYVT VSSRAAVRIP DGITMEQAAA IPTAFITSYY ALYSLAKVNA SDRVLIHAAA
GGVGQAALQL CRRVGAEVFA TASHRKWDVL RNQGVDRIMD SRNINFGEEI LRMTDGGGVS
VVLNSLNKDF IPVSLAATAH GGRFVELGKL GVWSKQQVTE VRPDISYSQF DLSEISENEL
LDLNKSILED IAAYLSAGEI TPPLVTSYSV TDIAEAFGVL SRGENVGKIV LTFGREQDSD
LSLSRVVSGE GTYVITGGYG ALGQRVARCL IQAGARNVTL LGRNLPNQDA LAQLKMRLDG
VENLDLCTGD VADSDVVDRI FVEAAEKGRP VCGIVHLAGL ISDAPITEQT WISFRTVFLP
KVVGTWNLWK AAERHGGVEL FAGFSSIASV VGSVSQSNYA SANAFIDGLM NRTRGGGRIG
LALNWGPWGG AGMAAELTDQ QRKSIERKGF SLIPMQLGME AFGRLARQAQ GQVVIGNVDW
SAYKESLPGD DSLYDDVKDA KSDAPSDVFD YNSLLALSED QRKEIVLEKL ILILRQVLQY
GEKERVSRRA TFSDLGIDSL VAVELRNTLE KSFGIALPSS LVFDYPSVPV LSGYLLEYLK
NNYVSTSGDG ENSDASSEMH KTSEEEDSTE GELI
//