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Database: UniProt
Entry: A0A1I5UFV8_9BACT
LinkDB: A0A1I5UFV8_9BACT
Original site: A0A1I5UFV8_9BACT 
ID   A0A1I5UFV8_9BACT        Unreviewed;       333 AA.
AC   A0A1I5UFV8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Beta-ketoacyl-[acyl-carrier-protein] synthase III {ECO:0000256|HAMAP-Rule:MF_01815};
DE            Short=Beta-ketoacyl-ACP synthase III {ECO:0000256|HAMAP-Rule:MF_01815};
DE            Short=KAS III {ECO:0000256|HAMAP-Rule:MF_01815};
DE            EC=2.3.1.180 {ECO:0000256|HAMAP-Rule:MF_01815};
DE   AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {ECO:0000256|HAMAP-Rule:MF_01815};
DE   AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III {ECO:0000256|HAMAP-Rule:MF_01815};
GN   Name=fabH {ECO:0000256|HAMAP-Rule:MF_01815};
GN   ORFNames=SAMN04515674_107160 {ECO:0000313|EMBL:SFP94164.1};
OS   Pseudarcicella hirudinis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Pseudarcicella.
OX   NCBI_TaxID=1079859 {ECO:0000313|EMBL:SFP94164.1, ECO:0000313|Proteomes:UP000199306};
RN   [1] {ECO:0000313|EMBL:SFP94164.1, ECO:0000313|Proteomes:UP000199306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E92,LMG 26720,CCM 7988 {ECO:0000313|Proteomes:UP000199306};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis
CC       by the addition to an acyl acceptor of two carbons from malonyl-ACP.
CC       Catalyzes the first condensation reaction which initiates fatty acid
CC       synthesis and may therefore play a role in governing the total rate of
CC       fatty acid production. Possesses both acetoacetyl-ACP synthase and
CC       acetyl transacylase activities. Its substrate specificity determines
CC       the biosynthesis of branched-chain and/or straight-chain of fatty
CC       acids. {ECO:0000256|HAMAP-Rule:MF_01815}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2
CC         + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-
CC         COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450;
CC         EC=2.3.1.180; Evidence={ECO:0000256|HAMAP-Rule:MF_01815};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP-
CC       Rule:MF_01815}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01815}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01815}.
CC   -!- DOMAIN: The last Arg residue of the ACP-binding site is essential for
CC       the weak association between ACP/AcpP and FabH. {ECO:0000256|HAMAP-
CC       Rule:MF_01815}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC       {ECO:0000256|HAMAP-Rule:MF_01815}.
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DR   EMBL; FOXH01000007; SFP94164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5UFV8; -.
DR   STRING; 1079859.SAMN04515674_107160; -.
DR   OrthoDB; 9815506at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000199306; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0033818; F:beta-ketoacyl-acyl-carrier-protein synthase III activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00830; KAS_III; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   HAMAP; MF_01815; FabH; 1.
DR   InterPro; IPR013747; ACP_syn_III_C.
DR   InterPro; IPR013751; ACP_syn_III_N.
DR   InterPro; IPR004655; FabH.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR00747; fabH; 1.
DR   PANTHER; PTHR34069; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 3; 1.
DR   PANTHER; PTHR34069:SF2; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 3; 1.
DR   Pfam; PF08545; ACP_syn_III; 1.
DR   Pfam; PF08541; ACP_syn_III_C; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01815};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01815};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW   Rule:MF_01815};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW   Rule:MF_01815};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_01815};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_01815}; Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01815};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199306};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01815}.
FT   DOMAIN          110..188
FT                   /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08545"
FT   DOMAIN          240..327
FT                   /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08541"
FT   REGION          257..261
FT                   /note="ACP-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT   ACT_SITE        256
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
SQ   SEQUENCE   333 AA;  36084 MW;  26F5F97E489983D0 CRC64;
     MNKTTAAITG VSGYVPEYVL TNAELEKIVD TNDEWIVSRT GIKERRILKG EGKGSSVMGA
     EAVKRLLEKT NTRPEDVDLL ICATVTPDYF FPATANLICA KVGIPESASY DLAAACSGFL
     NALVTGAMFI ESGRYKKVVV VGSDKMSSIV DYTDRTTCVL FGDGAGAVLL EPDADGLGIQ
     DFILKSDGNG ASHLIQKAGG SAYPPTHETI DSRLHFIHQE GQAVFKFAVT RMADVSAEIM
     ERNKLTGEDV AFLVPHQANK RIIDATAKRM GVGEEKVMLN IHKYGNTTAA TIPLCLWDYE
     DQLKKGDNLI LAAFGGGFTW GSIYLKWAYD PNK
//
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