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Database: UniProt
Entry: A0A428J3R7_9BACI
LinkDB: A0A428J3R7_9BACI
Original site: A0A428J3R7_9BACI 
ID   A0A428J3R7_9BACI        Unreviewed;       312 AA.
AC   A0A428J3R7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-SEP-2023, entry version 13.
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=EJF36_06085 {ECO:0000313|EMBL:RSK26462.1};
OS   Bacillus sp. HMF5848.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2495421 {ECO:0000313|EMBL:RSK26462.1, ECO:0000313|Proteomes:UP000274811};
RN   [1] {ECO:0000313|EMBL:RSK26462.1, ECO:0000313|Proteomes:UP000274811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMF5848 {ECO:0000313|EMBL:RSK26462.1,
RC   ECO:0000313|Proteomes:UP000274811};
RA   Kang H., Kang J., Cha I., Kim H., Joh K.;
RT   "Bacillus sp. HMF5848 Genome sequencing and assembly.";
RL   Submitted (DEC-2018) 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|ARBA:ARBA00008642, ECO:0000256|HAMAP-Rule:MF_01815}.
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:RSK26462.1}.
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DR   EMBL; RWIV01000001; RSK26462.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428J3R7; -.
DR   OrthoDB; 9815506at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000274811; 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; PTHR43091; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE; 1.
DR   PANTHER; PTHR43091:SF1; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE III, CHLOROPLASTIC; 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|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_01815}; Cytoplasm {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};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_01815}; Reference proteome {ECO:0000313|Proteomes:UP000274811};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01815}.
FT   DOMAIN          106..184
FT                   /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08545"
FT   DOMAIN          221..310
FT                   /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08541"
FT   REGION          238..242
FT                   /note="ACP-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT   ACT_SITE        112
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT   ACT_SITE        237
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
SQ   SEQUENCE   312 AA;  33971 MW;  D88D22EA58BAD98F CRC64;
     MNAGILGIAK YVPETVVTNV DLEKRMDTSD EWIRTRTGIE QRRIAEKSID TSDMAYFAAK
     QAIENANLTA EDIDMILVAT VTPDQPFPSV ACMLQDKLGA KKVAAMDISA ACAGFMYGMV
     TAKQFIETGT YKHVLVVGVE KLSKITDWND RNTAVLFGDG AGAAVLGPVS GDRGILSFEL
     GSDGSGGKHL YQTEEDVIFM NGREVFKFAV RQMGESSVNV IEKAGLKKED VDFLVPHQAN
     IRIMESARER LNLPIEKMSK TVHKYGNTSA ASIPISIVEE LEEGKINDDD VIVMVGFGGG
     LTWGAIALRW GR
//
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