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Database: UniProt
Entry: A0A0P7ZNL6_9GAMM
LinkDB: A0A0P7ZNL6_9GAMM
Original site: A0A0P7ZNL6_9GAMM 
ID   A0A0P7ZNL6_9GAMM        Unreviewed;       319 AA.
AC   A0A0P7ZNL6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   ECO:0000313|EMBL:KPQ03895.1};
GN   ORFNames=HLUCCO02_02760 {ECO:0000313|EMBL:KPQ03895.1};
OS   Idiomarinaceae bacterium HL-53.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae.
OX   NCBI_TaxID=1298881 {ECO:0000313|EMBL:KPQ03895.1, ECO:0000313|Proteomes:UP000053932};
RN   [1] {ECO:0000313|EMBL:KPQ03895.1, ECO:0000313|Proteomes:UP000053932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-53 {ECO:0000313|EMBL:KPQ03895.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (AUG-2015) 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:KPQ03895.1}.
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DR   EMBL; LIHO01000009; KPQ03895.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7ZNL6; -.
DR   STRING; 1298881.Ga0003345_1923; -.
DR   PATRIC; fig|1298881.4.peg.523; -.
DR   OrthoDB; 9815506at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000053932; 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|HAMAP-Rule:MF_01815,
KW   ECO:0000313|EMBL:KPQ03895.1}; 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}; Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01815};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01815}.
FT   DOMAIN          106..182
FT                   /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08545"
FT   DOMAIN          230..319
FT                   /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08541"
FT   REGION          247..251
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        246
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT   ACT_SITE        276
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
SQ   SEQUENCE   319 AA;  34227 MW;  50899BC881F6A219 CRC64;
     MYSKIAGTGH YLPAQVLSNQ DLERRVDTSD QWIRERTGIR ERRIAEKHEN VVSMAVAAGK
     DALESAKLDA AQLNMIIVAT TSADKAFPSA ACEVQAALGA KHAAAFDVAA ACAGFMFAMS
     VADQYIKTGM ARHVLIVGSD VLSRLCNPDD RNTIVLFGDG AGAAVLSASA TQGVLSTHIY
     CAGEYAELLG ADLPSRHPDP IEEQAWLYMK GSEVFKVAVQ KLSELVNTTL KQHEIAASEL
     DWLVPHQANY RIIQATAKKL SMPMERVVMT LEQTGNTSAA SVPIALDCAI KDGRIQPGHL
     LLLEAFGGGF AWGSALVKY
//
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