FABH_STRZP
ID FABH_STRZP Reviewed; 324 AA.
AC C1CIR8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {ECO:0000255|HAMAP-Rule:MF_01815};
DE EC=2.3.1.180 {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=Beta-ketoacyl-ACP synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
DE Short=KAS III {ECO:0000255|HAMAP-Rule:MF_01815};
GN Name=fabH {ECO:0000255|HAMAP-Rule:MF_01815}; OrderedLocusNames=SPP_0448;
OS Streptococcus pneumoniae (strain P1031).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=488223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1031;
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
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:0000255|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:0000255|HAMAP-Rule:MF_01815};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_01815}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01815}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_01815}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC {ECO:0000255|HAMAP-Rule:MF_01815}.
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DR EMBL; CP000920; ACO20732.1; -; Genomic_DNA.
DR RefSeq; WP_000852956.1; NC_012467.1.
DR PDB; 5BQS; X-ray; 1.90 A; A/B=2-324.
DR PDBsum; 5BQS; -.
DR AlphaFoldDB; C1CIR8; -.
DR SMR; C1CIR8; -.
DR KEGG; spp:SPP_0448; -.
DR HOGENOM; CLU_039592_4_1_9; -.
DR OMA; WGSEGDK; -.
DR UniPathway; UPA00094; -.
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 Gene3D; 3.40.47.10; -; 1.
DR HAMAP; MF_01815; FabH; 1.
DR InterPro; IPR013751; ACP_syn_III.
DR InterPro; IPR013747; ACP_syn_III_C.
DR InterPro; IPR004655; FabH_synth.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF08545; ACP_syn_III; 1.
DR Pfam; PF08541; ACP_syn_III_C; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR TIGRFAMs; TIGR00747; fabH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW Multifunctional enzyme; Transferase.
FT CHAIN 1..324
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT /id="PRO_1000187905"
FT REGION 250..254
FT /note="ACP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 112
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 249
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 279
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:5BQS"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:5BQS"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:5BQS"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:5BQS"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:5BQS"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:5BQS"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:5BQS"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:5BQS"
FT STRAND 159..171
FT /evidence="ECO:0007829|PDB:5BQS"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:5BQS"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 224..235
FT /evidence="ECO:0007829|PDB:5BQS"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:5BQS"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 253..263
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:5BQS"
FT HELIX 284..294
FT /evidence="ECO:0007829|PDB:5BQS"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:5BQS"
FT STRAND 304..312
FT /evidence="ECO:0007829|PDB:5BQS"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:5BQS"
FT STRAND 316..324
FT /evidence="ECO:0007829|PDB:5BQS"
SQ SEQUENCE 324 AA; 34903 MW; 53E0BF125B3A9A70 CRC64;
MAFAKISQVA HYVPEQVVTN HDLAQIMDTN DEWISSRTGI RQRHISRTES TSDLATEVAK
KLMAKAGITG KELDFIILAT ITPDSMMPST AARVQANIGA NKAFAFDLTA ACSGFVFALS
TAEKFIASGR FQKGLVIGSE TLSKAVDWSD RSTAVLFGDG AGGVLLEASE QEHFLAESLN
SDGSRSECLT YGHSGLHSPF SDQESADSFL KMDGRTVFDF AIRDVAKSIK QTIDESPIEV
TDLDYLLLHQ ANDRILDKMA RKIGVDRAKL PANMMEYGNT SAASIPILLS ECVEQGLIPL
DGSQTVLLSG FGGGLTWGTL ILTI
