FABH_NEIMF
ID FABH_NEIMF Reviewed; 320 AA.
AC A1KRY9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=NMC0307;
OS Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS 15464 / FAM18).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=272831;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT "Meningococcal genetic variation mechanisms viewed through comparative
RT analysis of serogroup C strain FAM18.";
RL PLoS Genet. 3:230-240(2007).
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; AM421808; CAM09618.1; -; Genomic_DNA.
DR RefSeq; WP_002218026.1; NC_008767.1.
DR PDB; 4RYB; X-ray; 2.45 A; A/B=1-320.
DR PDBsum; 4RYB; -.
DR AlphaFoldDB; A1KRY9; -.
DR SMR; A1KRY9; -.
DR EnsemblBacteria; CAM09618; CAM09618; NMC0307.
DR KEGG; nmc:NMC0307; -.
DR HOGENOM; CLU_039592_4_1_4; -.
DR OMA; WGSEGDK; -.
DR OrthoDB; 872193at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002286; Chromosome.
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..320
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT /id="PRO_1000056382"
FT REGION 248..252
FT /note="ACP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 114
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 247
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 277
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:4RYB"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:4RYB"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:4RYB"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:4RYB"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:4RYB"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:4RYB"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:4RYB"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:4RYB"
FT STRAND 161..173
FT /evidence="ECO:0007829|PDB:4RYB"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 185..190
FT /evidence="ECO:0007829|PDB:4RYB"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:4RYB"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:4RYB"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 212..234
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:4RYB"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:4RYB"
FT HELIX 282..292
FT /evidence="ECO:0007829|PDB:4RYB"
FT STRAND 301..308
FT /evidence="ECO:0007829|PDB:4RYB"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:4RYB"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:4RYB"
SQ SEQUENCE 320 AA; 33819 MW; 4247A007A4BAB9B1 CRC64;
MQYAKISGTG SYLPANRVSN DDLAQKVDTS DEWITARTGI KFRHIAAENE KTSDLAAEAA
RRALDAAGLD SGEIDLIIVA TATPDMQFPS TATIVQQKLG ITNGCPAFDV QAVCAGFMYA
LTTANAYIKS GMAKNALVIG AETFSRIVDW NDRTTCVLFG DGAGAVVLSA ADKPGIIHSK
LKADGNYLKL LNVPGQIACG KVSGSPYISM DGPGVFKFAV KMLSKIADDV IEEAGYTAAQ
IDWIVPHQAN RRIIESTAKH LGLSMDKVVL TVQDHGNTSA ASIPLALDTG IRSGQIKRGQ
NLLLEGIGGG FAWGAVLLQY
