ID Q982F9_RHILO Unreviewed; 327 AA.
AC Q982F9;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=3-oxopimeloyl-[acyl-carrier-protein] synthase {ECO:0000256|HAMAP-Rule:MF_02249};
DE Short=3-oxopimeloyl-[ACP] synthase {ECO:0000256|HAMAP-Rule:MF_02249};
DE EC=2.3.1.- {ECO:0000256|HAMAP-Rule:MF_02249};
GN Name=bioZ {ECO:0000256|HAMAP-Rule:MF_02249};
GN OrderedLocusNames=mll9094 {ECO:0000313|EMBL:BAB54500.1};
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OG Plasmid pMLa {ECO:0000313|EMBL:BAB54500.1,
OG ECO:0000313|Proteomes:UP000000552}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB54500.1, ECO:0000313|Proteomes:UP000000552};
RN [1] {ECO:0000313|EMBL:BAB54500.1, ECO:0000313|Proteomes:UP000000552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC {ECO:0000313|Proteomes:UP000000552};
RC PLASMID=pMLa {ECO:0000313|EMBL:BAB54500.1,
RC ECO:0000313|Proteomes:UP000000552};
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
CC -!- FUNCTION: Involved in the formation of the biotin precursor pimeloyl-
CC ACP. Catalyzes the condensation of glutaryl-CoA, an intermediate in
CC lysine degradation, with malonyl-ACP to produce 3-oxopimeloyl-ACP.
CC {ECO:0000256|HAMAP-Rule:MF_02249}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 +
CC CoA; Xref=Rhea:RHEA:44448, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9916,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02249};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutaryl-CoA + H(+) + malonyl-[ACP] = 3-oxo-6-carboxyhexanoyl-
CC [ACP] + CO2 + CoA; Xref=Rhea:RHEA:67904, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:17387, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57378, ChEBI:CHEBI:78449,
CC ChEBI:CHEBI:176519; Evidence={ECO:0000256|HAMAP-Rule:MF_02249};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02249}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. BioZ family.
CC {ECO:0000256|HAMAP-Rule:MF_02249}.
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DR EMBL; BA000013; BAB54500.1; -; Genomic_DNA.
DR RefSeq; WP_010916034.1; NC_002679.1.
DR AlphaFoldDB; Q982F9; -.
DR KEGG; mlo:mll9094; -.
DR PATRIC; fig|266835.9.peg.6921; -.
DR HOGENOM; CLU_039592_3_1_5; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000000552; Plasmid pMLa.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00830; KAS_III; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR HAMAP; MF_02249; BioZ; 1.
DR InterPro; IPR013747; ACP_syn_III_C.
DR InterPro; IPR013751; ACP_syn_III_N.
DR InterPro; IPR046403; BioZ.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR34069; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 3; 1.
DR PANTHER; PTHR34069:SF2; BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE III; 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_02249};
KW Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_02249};
KW Plasmid {ECO:0000313|EMBL:BAB54500.1};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02249}.
FT DOMAIN 109..186
FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08545"
FT DOMAIN 238..325
FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08541"
FT REGION 255..259
FT /note="ACP-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02249"
FT ACT_SITE 114
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02249"
FT ACT_SITE 254
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02249"
FT ACT_SITE 284
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02249"
SQ SEQUENCE 327 AA; 33988 MW; 4CE00A9BED88CF72 CRC64;
MSKSSRILGF GHHAPGRKVE NAEIENNLGL EPGWIERRTG IRSRFWATDE DTLSGLAAQA
GDMALANAGI DQSDIGLLLL ATSTPDHLLP PSAPLVAHNL GVGRAGAVDL TAACAGFIYA
LMFADGFTRL HGKPALVIAA NILSRRINPA ERASAVLFAD AAGALVIGPC EDPERGILGA
SVDSDGSRYG LIQIPAGGSN TPFHSDLDLA QTRMTITDGR EVFSKAVEMM TACSQDALAA
ARMRPQDIDR FVPHQANSRI FDAVGRSLGI ADQAIVKTIA NYGNSSAATI PLSLSLANQT
EPFRSGEKIL LAAAGAGLSG GALVVGI
//
