BIOZ_RHILI
ID BIOZ_RHILI Reviewed; 327 AA.
AC Q9EYU2;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=3-oxopimeloyl-[acyl-carrier-protein] synthase {ECO:0000250|UniProtKB:Q7CTU0, ECO:0000255|HAMAP-Rule:MF_02249};
DE Short=3-oxopimeloyl-[ACP] synthase {ECO:0000250|UniProtKB:Q7CTU0, ECO:0000255|HAMAP-Rule:MF_02249};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q7CTU0, ECO:0000255|HAMAP-Rule:MF_02249};
GN Name=bioZ {ECO:0000255|HAMAP-Rule:MF_02249, ECO:0000303|PubMed:11320134};
OS Rhizobium loti (Mesorhizobium loti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=381;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=R7A;
RX PubMed=11320134; DOI=10.1099/00221287-147-5-1315;
RA Sullivan J.T., Brown S.D., Yocum R.R., Ronson C.W.;
RT "The bio operon on the acquired symbiosis island of Mesorhizobium sp.
RT strain R7A includes a novel gene involved in pimeloyl-CoA synthesis.";
RL Microbiology 147:1315-1322(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R7A;
RX PubMed=12003951; DOI=10.1128/jb.184.11.3086-3095.2002;
RA Sullivan J.T., Trzebiatowski J.R., Cruickshank R.W., Gouzy J., Brown S.D.,
RA Elliot R.M., Fleetwood D.J., McCallum N.G., Rossbach U., Stuart G.S.,
RA Weaver J.E., Webby R.J., de Bruijn F.J., Ronson C.W.;
RT "Comparative sequence analysis of the symbiosis island of Mesorhizobium
RT loti strain R7A.";
RL J. Bacteriol. 184:3086-3095(2002).
CC -!- FUNCTION: Involved in the formation of the biotin precursor pimeloyl-
CC ACP (Probable). Catalyzes the condensation of glutaryl-CoA, an
CC intermediate in lysine degradation, with malonyl-ACP to produce 3-
CC oxopimeloyl-ACP (By similarity). {ECO:0000250|UniProtKB:Q7CTU0,
CC ECO:0000305|PubMed:11320134}.
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:0000250|UniProtKB:Q7CTU0, ECO:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_02249};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02249, ECO:0000269|PubMed:11320134}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene leads to biotin
CC auxotrophy. {ECO:0000269|PubMed:11320134}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. BioZ family.
CC {ECO:0000255|HAMAP-Rule:MF_02249, ECO:0000305}.
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DR EMBL; AF311738; AAG47795.1; -; Genomic_DNA.
DR EMBL; AL672114; CAD31403.1; -; Genomic_DNA.
DR RefSeq; WP_027033150.1; NZ_CP051772.1.
DR SMR; Q9EYU2; -.
DR GeneID; 66686421; -.
DR UniPathway; UPA00078; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IGI:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.47.10; -; 1.
DR HAMAP; MF_02249; BioZ; 1.
DR InterPro; IPR013751; ACP_syn_III.
DR InterPro; IPR013747; ACP_syn_III_C.
DR InterPro; IPR046403; BioZ.
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.
PE 3: Inferred from homology;
KW Acyltransferase; Biotin biosynthesis; Transferase.
FT CHAIN 1..327
FT /note="3-oxopimeloyl-[acyl-carrier-protein] synthase"
FT /id="PRO_0000453632"
FT REGION 255..259
FT /note="ACP-binding"
FT /evidence="ECO:0000250|UniProtKB:P0A6R0, ECO:0000255|HAMAP-
FT Rule:MF_02249"
FT ACT_SITE 114
FT /evidence="ECO:0000250|UniProtKB:Q7CTU0, ECO:0000255|HAMAP-
FT Rule:MF_02249"
FT ACT_SITE 254
FT /evidence="ECO:0000250|UniProtKB:Q7CTU0, ECO:0000255|HAMAP-
FT Rule:MF_02249"
FT ACT_SITE 284
FT /evidence="ECO:0000250|UniProtKB:Q7CTU0, ECO:0000255|HAMAP-
FT Rule:MF_02249"
SQ SEQUENCE 327 AA; 33967 MW; EA6FCA0E7C2AA794 CRC64;
MSRSSRVLGF GHHAPSRKVE NPEIENRLGL EPGWIERRTG IRSRFWATDQ DTLSGLATQA
GDMALANAGI DRSDIGLLLL ATSTPDHLLP PSAPLVAHKL GLGRAGAVDL TGACAGFIYA
LMFADGFTRL HGKASLVIAA NILSRRINPA ERASSVLFAD AAGALVIGAC EDPDLGILGA
SVDSDGSRYG LIQIPAGGSS IPFHDDLDLG QTRMTMTDGR EVFAKAVEMM TDCSTSALAV
AGVRPQDIDR FVPHQANARI FDAVGRNLGI ADEAIVKTIA EYGNSSAATI PLSLSLAHRA
APFRPGEKVL LAAAGAGLSG GAIVVGI
