ID   BIOZ_BRUA2              Reviewed;         326 AA.
AC   Q2YKB4;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=3-oxopimeloyl-[acyl-carrier-protein] synthase {ECO:0000255|HAMAP-Rule:MF_02249, ECO:0000305};
DE            Short=3-oxopimeloyl-[ACP] synthase {ECO:0000255|HAMAP-Rule:MF_02249, ECO:0000305};
DE            EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_02249, ECO:0000269|PubMed:33154364};
GN   Name=bioZ {ECO:0000255|HAMAP-Rule:MF_02249};
GN   OrderedLocusNames=BAB2_0748 {ECO:0000312|EMBL:CAJ12914.1};
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=33154364; DOI=10.1038/s41467-020-19251-5;
RA   Hu Y., Cronan J.E.;
RT   "Alpha-proteobacteria synthesize biotin precursor pimeloyl-ACP using BioZ
RT   3-ketoacyl-ACP synthase and lysine catabolism.";
RL   Nat. Commun. 11:5598-5598(2020).
CC   -!- FUNCTION: Involved in the formation of the biotin precursor pimeloyl-
CC       ACP (PubMed:33154364). Catalyzes the condensation of glutaryl-CoA, an
CC       intermediate in lysine degradation, with malonyl-ACP to produce 3-
CC       oxopimeloyl-ACP (PubMed:33154364). {ECO:0000269|PubMed:33154364}.
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:0000255|HAMAP-Rule:MF_02249,
CC         ECO:0000269|PubMed:33154364};
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         ECO:0000269|PubMed:33154364};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02249, ECO:0000269|PubMed:33154364}.
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; AM040265; CAJ12914.1; -; Genomic_DNA.
DR   RefSeq; WP_002966140.1; NZ_KN046823.1.
DR   SMR; Q2YKB4; -.
DR   STRING; 359391.BAB2_0748; -.
DR   EnsemblBacteria; CAJ12914; CAJ12914; BAB2_0748.
DR   GeneID; 45053535; -.
DR   GeneID; 55592170; -.
DR   KEGG; bmf:BAB2_0748; -.
DR   PATRIC; fig|359391.11.peg.441; -.
DR   HOGENOM; CLU_039592_4_2_5; -.
DR   OMA; IDLAGAC; -.
DR   PhylomeDB; Q2YKB4; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000002719; Chromosome II.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
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   1: Evidence at protein level;
KW   Acyltransferase; Biotin biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..326
FT                   /note="3-oxopimeloyl-[acyl-carrier-protein] synthase"
FT                   /id="PRO_0000453631"
FT   REGION          254..258
FT                   /note="ACP-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6R0, ECO:0000255|HAMAP-
FT                   Rule:MF_02249"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000250|UniProtKB:Q7CTU0, ECO:0000255|HAMAP-
FT                   Rule:MF_02249"
FT   ACT_SITE        253
FT                   /evidence="ECO:0000250|UniProtKB:Q7CTU0, ECO:0000255|HAMAP-
FT                   Rule:MF_02249"
FT   ACT_SITE        283
FT                   /evidence="ECO:0000250|UniProtKB:Q7CTU0, ECO:0000255|HAMAP-
FT                   Rule:MF_02249"
SQ   SEQUENCE   326 AA;  34341 MW;  2A46199531D72376 CRC64;
     MTVCSSRLAG FGHAVPDRRV ENAEIEAQLG LETGWIERRT GIRCRRWAMP DETLSHLAAS
     AADMALSDAG IERSDIALTL LATSTPDHLL PPTAPLLTHW LNLQNSGAAD LAGACTGFLY
     ALVLADGFVR AQGKPVLVVA ANLLSRRINM AERASAVLFG DAAGAVVLAP SAKANSFQSQ
     FITNGSHYDL IKVPAGGSAR AYAPERDASE FLMTMQDGRA VFTEAVRIMS GASQNVLASA
     AMLPQAIDRF FPHQANIRIV DKVCETIGVP RAKAASTLET YGNSSAATIP LSLSLANLEQ
     PLREGERLLF AAAGAGMTGG AVLMQV