BIOZ_AGRFC
ID BIOZ_AGRFC Reviewed; 328 AA.
AC Q7CTU0;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 87.
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, ECO:0000269|PubMed:33824341};
DE AltName: Full=3-ketoacyl-ACP synthase {ECO:0000303|PubMed:33154364};
DE AltName: Full=3-oxoacyl-(acyl-carrier-protein) synthase {ECO:0000305};
DE AltName: Full=Beta-ketoacyl-ACP synthase {ECO:0000303|PubMed:33824341};
GN Name=bioZ {ECO:0000255|HAMAP-Rule:MF_02249, ECO:0000303|PubMed:33154364};
GN Synonyms=fabH2 {ECO:0000303|PubMed:33824341};
GN OrderedLocusNames=Atu4001 {ECO:0000312|EMBL:AAK89424.2};
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF CYS-115.
RC STRAIN=C58 / ATCC 33970;
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, SUBUNIT, AND MUTAGENESIS OF ARG-39; CYS-115; ARG-153; ARG-221;
RP HIS-255; ARG-260 AND ASN-285.
RX PubMed=33824341; DOI=10.1038/s41467-021-22360-4;
RA Zhang S., Xu Y., Guan H., Cui T., Liao Y., Wei W., Li J., Hassan B.H.,
RA Zhang H., Jia X., Ouyang S., Feng Y.;
RT "Biochemical and structural characterization of the BioZ enzyme engaged in
RT bacterial biotin synthesis pathway.";
RL Nat. Commun. 12:2056-2056(2021).
CC -!- FUNCTION: Involved in the formation of the biotin precursor pimeloyl-
CC ACP (PubMed:33154364, PubMed:33824341). Catalyzes the condensation of
CC glutaryl-CoA, an intermediate in lysine degradation, with malonyl-ACP
CC to produce 3-oxopimeloyl-ACP (PubMed:33154364, PubMed:33824341).
CC {ECO:0000269|PubMed:33154364, ECO:0000269|PubMed:33824341}.
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, ECO:0000269|PubMed:33824341};
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, ECO:0000269|PubMed:33824341};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02249, ECO:0000269|PubMed:33154364,
CC ECO:0000269|PubMed:33824341}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:33824341}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene leads to biotin
CC auxotrophy. {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; AE007870; AAK89424.2; -; Genomic_DNA.
DR RefSeq; NP_356639.2; NC_003063.2.
DR RefSeq; WP_010973495.1; NC_003063.2.
DR PDB; 6KUE; X-ray; 1.99 A; A/B=1-328.
DR PDBsum; 6KUE; -.
DR SMR; Q7CTU0; -.
DR STRING; 176299.Atu4001; -.
DR EnsemblBacteria; AAK89424; AAK89424; Atu4001.
DR GeneID; 66224255; -.
DR KEGG; atu:Atu4001; -.
DR PATRIC; fig|176299.10.peg.3820; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_4_2_5; -.
DR OMA; IDLAGAC; -.
DR PhylomeDB; Q7CTU0; -.
DR BioCyc; AGRO:ATU4001-MON; -.
DR BioCyc; MetaCyc:ATU4001-MON; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000000813; Chromosome linear.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
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 3D-structure; Acyltransferase; Biotin biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..328
FT /note="3-oxopimeloyl-[acyl-carrier-protein] synthase"
FT /id="PRO_0000453630"
FT REGION 256..260
FT /note="ACP-binding"
FT /evidence="ECO:0000250|UniProtKB:P0A6R0, ECO:0000255|HAMAP-
FT Rule:MF_02249"
FT ACT_SITE 115
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02249,
FT ECO:0000305|PubMed:33824341"
FT ACT_SITE 255
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02249,
FT ECO:0000305|PubMed:33824341"
FT ACT_SITE 285
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02249,
FT ECO:0000305|PubMed:33824341"
FT MUTAGEN 39
FT /note="R->A: No change in activity. Loss of activity; when
FT associated with A-153; A-221 and A-260."
FT /evidence="ECO:0000269|PubMed:33824341"
FT MUTAGEN 115
FT /note="C->A: Loss of activity. Binds modestly malonyl-ACP.
FT Increases binding to glutaryl-ACP."
FT /evidence="ECO:0000269|PubMed:33824341"
FT MUTAGEN 115
FT /note="C->S: Loss of activity. Biotin auxotroph."
FT /evidence="ECO:0000269|PubMed:33154364"
FT MUTAGEN 153
FT /note="R->A: No change in activity. Loss of activity; when
FT associated with A-39; A-221 and A-260."
FT /evidence="ECO:0000269|PubMed:33824341"
FT MUTAGEN 221
FT /note="R->A: No change in activity. Loss of activity; when
FT associated with A-39; A-153 and A-260."
FT /evidence="ECO:0000269|PubMed:33824341"
FT MUTAGEN 255
FT /note="H->A: Retains low activity."
FT /evidence="ECO:0000269|PubMed:33824341"
FT MUTAGEN 260
FT /note="R->A: Exhibits poor activity. Loss of activity; when
FT associated with A-39; A-153 and A-221."
FT /evidence="ECO:0000269|PubMed:33824341"
FT MUTAGEN 285
FT /note="N->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:33824341"
SQ SEQUENCE 328 AA; 34135 MW; 34773BBBC35A971D CRC64;
MQTRSSRMAG FGHAVPARCV DNAEIEASLG LEAGWIERRT GIRSRYWAEA GDTLSGLAER
AGRMALEDAK INADDIALTL LATSTPDHLL PPSAPLLAHR LGLTRSGAID LAGACSGFLY
ALTLADGFVR TYGRAVLVVA ANILSRRINP AERASAVLFA DAAGAVVLTP CPEVKRGVLS
ADLVADGSGY DLIQIAAGGS SQPFSAGMIA EDALMTMRDG REVFSRAVAL MTNTSQRVLH
EAELTAADIS RFVPHQANAR MSDAVCGNLG IEREKTVRTI GSFGNSSAAT IPLSLSITNA
ERPLAGGETL LLTAAGAGMT GGAVVYRV
