BIOZ_RHOM4
ID BIOZ_RHOM4 Reviewed; 343 AA.
AC D0MCQ4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=Rmar_0105 {ECO:0000312|EMBL:ACY47014.1};
OS Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS obamensis).
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Rhodothermus.
OX NCBI_TaxID=518766;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43812 / DSM 4252 / R-10;
RX PubMed=21304669; DOI=10.4056/sigs.46736;
RA Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Detter J.C.;
RT "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL Stand. Genomic Sci. 1:283-291(2009).
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; CP001807; ACY47014.1; -; Genomic_DNA.
DR RefSeq; WP_012842626.1; NC_013501.1.
DR SMR; D0MCQ4; -.
DR STRING; 518766.Rmar_0105; -.
DR EnsemblBacteria; ACY47014; ACY47014; Rmar_0105.
DR KEGG; rmr:Rmar_0105; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_4_2_10; -.
DR OMA; LFGCPGW; -.
DR OrthoDB; 872193at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000002221; Chromosome.
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; Transferase.
FT CHAIN 1..343
FT /note="3-oxopimeloyl-[acyl-carrier-protein] synthase"
FT /id="PRO_0000453633"
FT REGION 273..277
FT /note="ACP-binding"
FT /evidence="ECO:0000250|UniProtKB:P0A6R0, ECO:0000255|HAMAP-
FT Rule:MF_02249"
FT ACT_SITE 132
FT /evidence="ECO:0000250|UniProtKB:Q7CTU0, ECO:0000255|HAMAP-
FT Rule:MF_02249"
FT ACT_SITE 272
FT /evidence="ECO:0000250|UniProtKB:Q7CTU0, ECO:0000255|HAMAP-
FT Rule:MF_02249"
FT ACT_SITE 302
FT /evidence="ECO:0000250|UniProtKB:Q7CTU0, ECO:0000255|HAMAP-
FT Rule:MF_02249"
SQ SEQUENCE 343 AA; 36075 MW; F4F4424F31E4A81E CRC64;
MLPEQSLTTP LPATATAAPA RRAAVLGVGA ALPAHREPST ETERRLGLPP GWIARRTGIR
ERPLVGPDEA TSDLAVRAGA AALAQAELSP ERIGLLLLAT STPDHLLPPT APVVAHRLGL
KHAGAVDLAG ACSGFLYALA LADGYVRLQR TCVLVIGANV LSRRTNPDDP KTSALFADGA
GAVVLGPSEG SRGIVACWLG ADGSCWDDLY IPAGGSRRPL TPERVARGEH LMYMKDGRAL
FRRAATGMAE AGRRVLQQAG LDLDDVAWWI PHQANHRLIE EARRQLGMPE ARTVNLVDRI
GNSSAATIPL ALALEAHRFA PGDLLLLTAV GAGLLSAAVL IQW
