ID V8G8S9_9BURK Unreviewed; 484 AA.
AC V8G8S9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00336, ECO:0000256|HAMAP-Rule:MF_00835};
DE Includes:
DE RecName: Full=ATP-dependent dethiobiotin synthetase BioD {ECO:0000256|HAMAP-Rule:MF_00336};
DE EC=6.3.3.3 {ECO:0000256|HAMAP-Rule:MF_00336};
DE AltName: Full=DTB synthetase {ECO:0000256|HAMAP-Rule:MF_00336};
DE AltName: Full=Dethiobiotin synthase {ECO:0000256|HAMAP-Rule:MF_00336};
DE Short=DTBS {ECO:0000256|HAMAP-Rule:MF_00336};
DE Includes:
DE RecName: Full=Malonyl-[acyl-carrier protein] O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00835};
DE Short=Malonyl-ACP O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00835};
DE EC=2.1.1.197 {ECO:0000256|HAMAP-Rule:MF_00835};
DE AltName: Full=Biotin synthesis protein BioC {ECO:0000256|HAMAP-Rule:MF_00835};
GN Name=bioC {ECO:0000256|HAMAP-Rule:MF_00835};
GN Synonyms=bioD {ECO:0000256|HAMAP-Rule:MF_00336};
GN ORFNames=V757_01340 {ECO:0000313|EMBL:ETD72944.1};
OS Pelistega indica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pelistega.
OX NCBI_TaxID=1414851 {ECO:0000313|EMBL:ETD72944.1, ECO:0000313|Proteomes:UP000018766};
RN [1] {ECO:0000313|EMBL:ETD72944.1, ECO:0000313|Proteomes:UP000018766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HM-7 {ECO:0000313|EMBL:ETD72944.1,
RC ECO:0000313|Proteomes:UP000018766};
RA Kumbhare S.V., Shetty S.A., Sharma O., Dhotre D.P.;
RT "Genomic analysis of Pelistega sp. HM-7.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP-
CC dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-
CC diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to
CC form a ureido ring. {ECO:0000256|HAMAP-Rule:MF_00336}.
CC -!- FUNCTION: Converts the free carboxyl group of a malonyl-thioester to
CC its methyl ester by transfer of a methyl group from S-adenosyl-L-
CC methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty
CC acid synthetic pathway. {ECO:0000256|HAMAP-Rule:MF_00835}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-
CC dethiobiotin + ADP + 3 H(+) + phosphate; Xref=Rhea:RHEA:15805,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:149469, ChEBI:CHEBI:149473,
CC ChEBI:CHEBI:456216; EC=6.3.3.3; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00336};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl
CC ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17105, Rhea:RHEA-
CC COMP:9623, Rhea:RHEA-COMP:9954, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78845; EC=2.1.1.197;
CC Evidence={ECO:0000256|ARBA:ARBA00000852, ECO:0000256|HAMAP-
CC Rule:MF_00835};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00336};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC diaminononanoate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00336}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00336}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336}.
CC -!- SIMILARITY: Belongs to the dethiobiotin synthetase family.
CC {ECO:0000256|HAMAP-Rule:MF_00336}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00835}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00336}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETD72944.1}.
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DR EMBL; AYSV01000008; ETD72944.1; -; Genomic_DNA.
DR AlphaFoldDB; V8G8S9; -.
DR OrthoDB; 9802097at2; -.
DR UniPathway; UPA00078; UER00161.
DR Proteomes; UP000018766; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010340; F:carboxyl-O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004141; F:dethiobiotin synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0102130; F:malonyl-CoA methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd03109; DTBS; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00835; BioC; 1.
DR HAMAP; MF_00336; BioD; 1.
DR InterPro; IPR011814; BioC.
DR InterPro; IPR004472; DTB_synth_BioD.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR02072; BioC; 1.
DR NCBIfam; TIGR00347; bioD; 1.
DR PANTHER; PTHR43210:SF2; ATP-DEPENDENT DETHIOBIOTIN SYNTHETASE BIOD 2; 1.
DR PANTHER; PTHR43210; DETHIOBIOTIN SYNTHETASE; 1.
DR Pfam; PF13500; AAA_26; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00336};
KW Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00336};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00336};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00336};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00336};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00336};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00835};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00336};
KW Reference proteome {ECO:0000313|Proteomes:UP000018766};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00835};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00835}.
FT DOMAIN 49..141
FT /note="Methyltransferase type 11"
FT /evidence="ECO:0000259|Pfam:PF08241"
FT ACT_SITE 288
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 263..268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 365..368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 365
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 425..426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
FT BINDING 451..453
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00336"
SQ SEQUENCE 484 AA; 55704 MW; BFEAF98B10B9B6DF CRC64;
MIDKNLVRLR FSQACSSYDH NAFAQQRINH TLITLLKQYA GDQFNQVFEI GCGTGLLTQM
MYKNLTINHW ILNDLCSMQA YIKTKLPSID FTFIEGDIEH IPFPPHNQLI ASASTVQWLN
QPQHFLKKCA QHLQTNGYLL IGTFTQNNLK EIKTLTHIGL NYPDISDWRT WLEEDFQLLL
CQHEDWILPF ESPLHILQHL KFTGVSGIQK NLWTGTKLRQ FIADYQYHFR LSSGEVSLSY
SPLFLLARKK MKQVIFISGI DTDVGKTIAT AWYAKKLMLQ GKKVITQKFV QTGCKTYSDD
IMKHRQLQGI TVTEEDLAGI TCPYVFEFPC SPHLAAKLEN KKINENLITQ STQRLLETYD
IVLLEGAGGL YVPYNDQDTI IDYIQKQQYP LILVTSGKLG SINHTLLSLQ ACAQRQIPLH
SVIYNRFPEG DSIISQDTLS FLRNYLQTYF PETQFTTMEK MTISDQSMPK ILFSNQNYVK
KNLA
//
