ID A0A3S1APP2_CHLFR Unreviewed; 340 AA.
AC A0A3S1APP2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=(S)-8-amino-7-oxononanoate synthase BioU {ECO:0000256|HAMAP-Rule:MF_00852};
DE EC=2.6.1.121 {ECO:0000256|HAMAP-Rule:MF_00852};
DE AltName: Full=8-amino-7-oxononanoate carboxylating dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00852};
GN Name=bioU {ECO:0000256|HAMAP-Rule:MF_00852};
GN ORFNames=PCC6912_03190 {ECO:0000313|EMBL:RUR86876.1};
OS Chlorogloeopsis fritschii PCC 6912.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Chlorogloeopsidaceae;
OC Chlorogloeopsis.
OX NCBI_TaxID=211165 {ECO:0000313|EMBL:RUR86876.1, ECO:0000313|Proteomes:UP000268857};
RN [1] {ECO:0000313|EMBL:RUR86876.1, ECO:0000313|Proteomes:UP000268857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6912 {ECO:0000313|EMBL:RUR86876.1,
RC ECO:0000313|Proteomes:UP000268857};
RX PubMed=30590650;
RA Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA Neumann-Schaal M., Petersen J.;
RT "Day and night: Metabolic profiles and evolutionary relationships of six
RT axenic non-marine cyanobacteria.";
RL Genome Biol. Evol. 0:0-0(2018).
CC -!- FUNCTION: A 'suicide' enzyme that participates in biotin synthesis.
CC Catalyzes the formation of (S)-8-amino-7-oxononanoate (DAN-carbamic
CC acid) from (7R,8S)-8-amino-7-(carboxyamino)nonanoate (DAN), a function
CC equivalent to the cannonical BioA reaction and the first half-reaction
CC of BioD. The cellular requirement for biotin is thought be low enough
CC that this single turnover enzyme supplies a sufficient amount of the
CC cofactor. Overall it catalyzes three reactions: formation of a covalent
CC linkage with 8-amino-7-oxononanoate to yield a BioU-DAN conjugate at
CC the epsilon-amino group of Lys124 of BioU using NAD(P)H, carboxylation
CC of the conjugate to form BioU-DAN-carbamic acid, and release of DAN-
CC carbamic acid using NAD(P)+. {ECO:0000256|HAMAP-Rule:MF_00852}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-8-amino-7-oxononanoate + CO2 + L-lysyl-[protein] =
CC (7R,8S)-8-amino-7-(carboxyamino)nonanoate + (S)-2-amino-6-
CC oxohexanoyl-[protein] + 2 H(+); Xref=Rhea:RHEA:63660, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803,
CC ChEBI:CHEBI:149468, ChEBI:CHEBI:149470; EC=2.6.1.121;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00852};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-8-amino-7-oxononanoate + H(+) + L-lysyl-[protein] + NADH
CC = H2O + N(6)-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein]
CC + NAD(+); Xref=Rhea:RHEA:63672, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:16405, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:149468,
CC ChEBI:CHEBI:149472; Evidence={ECO:0000256|HAMAP-Rule:MF_00852};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-8-amino-7-oxononanoate + H(+) + L-lysyl-[protein] + NADPH
CC = H2O + N(6)-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein]
CC + NADP(+); Xref=Rhea:RHEA:63664, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:16405, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:149468,
CC ChEBI:CHEBI:149472; Evidence={ECO:0000256|HAMAP-Rule:MF_00852};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CO2 + H2O + N(6)-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-
CC lysyl-[protein] + NAD(+) = (7R,8S)-8-amino-7-(carboxyamino)nonanoate
CC + (S)-2-amino-6-oxohexanoyl-[protein] + 3 H(+) + NADH;
CC Xref=Rhea:RHEA:63676, Rhea:RHEA-COMP:12448, Rhea:RHEA-COMP:16405,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:131803,
CC ChEBI:CHEBI:149470, ChEBI:CHEBI:149472; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00852};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CO2 + H2O + N(6)-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-
CC lysyl-[protein] + NADP(+) = (7R,8S)-8-amino-7-(carboxyamino)nonanoate
CC + (S)-2-amino-6-oxohexanoyl-[protein] + 3 H(+) + NADPH;
CC Xref=Rhea:RHEA:63668, Rhea:RHEA-COMP:12448, Rhea:RHEA-COMP:16405,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:131803,
CC ChEBI:CHEBI:149470, ChEBI:CHEBI:149472; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00852};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00852}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00852}.
CC -!- MISCELLANEOUS: In cannonical biotin synthesis a pimeloyl-conjugate is
CC transformed into biotin by the subsequent action of BioF, BioA, BioD
CC and BioB. This enzyme replaces BioA and performs the first half-
CC reaction of BioD. {ECO:0000256|HAMAP-Rule:MF_00852}.
CC -!- SIMILARITY: Belongs to the BioU family. {ECO:0000256|HAMAP-
CC Rule:MF_00852}.
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:RUR86876.1}.
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DR EMBL; RSCJ01000001; RUR86876.1; -; Genomic_DNA.
DR RefSeq; WP_016874208.1; NZ_RSCJ01000001.1.
DR AlphaFoldDB; A0A3S1APP2; -.
DR STRING; 211165.GCA_000317285_05232; -.
DR OrthoDB; 447533at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000268857; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00852; BioU; 1.
DR InterPro; IPR044262; BioU-like.
DR InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00852};
KW Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00852};
KW NAD {ECO:0000256|HAMAP-Rule:MF_00852};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00852};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00852};
KW Reference proteome {ECO:0000313|Proteomes:UP000268857};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00852}.
FT DOMAIN 14..123
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00208"
FT ACT_SITE 133
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT ACT_SITE 203
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT ACT_SITE 207
FT /note="Proton donor and proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT BINDING 22..26
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT BINDING 67
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT BINDING 199..200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT MOD_RES 133
FT /note="Allysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
SQ SEQUENCE 340 AA; 36550 MW; 4C86013C701D46FF CRC64;
MNAEQVMDFS NFPQAKRIGV LGFGGLGQAA AKVLAPKKEM ILVTVADKKG YAYSPEGLNA
KECIATYHSQ GSVGYLDIFG TLTNYSIQDL IESGHPVDGY FLALPNLPND FIASVAQQFI
KSGWRGVLVD AIKRTSAVEQ LLKMKEELQA AGITYMTGCG ATPGLLTAAA ALAAQSYSEI
HQVEITFGVG IANWEAYRAT IREDIAHMPG YSTETARAMT DAEVEALLDR TNGVLTLENM
EHADDVMLEL AGICPRDRVT VGGVVDTRNP KKPLSTNVKI TGRTFEGKIS THTFTLGDET
SMAANVCGPA FGYLKAGIGL HQRGIYGIFT AAEIMPQFVR
//
