ID L8M501_9CYAN Unreviewed; 353 AA.
AC L8M501;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=Xen7305DRAFT_00030380 {ECO:0000313|EMBL:ELS03317.1};
OS Xenococcus sp. PCC 7305.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Xenococcaceae;
OC Xenococcus.
OX NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS03317.1, ECO:0000313|Proteomes:UP000011203};
RN [1] {ECO:0000313|EMBL:ELS03317.1, ECO:0000313|Proteomes:UP000011203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS03317.1,
RC ECO:0000313|Proteomes:UP000011203};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-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:ELS03317.1}.
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DR EMBL; ALVZ01000167; ELS03317.1; -; Genomic_DNA.
DR AlphaFoldDB; L8M501; -.
DR STRING; 102125.Xen7305DRAFT_00030380; -.
DR PATRIC; fig|102125.3.peg.2378; -.
DR eggNOG; COG1748; Bacteria.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000011203; 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:UP000011203};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00852}.
FT DOMAIN 31..140
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00208"
FT ACT_SITE 146
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT ACT_SITE 216
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT ACT_SITE 220
FT /note="Proton donor and proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT BINDING 36..40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT BINDING 212..213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT MOD_RES 146
FT /note="Allysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
SQ SEQUENCE 353 AA; 37826 MW; 026EB45B94ED0A09 CRC64;
MGDKYAMLEF VRMSGLKKKL MIIDKVNQPI KVGVLGFGGL GQAAAKILAP KGEMIWVAAA
DHQGYAYNSL GLNPDLVIKT CRDRGSIGHL DADGTLSKNS IQDLVVNHSV DGYFLALPNL
PNTFMADVAQ QFIKSGWQGV LVDALKRTSA VEQLLEIQDD LQAAGITYLT GCGATPGLLT
AAAAVAAQSY AEIHSVKITF GVGIANWEAY KSTIREDIAH MSEYDVETAR AMTDDEVSAL
LDKTNGIIAL ENMEHADDIM LELAGICDRD RVTVGGVVDT RNPKKPLSTN VAITGRTFEG
KISTHTFTLG DETSMAANVC GPAFGYLKAG IALQRRKVTG LFTAAEIMPQ FVN
//
