ID A0A218Q112_9CYAN Unreviewed; 334 AA.
AC A0A218Q112;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, 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=NIES3585_15790 {ECO:0000313|EMBL:GAX35562.1};
OS Nodularia sp. NIES-3585.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Nodularia.
OX NCBI_TaxID=1973477 {ECO:0000313|EMBL:GAX35562.1, ECO:0000313|Proteomes:UP000198352};
RN [1] {ECO:0000313|EMBL:GAX35562.1, ECO:0000313|Proteomes:UP000198352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3585 {ECO:0000313|EMBL:GAX35562.1,
RC ECO:0000313|Proteomes:UP000198352};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:GAX35562.1}.
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DR EMBL; BDUB01000001; GAX35562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218Q112; -.
DR OrthoDB; 447533at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000198352; 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 Transferase {ECO:0000256|HAMAP-Rule:MF_00852}.
FT DOMAIN 11..95
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00208"
FT ACT_SITE 127
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT ACT_SITE 201
FT /note="Proton donor and proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT BINDING 16..20
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT BINDING 61
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT BINDING 193..194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
FT MOD_RES 127
FT /note="Allysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00852"
SQ SEQUENCE 334 AA; 35750 MW; 95579AC9DC9BF0E9 CRC64;
MNTQPTNQPI RVGVLGFGGL GQAAAKLLSS KREMILVAAA DQKGYAYSTE GLNTQECIKT
YQSQGSVGYL EPVGRLSNNS IQDLIATTQP VDGYFLALPN LPNDFIPSVA QQFIKSGWRG
VLVDAIKRTS AVEQLLAMKD ELQAAGITYM SGCGATPGLL TAAAALAAQS YAEIHKVEIT
FGVGIANWEA YRATVREDIG HMPGYSVETA RAMTDAEVEA LLDKTNGVLT LDNMEHADDV
MLEFAGICSR DRVTVGGVVD TRNAKKPLST NVKVTGRTFE GKISTHTFTL GDETSMAANV
CGPAFGYLKA GRQLHQRGIY GIFTAAEIMP QFVK
//
