BIOU_HALMT
ID BIOU_HALMT Reviewed; 353 AA.
AC I3R9K3;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=(S)-8-amino-7-oxononanoate synthase BioU {ECO:0000255|HAMAP-Rule:MF_00852};
DE EC=2.6.1.- {ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000305|PubMed:32042199};
DE AltName: Full=8-amino-7-oxononanoate carboxylating dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00852};
GN Name=bioU {ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000303|PubMed:32042199};
GN OrderedLocusNames=HFX_5078; ORFNames=BM92_18625, C439_00820, E6P09_18710;
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OG Plasmid HMPLAS2, Plasmid pHM300, and Plasmid pHME322.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RC PLASMID=pHM300 {ECO:0000312|Proteomes:UP000006469};
RX PubMed=22843593; DOI=10.1128/jb.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RC PLASMID=HMPLAS2 {ECO:0000312|EMBL:AHZ24218.1};
RA Bautista V.;
RT "Transcriptional profiles of Haloferax mediterranei on the basis of
RT nitrogen availability.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RC PLASMID=pHME322;
RA DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA Roberts R.J.;
RT "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT mediterranei.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RC PLASMID=pHM300;
RX PubMed=32042199; DOI=10.1038/s41589-019-0461-9;
RA Sakaki K., Ohishi K., Shimizu T., Kobayashi I., Mori N., Matsuda K.,
RA Tomita T., Watanabe H., Tanaka K., Kuzuyama T., Nishiyama M.;
RT "A suicide enzyme catalyzes multiple reactions for biotin biosynthesis in
RT cyanobacteria.";
RL Nat. Chem. Biol. 16:415-422(2020).
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)+ (By similarity). Complements a bioA
CC deletion in E.coli (PubMed:32042199). {ECO:0000255|HAMAP-Rule:MF_00852,
CC ECO:0000269|PubMed:32042199}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00852, ECO:0000305|PubMed:32042199};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63661;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00852,
CC ECO:0000305|PubMed:32042199};
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:0000255|HAMAP-Rule:MF_00852,
CC ECO:0000305|PubMed:32042199};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63665;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00852,
CC ECO:0000305|PubMed:32042199};
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:0000255|HAMAP-
CC Rule:MF_00852, ECO:0000305|PubMed:32042199};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63669;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00852,
CC ECO:0000305|PubMed:32042199};
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:0000255|HAMAP-Rule:MF_00852,
CC ECO:0000305|PubMed:32042199};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63673;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00852,
CC ECO:0000305|PubMed:32042199};
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:0000255|HAMAP-
CC Rule:MF_00852, ECO:0000305|PubMed:32042199};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63677;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00852,
CC ECO:0000305|PubMed:32042199};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00852, ECO:0000269|PubMed:32042199}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00852, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the BioU family. {ECO:0000255|HAMAP-
CC Rule:MF_00852, ECO:0000305}.
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DR EMBL; CP001870; AFK20913.1; -; Genomic_DNA.
DR EMBL; CP007553; AHZ24218.1; -; Genomic_DNA.
DR EMBL; AOLO01000001; EMA05297.1; -; Genomic_DNA.
DR EMBL; CP039141; QCQ77342.1; -; Genomic_DNA.
DR RefSeq; WP_004056369.1; NZ_CP039141.1.
DR AlphaFoldDB; I3R9K3; -.
DR SMR; I3R9K3; -.
DR EnsemblBacteria; AFK20913; AFK20913; HFX_5078.
DR EnsemblBacteria; AHZ24218; AHZ24218; BM92_18625.
DR EnsemblBacteria; EMA05297; EMA05297; C439_00820.
DR EnsemblBacteria; QCQ77342; QCQ77342; E6P09_18710.
DR GeneID; 40158493; -.
DR KEGG; hme:HFX_5078; -.
DR PATRIC; fig|523841.21.peg.164; -.
DR HOGENOM; CLU_072022_0_0_2; -.
DR OMA; MAANVCG; -.
DR OrthoDB; 42750at2157; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000006469; Plasmid pHM300.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR Proteomes; UP000027075; Plasmid HMPLAS2.
DR Proteomes; UP000299011; Plasmid pHME322.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009102; P:biotin biosynthetic process; IMP:UniProtKB.
DR HAMAP; MF_00852; BioU; 1.
DR InterPro; IPR044262; BioU-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Biotin biosynthesis; NAD; NADP; Nucleotide-binding;
KW Plasmid; Transferase.
FT CHAIN 1..353
FT /note="(S)-8-amino-7-oxononanoate synthase BioU"
FT /id="PRO_0000450576"
FT ACT_SITE 147
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00852"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00852"
FT ACT_SITE 222
FT /note="Proton donor and proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00852"
FT BINDING 10..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00852"
FT BINDING 214..215
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00852"
FT MOD_RES 147
FT /note="Allysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00852"
SQ SEQUENCE 353 AA; 37612 MW; FFA1A1EA39D0F998 CRC64;
MDEINFAVLG TGGIGRRTLE VSTYKDGLTP VAACDRHGVA VNHDGLDVEE ILDATEGNIA
GDGTGDTEDK RVTDGGAAVK QHGDGAGIVA SAQGTSTETP IDEIIAESDE IDAVLLALPN
LEHDFIPRIA ERFAEAEFEG VLIDVLKRSR VIGMLDDREE TLVESGITFV CGAGATPGLL
TGAAALAAQS FVEVEEVEIW WGVGLKSGYE DNRGTVREDI AHLDGYDIET AREMDESEIE
AVIEEHDGVL EFNDMEHADD VLLERAGICD AEDVTVGGIL DIRKDEKPTT TTVRVTGRTF
DGKRGTNTFQ LDDATSMAAN VNGPALGYLK SAVRRNRAGD YGVFGPAELM PGF
