MQNX_NITSB
ID MQNX_NITSB Reviewed; 405 AA.
AC A6Q234;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Aminodeoxyfutalosine deaminase;
DE Short=AFL deaminase;
DE Short=Aminofutalosine deaminase;
DE EC=3.5.4.40 {ECO:0000269|PubMed:23972005};
GN OrderedLocusNames=NIS_0429;
OS Nitratiruptor sp. (strain SB155-2).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC Nitratiruptoraceae; Nitratiruptor; unclassified Nitratiruptor.
OX NCBI_TaxID=387092;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB155-2;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-145 IN
RP COMPLEX WITH IRON AND BENZOATE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, KINETIC PARAMETERS, COFACTOR, PATHWAY, AND MUTAGENESIS OF
RP SER-145.
RC STRAIN=SB155-2;
RX PubMed=23972005; DOI=10.1021/bi400750a;
RA Goble A.M., Toro R., Li X., Ornelas A., Fan H., Eswaramoorthy S.,
RA Patskovsky Y., Hillerich B., Seidel R., Sali A., Shoichet B.K., Almo S.C.,
RA Swaminathan S., Tanner M.E., Raushel F.M.;
RT "Deamination of 6-aminodeoxyfutalosine in menaquinone biosynthesis by
RT distantly related enzymes.";
RL Biochemistry 52:6525-6536(2013).
CC -!- FUNCTION: Catalyzes the deamination of aminodeoxyfutalosine (AFL) into
CC futalosine (FL), a step in the biosynthesis of menaquinone (MK, vitamin
CC K2). To a lesser extent, can also deaminate 5'-methylthioadenosine.
CC {ECO:0000269|PubMed:23972005}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-amino-6-deoxyfutalosine + H(+) + H2O = futalosine + NH4(+);
CC Xref=Rhea:RHEA:40075, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58863, ChEBI:CHEBI:64286; EC=3.5.4.40;
CC Evidence={ECO:0000269|PubMed:23972005};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:23972005};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000269|PubMed:23972005};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.9 uM for aminodeoxyfutalosine {ECO:0000269|PubMed:23972005};
CC KM=110 uM for 5'-methylthioadenosine {ECO:0000269|PubMed:23972005};
CC KM=42 uM for 5'-deoxyadenosine {ECO:0000269|PubMed:23972005};
CC Note=kcat is 1.28 sec(-1) with aminodeoxyfutalosine as substrate.
CC kcat is 0.31 sec(-1) with 5'-methylthioadenosine as substrate. kcat
CC is 0.017 sec(-1) with 5'-deoxyadenosine as substrate.;
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000269|PubMed:23972005}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC {ECO:0000305}.
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DR EMBL; AP009178; BAF69543.1; -; Genomic_DNA.
DR RefSeq; WP_012081806.1; NC_009662.1.
DR PDB; 3V7P; X-ray; 1.35 A; A=1-405.
DR PDB; 4M51; X-ray; 1.08 A; A=1-405.
DR PDBsum; 3V7P; -.
DR PDBsum; 4M51; -.
DR AlphaFoldDB; A6Q234; -.
DR SMR; A6Q234; -.
DR STRING; 387092.NIS_0429; -.
DR EnsemblBacteria; BAF69543; BAF69543; NIS_0429.
DR KEGG; nis:NIS_0429; -.
DR eggNOG; COG0402; Bacteria.
DR HOGENOM; CLU_012358_10_1_7; -.
DR OMA; CNEKCEV; -.
DR OrthoDB; 1592010at2; -.
DR BioCyc; MetaCyc:MON-18223; -.
DR BRENDA; 3.5.4.40; 12235.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000001118; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Iron; Menaquinone biosynthesis; Metal-binding;
KW Reference proteome.
FT CHAIN 1..405
FT /note="Aminodeoxyfutalosine deaminase"
FT /id="PRO_0000425135"
FT ACT_SITE 209
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 63
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 206
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 306
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT MUTAGEN 145
FT /note="S->A: 3-fold reduction in catalytic efficiency with
FT AFL as substrate."
FT /evidence="ECO:0000269|PubMed:23972005"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:4M51"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:4M51"
FT STRAND 20..31
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:4M51"
FT STRAND 44..55
FT /evidence="ECO:0007829|PDB:4M51"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4M51"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 78..95
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:4M51"
FT STRAND 113..123
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:4M51"
FT STRAND 132..142
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 150..165
FT /evidence="ECO:0007829|PDB:4M51"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:4M51"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 186..199
FT /evidence="ECO:0007829|PDB:4M51"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:4M51"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:4M51"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:4M51"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:4M51"
FT TURN 293..298
FT /evidence="ECO:0007829|PDB:4M51"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 316..326
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 332..343
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 345..351
FT /evidence="ECO:0007829|PDB:4M51"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:4M51"
FT HELIX 381..388
FT /evidence="ECO:0007829|PDB:4M51"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:4M51"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:4M51"
SQ SEQUENCE 405 AA; 45532 MW; 75BFC47BD4919062 CRC64;
MRIIKPFAIL TPQTIIQDKA VAFDKKIEAI DTVENLIKKY PNAAVEHDEN SLLLPGFANP
HLHLEFSANK ATLQYGDFIP WLYSVIRHRE DLLPLCDGAC LEQTLSSIIQ TGTTAIGAIS
SYGEDLQACI DSALKVVYFN EVIGSNAATA DVMYASFLER FHQSKKHENE RFKAAVAIHS
PYSVHYILAK RALDIAKKYG SLVSVHFMES RAEREWLDKG SGEFAKFFKE FLNQTRPVND
TKSFLELFKE LHTLFVHMVW ANEEEIQTIA SYNAHIIHCP ISNRLLGNGV LDLEKIKSIP
YAIATDGLSS NYSLNMYEEL KAALFVHPNK EATTFAKELI IRATKAGYDA LGFEGGEIAV
GKDADMQLID LPEGLTNVED LYLHVILHTT KPKKVYIQGE EHVRE
