MQNX_DEIRA
ID MQNX_DEIRA Reviewed; 418 AA.
AC Q9RW45;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=DR_0824;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEX WITH ZINC ION, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, AND
RP COFACTOR.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
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). To a lesser extent, can also deaminate 5'-
CC deoxyadenosine, 5'-methylthioadenosine, 2'-deoxyadenosine, adenosine,
CC 1-(6-amino-9H-purin-9-yl)-1-deoxy-N-ethyl-beta-D-ribofuranuronamide
CC (NECA), and S-adenosylhomocysteine. {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=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:23972005};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:23972005};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 uM for aminodeoxyfutalosine {ECO:0000269|PubMed:23972005};
CC KM=37 uM for 2'-deoxyadenosine {ECO:0000269|PubMed:23972005};
CC Note=kcat is 8.6 sec(-1) with aminodeoxyfutalosine as substrate. kcat
CC is 0.72 sec(-1) with 2'-deoxyadenosine as substrate.;
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC {ECO:0000305}.
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DR EMBL; AE000513; AAF10399.1; -; Genomic_DNA.
DR PIR; F75472; F75472.
DR RefSeq; NP_294548.1; NC_001263.1.
DR RefSeq; WP_010887470.1; NZ_CP015081.1.
DR PDB; 2IMR; X-ray; 1.78 A; A=2-418.
DR PDBsum; 2IMR; -.
DR AlphaFoldDB; Q9RW45; -.
DR SMR; Q9RW45; -.
DR STRING; 243230.DR_0824; -.
DR EnsemblBacteria; AAF10399; AAF10399; DR_0824.
DR KEGG; dra:DR_0824; -.
DR PATRIC; fig|243230.17.peg.1005; -.
DR eggNOG; COG0402; Bacteria.
DR HOGENOM; CLU_012358_2_5_0; -.
DR InParanoid; Q9RW45; -.
DR OMA; CNEKCEV; -.
DR OrthoDB; 1592010at2; -.
DR BRENDA; 3.5.4.40; 1856.
DR UniPathway; UPA00079; -.
DR EvolutionaryTrace; Q9RW45; -.
DR Proteomes; UP000002524; Chromosome I.
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; Menaquinone biosynthesis; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..418
FT /note="Aminodeoxyfutalosine deaminase"
FT /id="PRO_0000122306"
FT ACT_SITE 241
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:2IMR"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:2IMR"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:2IMR"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:2IMR"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:2IMR"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:2IMR"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 154..161
FT /evidence="ECO:0007829|PDB:2IMR"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 182..197
FT /evidence="ECO:0007829|PDB:2IMR"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:2IMR"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 218..231
FT /evidence="ECO:0007829|PDB:2IMR"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 269..273
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 283..289
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:2IMR"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:2IMR"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 337..342
FT /evidence="ECO:0007829|PDB:2IMR"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 363..372
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 378..393
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:2IMR"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:2IMR"
SQ SEQUENCE 418 AA; 45524 MW; 4900A97AB3867C0A CRC64;
MRFSAVSRHH RGASIDPMTF SEATTPDALT PDAHTPRLLT CDVLYTGMGG AQSPGGVVVV
GETVAAAGHP DELRRQYPHA AEERAGAVIA PPPVNAHTHL DMSAYEFQAL PYFQWIPEVV
IRGRHLRGVA AAQAGADTLT RLGAGGVGDI VWAPEVMDAL LAREDLSGTL YFEVLNPFPD
KADEVFAAAR THLERWRRLE RPGLRLGLSP HTPFTVSHRL MRLLSDYAAG EGLPLQIHVA
EHPTELEMFR TGGGPLWDNR MPALYPHTLA EVIGREPGPD LTPVRYLDEL GVLAARPTLV
HMVNVTPDDI ARVARAGCAV VTCPRSNHHL ECGTFDWPAF AAAGVEVALG TDSVASGETL
NVREEVTFAR QLYPGLDPRV LVRAAVKGGQ RVVGGRTPFL RRGETWQEGF RWELSRDL
