MQNX_ACIC1
ID MQNX_ACIC1 Reviewed; 356 AA.
AC A0LRH8;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Aminodeoxyfutalosine deaminase;
DE Short=AFL deaminase;
DE Short=Aminofutalosine deaminase;
DE EC=3.5.4.40;
GN OrderedLocusNames=Acel_0264;
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX NCBI_TaxID=351607;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=21098241; DOI=10.1128/aac.01362-10;
RA Arakawa C., Kuratsu M., Furihata K., Hiratsuka T., Itoh N., Seto H.,
RA Dairi T.;
RT "Diversity of the early step of the futalosine pathway.";
RL Antimicrob. Agents Chemother. 55:913-916(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP AND PATHWAY.
RC STRAIN=ATCC 43068 / DSM 8971 / 11B;
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). Is very poorly efficient on 1-(6-amino-9H-purin-9-yl)-1-deoxy-N-
CC ethyl-beta-D-ribofuranuronamide (NECA), adenosine, 5'-
CC methylthioadenosine, 5'-deoxyadenosine, 2'-deoxyadenosine, and AMP as
CC substrate. {ECO:0000269|PubMed:21098241, 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:21098241, ECO:0000269|PubMed:23972005};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.0 uM for aminodeoxyfutalosine {ECO:0000269|PubMed:23972005};
CC KM=61 uM for 1-(6-amino-9H-purin-9-yl)-1-deoxy-N-ethyl-beta-D-
CC ribofuranuronamide {ECO:0000269|PubMed:23972005};
CC Note=kcat is 6.8 sec(-1) with aminodeoxyfutalosine as substrate. kcat
CC is 0.007 sec(-1) with 1-(6-amino-9H-purin-9-yl)-1-deoxy-N-ethyl-beta-
CC D-ribofuranuronamide as substrate.;
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000269|PubMed:21098241, ECO:0000269|PubMed:23972005}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
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DR EMBL; CP000481; ABK52038.1; -; Genomic_DNA.
DR RefSeq; WP_011719101.1; NC_008578.1.
DR AlphaFoldDB; A0LRH8; -.
DR SMR; A0LRH8; -.
DR STRING; 351607.Acel_0264; -.
DR PRIDE; A0LRH8; -.
DR EnsemblBacteria; ABK52038; ABK52038; Acel_0264.
DR KEGG; ace:Acel_0264; -.
DR eggNOG; COG1816; Bacteria.
DR HOGENOM; CLU_039228_7_0_11; -.
DR OMA; EGIFSPW; -.
DR OrthoDB; 554648at2; -.
DR BRENDA; 3.5.4.40; 9545.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000008221; Chromosome.
DR GO; GO:0019239; F:deaminase activity; 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 InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43114; PTHR43114; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01430; aden_deam; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Menaquinone biosynthesis; Metal-binding; Reference proteome;
KW Zinc.
FT CHAIN 1..356
FT /note="Aminodeoxyfutalosine deaminase"
FT /id="PRO_0000425134"
FT ACT_SITE 202
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 356 AA; 38176 MW; 03BC2A25312E43EA CRC64;
MTPHDPVSVE AVPKIELHVH LEGTVEPATV LDIAARNGLA LPVSTVDELS ALYRVTTFSD
FLRLWILTTN VLRKAEDFSQ VVVDYARRAK RHGAVYIEGI FSPVERVMRG VGWAEIFDGY
CEGAERAYAE HGVVVRLTPE AYRGADPELV AEMVRYAGRY RDRGVVGVGI GGDERARPTR
HYAAAFAPAV DLGLGVVPHA GEFPLFPDGA SGAATLRETI EALNPVRIRH GIAAAADPAL
VAVIRERGIV LDVCPTSNLR TGAIRDLADH PLPRLAAAGI PCTVGTDDPA VFDTDLSREF
TIAARLGVEP RLLYDAGITG ALCDDDVKSH LRQIGAATTW PTTTATWSTT AAGESL
