ID A4G5R5_HERAR Unreviewed; 456 AA.
AC A4G5R5;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=AMP nucleosidase {ECO:0000256|ARBA:ARBA00011985};
DE EC=3.2.2.4 {ECO:0000256|ARBA:ARBA00011985};
DE AltName: Full=AMP nucleosidase {ECO:0000256|ARBA:ARBA00031983};
GN OrderedLocusNames=HEAR1695 {ECO:0000313|EMBL:CAL61852.1};
OS Herminiimonas arsenicoxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL61852.1, ECO:0000313|Proteomes:UP000006697};
RN [1] {ECO:0000313|EMBL:CAL61852.1, ECO:0000313|Proteomes:UP000006697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + H2O = adenine + D-ribose 5-phosphate;
CC Xref=Rhea:RHEA:20129, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=3.2.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000274};
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DR EMBL; CU207211; CAL61852.1; -; Genomic_DNA.
DR AlphaFoldDB; A4G5R5; -.
DR STRING; 204773.HEAR1695; -.
DR KEGG; har:HEAR1695; -.
DR eggNOG; COG1611; Bacteria.
DR HOGENOM; CLU_047550_0_0_4; -.
DR OrthoDB; 9801098at2; -.
DR Proteomes; UP000006697; Chromosome.
DR GO; GO:0008714; F:AMP nucleosidase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.450; -; 1.
DR Gene3D; 3.30.1850.10; MoCo carrier protein-like; 1.
DR InterPro; IPR031100; LOG_fam.
DR InterPro; IPR049788; PpnN.
DR InterPro; IPR037153; PpnN-like_sf.
DR InterPro; IPR021826; PpnN_C.
DR InterPro; IPR027820; PpnN_N.
DR NCBIfam; NF038390; Nsidase_PpnN; 1.
DR PANTHER; PTHR43393; CYTOKININ RIBOSIDE 5'-MONOPHOSPHATE PHOSPHORIBOHYDROLASE; 1.
DR PANTHER; PTHR43393:SF1; PYRIMIDINE_PURINE NUCLEOTIDE 5'-MONOPHOSPHATE NUCLEOSIDASE; 1.
DR Pfam; PF14793; DUF4478; 1.
DR Pfam; PF03641; Lysine_decarbox; 1.
DR Pfam; PF11892; PpnN_C; 1.
DR SUPFAM; SSF102405; MCP/YpsA-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006697}.
FT DOMAIN 9..116
FT /note="Pyrimidine/purine nucleotide 5'-monophosphate
FT nucleosidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14793"
FT DOMAIN 336..455
FT /note="Pyrimidine/purine nucleotide 5'-monophosphate
FT nucleosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11892"
SQ SEQUENCE 456 AA; 50622 MW; 53D9DF71DC71770D CRC64;
MAYEVVDTQL SPEGRLDILS KAEVQRLLDT RNGGLYQLFR NCALAVLNSG SSTDDGKELL
ERYQSFDINI IQRERGIKLD IKGAPASAFV DGKMIKGIHE HLFSVLRDIL YTHDEILSNP
TFDLDSSAGI SDSVFNILRN ANVLHPNLNP KLVVCWGGHS ISREEYDYTK KVGYQIGLRD
MDICTGCGPG AMKGPMKGAT IGHAKQRILN GRYLGISEPG IIAAEAPNPI VNDLVIMPDI
EKRLEAFVRA GHGIVVFPGG AGTAEEILYI LGILLHPDNA GLPFPLIFTG HAESAEYFRQ
IDQFIGVTLG PDAQKLYQII VDDPERVAQQ IQAGIVQVRE FRKSKGDAYY FNWTLKIDHA
FQQPFVPTHE NMRNLSLHKK QENHLLAANL RRAFSGVVAG NVKDSGIRSI EKHGLFEISG
DREIMEPMDA LLASFVAQNR MKLPGKTYVP CYRIIK
//
