ID C2NIW4_BACCE Unreviewed; 459 AA.
AC C2NIW4;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=adenosylhomocysteine nucleosidase {ECO:0000256|ARBA:ARBA00011974};
DE EC=3.2.2.9 {ECO:0000256|ARBA:ARBA00011974};
GN ORFNames=bcere0004_26370 {ECO:0000313|EMBL:EEK55970.1};
OS Bacillus cereus BGSC 6E1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=526970 {ECO:0000313|EMBL:EEK55970.1};
RN [1] {ECO:0000313|EMBL:EEK55970.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 6E1 {ECO:0000313|EMBL:EEK55970.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-
CC thioadenosine (hydrolase route): step 1/2.
CC {ECO:0000256|ARBA:ARBA00004945}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEK55970.1}.
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DR EMBL; ACLU01000067; EEK55970.1; -; Genomic_DNA.
DR RefSeq; WP_001079729.1; NZ_CM000716.1.
DR AlphaFoldDB; C2NIW4; -.
DR HOGENOM; CLU_590070_0_0_9; -.
DR UniPathway; UPA00904; UER00871.
DR Proteomes; UP000000284; Chromosome.
DR GO; GO:0008782; F:adenosylhomocysteine nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008930; F:methylthioadenosine nucleosidase activity; IEA:InterPro.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0009164; P:nucleoside catabolic process; IEA:InterPro.
DR CDD; cd09008; MTAN; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR010049; MTA_SAH_Nsdase.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR NCBIfam; TIGR01704; MTA_SAH-Nsdase; 1.
DR PANTHER; PTHR46832; 5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE; 1.
DR PANTHER; PTHR46832:SF1; 5'-METHYLTHIOADENOSINE_S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE; 1.
DR Pfam; PF13419; HAD_2; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167}.
FT DOMAIN 3..225
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 459 AA; 51225 MW; 2CDB1421650DBB78 CRC64;
MNRIGIIGAM QIEIDLLLEK LVVQEEQTIA GMPFYVGEFM GTEIIVARCG VGKVNAAACT
QTLIHKFDVD AIINTGVAGG LQPDVKVGDI VISTNVTHHD VSKTQMKNLF PFQEEFIASK
ELVELARKAC NSSSLHMEIH EGRIVSGECF VEDSKLKAKL IDEYAPHCTE MEGAAIGHVA
YINEVPFLVI RCISDSADDE AQISYDDFAK TAANYCSEII VEMLKTISSK TYSSKGENEM
LQALIFDMDG TLFQTDKILE LSLDDTFDHL RSLQLWDTVT PIDKYREIMG VPLPKVWEAL
LPDHSLEIRE QTDAYFLERL IENIKSGKGA LYPNVKEIFT YIKENNCSIY IASNGLTEYL
RAIVSYYDLD QWVTETFSIE QINSLNKSDL VKSILNKYDI KEAAVVGDRL SDINAAKDNG
LIAIGCNFDF AQEDELAQAD IVIDDLLELK GILSTVQRL
//
