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Database: UniProt
Entry: A0A0S9E147_9MICO
LinkDB: A0A0S9E147_9MICO
Original site: A0A0S9E147_9MICO 
ID   A0A0S9E147_9MICO        Unreviewed;       373 AA.
AC   A0A0S9E147;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000313|EMBL:KQO11942.1};
GN   ORFNames=ASF06_00320 {ECO:0000313|EMBL:KQO11942.1};
OS   Agreia sp. Leaf244.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agreia.
OX   NCBI_TaxID=1736305 {ECO:0000313|EMBL:KQO11942.1, ECO:0000313|Proteomes:UP000051484};
RN   [1] {ECO:0000313|EMBL:KQO11942.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf244 {ECO:0000313|EMBL:KQO11942.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQO11942.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf244 {ECO:0000313|EMBL:KQO11942.1};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC       {ECO:0000256|ARBA:ARBA00007122}.
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:KQO11942.1}.
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DR   EMBL; LMLX01000001; KQO11942.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S9E147; -.
DR   STRING; 1736305.ASF06_00320; -.
DR   Proteomes; UP000051484; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
DR   InterPro; IPR000043; Adenosylhomocysteinase-like.
DR   InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR   PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR   PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 1.
DR   Pfam; PF05221; AdoHcyase; 1.
DR   Pfam; PF00670; AdoHcyase_NAD; 1.
DR   SMART; SM00996; AdoHcyase; 1.
DR   SMART; SM00997; AdoHcyase_NAD; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00739; ADOHCYASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KQO11942.1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563}.
FT   DOMAIN          156..317
FT                   /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT                   /evidence="ECO:0000259|SMART:SM00997"
SQ   SEQUENCE   373 AA;  39474 MW;  5F38F4A92DB6D9DA CRC64;
     MRLLAAVSRQ FAETRPFEGH RIGMSLHIEP KTAVLLETLA AGGAEIVGTG NHGSTQDDVV
     AYLRNQGMTL FGRRDDTLEQ HYANVAAVLD ATPDILLDNG ADLAAGIVAR GAGASLIGGT
     EETTSGGDRL RDELLGRVPF PVIVINDSLL KQLGENKHAV GQSVVESFMR ITNLMIPGRR
     FVVVGYGWCG RGVAQYLRAL GGKVAVAEVD ELKAFEAALD GFRVDTADGL AEWGEVFITA
     TGRANVLTMS AIERMSDGAI LANCGHFPWE IDTASLRTAA TSTRAIGDTI ERIDLPNGRH
     VILIAGGRMF NLAGTAPKGN SLDSMDLGFL LQVLSLERVA TGASTLVAGA QPVPDDLERE
     IARRMVAAMG ASL
//
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