ID W4N772_9BIFI Unreviewed; 488 AA.
AC W4N772;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=S-adenosylhomocysteine hydrolase {ECO:0000313|EMBL:ETY70887.1};
GN ORFNames=BMOU_1748 {ECO:0000313|EMBL:ETY70887.1};
OS Bifidobacterium moukalabense DSM 27321.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1435051 {ECO:0000313|EMBL:ETY70887.1, ECO:0000313|Proteomes:UP000019155};
RN [1] {ECO:0000313|EMBL:ETY70887.1, ECO:0000313|Proteomes:UP000019155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27321 {ECO:0000313|EMBL:ETY70887.1,
RC ECO:0000313|Proteomes:UP000019155};
RX PubMed=24558236;
RA Lugli G.A., Duranti S., Milani C., Turroni F., Viappiani A., Mangifesta M.,
RA van Sinderen D., Ventura M.;
RT "The Genome Sequence of Bifidobacterium moukalabense DSM 27321 Highlights
RT the Close Phylogenetic Relatedness with the Bifidobacterium dentium
RT Taxon.";
RL Genome Announc. 2:e00048-e00014(2014).
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|PIRSR:PIRSR001109-2};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|PIRSR:PIRSR001109-2};
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:ETY70887.1}.
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DR EMBL; AZMV01000007; ETY70887.1; -; Genomic_DNA.
DR RefSeq; WP_034876771.1; NZ_AZMV01000007.1.
DR AlphaFoldDB; W4N772; -.
DR STRING; 1435051.BMOU_1748; -.
DR PATRIC; fig|1435051.3.peg.1737; -.
DR eggNOG; COG0499; Bacteria.
DR OrthoDB; 9802717at2; -.
DR Proteomes; UP000019155; 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; 2.
DR Pfam; PF00670; AdoHcyase_NAD; 1.
DR PIRSF; PIRSF001109; Ad_hcy_hydrolase; 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:ETY70887.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR001109-2};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563}.
FT DOMAIN 253..412
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 285..290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 406
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 488 AA; 52903 MW; D7FE592F349D8120 CRC64;
MEQFRFSTWA EGYSQRTNRS LAGTRLYIGH DGGDSYGIGQ PDLAQAQDWG MVPSCDSAEI
QTGRAIDATM PLGDVVDARR LTGAEAMRFA QEHMPVLDTL MRQMRDDVDF TGIRIAVCLI
LEPKTAVLLR QLKAAGAVVG AYCGSEANDE RVAAQLRAEG IPVAYDPDWT PAQAHQGALD
LLDEIQPNII IDDGASFARL AAMERPELME RIIGVAEETT SGIRAFQAMQ DAGALTFPVI
AVNDSMLKTG FDNAHGTGET CVTTLQRILG SDFFGGRNVS VIGYGPVGRG FAHRVRALGA
NVTICDTDPV IALQAVFDGF RAHDIDQAIG ESDAIISATG VRHTITLRHM RRMKPNAVLS
VIGGIANEIA LDQIDGFHAE NKREIRDLAV PDGPVIRLVS EGDGVNYTVG GGNPIEIMDL
SFAVQASAVA YLLRNRGTLR PGLQRLGRDV DRHIADIALR TRGYRASHAT ADNEYDWTLT
RFAENEKE
//
