ID A0A0C5WI27_9GAMM Unreviewed; 403 AA.
AC A0A0C5WI27;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Adenosylhomocysteinase {ECO:0000313|EMBL:AJR06768.1};
GN ORFNames=H744_1c1750 {ECO:0000313|EMBL:AJR06768.1};
OS Photobacterium gaetbulicola Gung47.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR06768.1, ECO:0000313|Proteomes:UP000032303};
RN [1] {ECO:0000313|EMBL:AJR06768.1, ECO:0000313|Proteomes:UP000032303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gung47 {ECO:0000313|EMBL:AJR06768.1,
RC ECO:0000313|Proteomes:UP000032303};
RA Kim Y.-O.;
RT "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT gaetbulicola Gung47.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP005973; AJR06768.1; -; Genomic_DNA.
DR RefSeq; WP_044621791.1; NZ_CP005973.1.
DR AlphaFoldDB; A0A0C5WI27; -.
DR STRING; 658445.H744_1c1750; -.
DR KEGG; pgb:H744_1c1750; -.
DR PATRIC; fig|658445.3.peg.1896; -.
DR HOGENOM; CLU_025194_0_2_6; -.
DR OrthoDB; 9802717at2; -.
DR Proteomes; UP000032303; Chromosome 1.
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 PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 1.
DR Pfam; PF05221; AdoHcyase; 1.
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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR001109-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000032303}.
FT DOMAIN 190..350
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 158..160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 221..226
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 242
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 298..300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 344
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 403 AA; 44567 MW; 2F6F8B71111D57D1 CRC64;
MEQNTYPEHD VADLSLAPLG RRRVAWARSH MPIMRSIIEH FEKEKPFTGL TIGICLHVEA
KTGVWLEALT KGGAKVVITG SPGSTQDETA AALVEDYGVS VYSRRDESFD DHINYCRKVL
SHQPDIIADN GADLHELIFT EPEFSGFQTS LLGATEETTT GANRLREDFH ADKFSTLIIN
DTQAKRIIEN RFGVGSSVVD GIMRATNVML HGKKVVVIGY GYCGSGTAQR LRGMGAHVTV
VESNPLTLLE AHMEGFYTST LEEALPDADM VVTITGRDNV LRKEHFELMR DNTIIANAGH
FQREINLADL AAVSQSQDKI RPHVTAYQLE EKQLFVLSDA NLVNLSAGDG NPIEIMDLGL
ALQSLSLERI ALNRDSLQNI PQPVPFDIEM QVAELAVKHW INH
//
