ID S4GXS2_GARVA Unreviewed; 504 AA.
AC S4GXS2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=S-adenosyl-L-homocysteine hydrolase, NAD binding domain protein {ECO:0000313|EMBL:EPI51757.1};
GN ORFNames=HMPREF1575_00894 {ECO:0000313|EMBL:EPI51757.1};
OS Gardnerella vaginalis JCP7672.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=1261060 {ECO:0000313|EMBL:EPI51757.1, ECO:0000313|Proteomes:UP000014621};
RN [1] {ECO:0000313|EMBL:EPI51757.1, ECO:0000313|Proteomes:UP000014621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCP7672 {ECO:0000313|EMBL:EPI51757.1,
RC ECO:0000313|Proteomes:UP000014621};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-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}.
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:EPI51757.1}.
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DR EMBL; ATJP01000065; EPI51757.1; -; Genomic_DNA.
DR RefSeq; WP_020760184.1; NZ_KE348213.1.
DR AlphaFoldDB; S4GXS2; -.
DR PATRIC; fig|1261060.4.peg.802; -.
DR HOGENOM; CLU_025194_0_2_11; -.
DR Proteomes; UP000014621; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; 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 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EPI51757.1};
KW NAD {ECO:0000256|PIRSR:PIRSR001109-2}.
FT DOMAIN 260..419
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 292..297
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 413
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 504 AA; 55033 MW; 1430B65D3B2F6520 CRC64;
MIDFSEWVAI TSQRTNQSLA GARVFIGDNN IQNENAKNSD QNSDVEKFLQ SAQSWGIIPT
TCKQYADFDA TKSYENIEDT MVNAPNLSGK DAIDYAQKHM PVMRTLLNNL KENGLDLKGV
RIAVCLVLEP KTAVLLRELH AHGAIIGVFC GPDETDQRVA DQLTKEGILV QANRDWTPEQ
THEGALKLLD EIQPDIIIDD GASFARLASL ERPQIAANLI GVAEETTSGV RAFEAMQKAS
RLRYPVIAVN NSALKTDFDN RHGTGETCVT TMQQILGSEC FKNAKITVVG YGPVGRGFAL
RIRALGAKVT ICDTNPVQSL RAVFDGFEAK NLECAVDTSD MIVSATGVRH TITLQHMQSM
QENAILAVIG GIANEIALDE IPDFKPVVGT PQRKIQIPNG PQITLISEGD GTNYTTGGGN
PIEIMDFSFA VQVSAVAYLL EHNGKNKKNS DKNPLDSGIY QLPESSDEQI ANIALAERGY
SASESNKDNG YRWDLTRFAE DENI
//
