ID A0A1E5MNT5_9MICO Unreviewed; 561 AA.
AC A0A1E5MNT5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=S-adenosyl-L-homocysteine hydrolase NAD binding domain-containing protein {ECO:0000259|SMART:SM00997};
GN ORFNames=Cus16_0871 {ECO:0000313|EMBL:OEI70244.1};
OS Curtobacterium sp. ER1/6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1891920 {ECO:0000313|EMBL:OEI70244.1, ECO:0000313|Proteomes:UP000095245};
RN [1] {ECO:0000313|EMBL:OEI70244.1, ECO:0000313|Proteomes:UP000095245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ER1/6 {ECO:0000313|EMBL:OEI70244.1,
RC ECO:0000313|Proteomes:UP000095245};
RA Garrido L.M., Alves J.M., Oliveira L.S., Gruber A., Padilla G.,
RA Araujo W.L.;
RT "Draft genome sequence of Curtobacterium sp. strain ER1/6, an endophytic
RT strain isolated from Citrus sinensis with potential to be used as a
RT biocontrol agent.";
RL Submitted (AUG-2016) 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:OEI70244.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MJAK01000001; OEI70244.1; -; Genomic_DNA.
DR RefSeq; WP_069711305.1; NZ_MJAK01000001.1.
DR AlphaFoldDB; A0A1E5MNT5; -.
DR STRING; 1891920.Cus16_0871; -.
DR PATRIC; fig|1891920.3.peg.900; -.
DR OrthoDB; 9802717at2; -.
DR Proteomes; UP000095245; Unassembled WGS sequence.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000095245}.
FT DOMAIN 313..481
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT REGION 533..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 561 AA; 57824 MW; 3BE7D7F9C404EE60 CRC64;
MPQRPDPERA AWASAAVRRS AAATNLLVAG RAVRVLGGDP RDAAALAGLL TALGARVAAD
DEPVDQLWCL GDPDESTAAV ERAADRPRGA TLVVVDAGRY APAVDEDAFG PVAPARPGVL
AVPALSDDVF LVSTGREPEH DPAAAARIRW ARRSMPVSRA LTADLRDDGL LRGTRVLVAM
VLEPKTAVLS LLLRDAGADV VVYAHADETD DAVAAVLREA GLPVHASSTA SLAEQHALAL
AALDTRPHVL LDDGSHLIRL THQERPDLLP TMLGAAEETT SGLRPLRVMA ERGTLGIPVV
AVNDARTKTV PDNRYGTGQS TVFATLDLVD GLPSGAHRVR PGGTAVVAGY GPVGEGVAQV
LAALGLRVTV ADVDPVRALQ ARLAGHAVAP LVDAVRGADL VVSASGVPDT IDHAVLRACA
AGAVVSVAGG VDREVALVDA ATAGAVRAAE ASHVERLTWP DGHQVVVLAG GNGVNTSAAE
GNPVEVMDLS FAVQLGAVRM LLERGDELER AVVPVDPAVD EATARAALAA WGSRHAPPLR
PAAQPADREP DVRTHRFGDP S
//
