ID A0A0Q5C8P8_9MICO Unreviewed; 524 AA.
AC A0A0Q5C8P8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=S-adenosyl-L-homocysteine hydrolase NAD binding domain-containing protein {ECO:0000259|SMART:SM00997};
GN ORFNames=ASF54_03870 {ECO:0000313|EMBL:KQQ27889.1};
OS Frondihabitans sp. Leaf304.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frondihabitans.
OX NCBI_TaxID=1736329 {ECO:0000313|EMBL:KQQ27889.1, ECO:0000313|Proteomes:UP000051456};
RN [1] {ECO:0000313|EMBL:KQQ27889.1, ECO:0000313|Proteomes:UP000051456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ27889.1,
RC ECO:0000313|Proteomes:UP000051456};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ27889.1, ECO:0000313|Proteomes:UP000051456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ27889.1,
RC ECO:0000313|Proteomes:UP000051456};
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:KQQ27889.1}.
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DR EMBL; LMNV01000002; KQQ27889.1; -; Genomic_DNA.
DR RefSeq; WP_055959034.1; NZ_LMNV01000002.1.
DR AlphaFoldDB; A0A0Q5C8P8; -.
DR STRING; 1736329.ASF54_03870; -.
DR OrthoDB; 9802717at2; -.
DR Proteomes; UP000051456; 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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000051456}.
FT DOMAIN 268..434
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 54764 MW; 71F7868B669B1CF9 CRC64;
MPEPDAAAPH DETDTRTDAD RKTDADLASS AVRRFARATN QVIAGKTFRI RGTAPALDLL
LRDLGARPAA AGHDADLDWF AAVDHDAEPT IALPNRGDAT GRIDWARRHM TVSGRLAAAL
THDGIVRGVR IGIAMVLEPK TAVLALLLRD AGAEVVVYAH ADETDDEVAD ALRTQGLEVF
ADSRATLAEQ RGLAVYLLDR RPAFLLDDGS HVIRLAHEIG HPALDTMVGA AEETTSGLRP
LRILARRHEL VIPVIAVNDA RTKTYFDNRY GTGQSCVFAI LDLLDTLPET PVRAGSRATV
AGFGPVGEGV AQVLAALGLT VTVAETDPVR ALQAVYAGYD VAELAVAASQ SDLIVSATGV
RETVSLEVLR ATREGAVVAV AGGVDQEVAL DAAAEAGATR EPVVPKIERL TMSGGPSLLL
LDDGGCINIT AAEGNPIEIM DLSFAVQLEA VRMLVDSGST LEPGVHALGP KADRVIATEA
LAAWGIAAPG AVAEARAPRG GDSDGDSADP RTTRFGPLGP EARS
//
