ID B5XPI3_KLEP3 Unreviewed; 369 AA.
AC B5XPI3;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Putative adenosylhomocysteinase {ECO:0000313|EMBL:ACI10040.1};
GN OrderedLocusNames=KPK_1725 {ECO:0000313|EMBL:ACI10040.1};
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522 {ECO:0000313|EMBL:ACI10040.1, ECO:0000313|Proteomes:UP000001734};
RN [1] {ECO:0000313|EMBL:ACI10040.1, ECO:0000313|Proteomes:UP000001734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342 {ECO:0000313|EMBL:ACI10040.1,
RC ECO:0000313|Proteomes:UP000001734};
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
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}.
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DR EMBL; CP000964; ACI10040.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XPI3; -.
DR KEGG; kpe:KPK_1725; -.
DR HOGENOM; CLU_025194_0_1_6; -.
DR BioCyc; KPNE507522:GI0B-1723-MONOMER; -.
DR Proteomes; UP000001734; Chromosome.
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;
FT DOMAIN 168..326
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
SQ SEQUENCE 369 AA; 40359 MW; 0D0EC80F32060E1E CRC64;
MNNKISLVKE VAWASQNMPR TLRQVAALPD LSGVRLACCM HLDMKMIPLV QGILDKGAQV
FLTTCNPTTV QDDVVAWLVE RGAEACAWRN MSDADWQQSW EKAIAWQPTH LCEMGADITT
LLHQRGEFGN IVAGLEATGS GVNRLGDIQP GYPIFNWDDL PVKEGLHNRH MVGLTAWHTF
FQTTHLTLHE KKVLVIGYGL VGQGVAAAAK AFGGQVMVAE IDPARRLQAA YDGWHVVDLQ
EAIASADVVA TATGGKNVVN RQALERAKAG VFILNVGHVA EEIDGEYLRQ YPQEEVMPYI
NAYRMADKTI YLLANGSMLN LSAGFGDSLN AFDVTLAVMA SGIRHIVTDG MRAPAQVYLL
PQAVWQQAL
//
