SAHH_BURP1
ID SAHH_BURP1 Reviewed; 473 AA.
AC Q3JY79;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Adenosylhomocysteinase {ECO:0000255|HAMAP-Rule:MF_00563};
DE EC=3.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00563};
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000255|HAMAP-Rule:MF_00563};
DE Short=AdoHcyase {ECO:0000255|HAMAP-Rule:MF_00563};
GN Name=ahcY {ECO:0000255|HAMAP-Rule:MF_00563};
GN OrderedLocusNames=BURPS1710b_0057;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NAD.
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "Crystal structure of S-adenosyl-L-homocysteine hydrolase from Burkholderia
RT pseudomallei.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE
RP ANALOG.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of S-adenosyl-l-homocysteine hydrolase from Burkholderia
RT pseudomallei in complex with 9-beta-D-arabino-furanosyl-adenine.";
RL Submitted (MAR-2009) to the PDB data bank.
CC -!- FUNCTION: May play a key role in the regulation of the intracellular
CC concentration of adenosylhomocysteine. {ECO:0000255|HAMAP-
CC Rule:MF_00563}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine;
CC Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.3.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00563};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Note=Binds 1 NAD(+) per subunit.;
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00563}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00563}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00563}.
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DR EMBL; CP000124; ABA47924.1; -; Genomic_DNA.
DR RefSeq; WP_004198634.1; NC_007434.1.
DR PDB; 3D64; X-ray; 2.30 A; A/B=1-473.
DR PDB; 3GLQ; X-ray; 2.30 A; A/B=1-473.
DR PDBsum; 3D64; -.
DR PDBsum; 3GLQ; -.
DR AlphaFoldDB; Q3JY79; -.
DR SMR; Q3JY79; -.
DR EnsemblBacteria; ABA47924; ABA47924; BURPS1710b_0057.
DR GeneID; 56594006; -.
DR KEGG; bpm:BURPS1710b_0057; -.
DR HOGENOM; CLU_025194_2_1_4; -.
DR OMA; NKYGCRE; -.
DR OrthoDB; 522981at2; -.
DR UniPathway; UPA00314; UER00076.
DR EvolutionaryTrace; Q3JY79; -.
DR Proteomes; UP000002700; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.1480; -; 1.
DR HAMAP; MF_00563; AdoHcyase; 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 InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR PANTHER; PTHR23420; PTHR23420; 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; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00936; ahcY; 1.
DR PROSITE; PS00738; ADOHCYASE_1; 1.
DR PROSITE; PS00739; ADOHCYASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; NAD; One-carbon metabolism.
FT CHAIN 1..473
FT /note="Adenosylhomocysteinase"
FT /id="PRO_1000024718"
FT BINDING 64
FT /ligand="substrate"
FT BINDING 139
FT /ligand="substrate"
FT BINDING 199
FT /ligand="substrate"
FT BINDING 200..202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 229
FT /ligand="substrate"
FT BINDING 233
FT /ligand="substrate"
FT BINDING 234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 263..268
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 266..267
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT BINDING 286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT BINDING 321
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT BINDING 342..344
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 342..343
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT BINDING 387
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:3D64"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:3D64"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:3D64"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:3D64"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:3D64"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:3D64"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:3D64"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:3D64"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 201..212
FT /evidence="ECO:0007829|PDB:3D64"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 227..239
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 242..250
FT /evidence="ECO:0007829|PDB:3D64"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:3D64"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:3D64"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 289..296
FT /evidence="ECO:0007829|PDB:3D64"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:3D64"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:3D64"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:3D64"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 327..332
FT /evidence="ECO:0007829|PDB:3D64"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:3D64"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:3D64"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:3D64"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:3D64"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 396..416
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:3D64"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 429..440
FT /evidence="ECO:0007829|PDB:3D64"
FT TURN 441..444
FT /evidence="ECO:0007829|PDB:3D64"
FT HELIX 452..458
FT /evidence="ECO:0007829|PDB:3D64"
SQ SEQUENCE 473 AA; 52201 MW; 7A40ECDD0A47B596 CRC64;
MNAAVIDSHS AQDYVVADIA LAGWGRKELN IAETEMPGLV QIRDEYKAQQ PLKGARIAGS
LHMTIQTGVL IETLKALGAD VRWASCNIFS TQDHAAAAIV EAGTPVFAFK GESLDEYWEF
SHRIFEWPNG EFANMILDDG GDATLLLILG SKAEKDRSVI ARPTNEEEVA LFKSIERHLE
IDGSWYSKRL AHIKGVTEET TTGVHRLYQM EKDGRLPFPA FNVNDSVTKS KFDNLYGCRE
SLVDGIKRAT DVMIAGKIAV VAGYGDVGKG CAQSLRGLGA TVWVTEIDPI CALQAAMEGY
RVVTMEYAAD KADIFVTATG NYHVINHDHM KAMRHNAIVC NIGHFDSEID VASTRQYQWE
NIKPQVDHII FPDGKRVILL AEGRLVNLGC ATGHPSFVMS NSFTNQTLAQ IELFTRGGEY
ANKVYVLPKH LDEKVARLHL ARIGAQLSEL SDDQAAYIGV SKAGPFKPDH YRY
