(data stored in SCRATCH9089 zone)

SWISSPROT: 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   11-DEC-2019, entry version 100.
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;
RA   Woods D.E., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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   SMR; Q3JY79; -.
DR   PRIDE; Q3JY79; -.
DR   EnsemblBacteria; ABA47924; ABA47924; BURPS1710b_0057.
DR   KEGG; bpm:BURPS1710b_0057; -.
DR   HOGENOM; HOG000227986; -.
DR   KO; K01251; -.
DR   OMA; QSTWDGI; -.
DR   OrthoDB; 522981at2; -.
DR   BioCyc; BPSE320372:G1G58-75-MONOMER; -.
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;
DR   PRODOM; Q3JY79.
DR   SWISS-2DPAGE; Q3JY79.
KW   3D-structure; Cytoplasm; Hydrolase; NAD; One-carbon metabolism.
FT   CHAIN           1..473
FT                   /note="Adenosylhomocysteinase"
FT                   /id="PRO_1000024718"
FT   NP_BIND         200..202
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   NP_BIND         263..268
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   NP_BIND         266..267
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT                   ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT   NP_BIND         342..344
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   NP_BIND         342..343
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT                   ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT   BINDING         64
FT                   /note="Substrate"
FT   BINDING         139
FT                   /note="Substrate"
FT   BINDING         199
FT                   /note="Substrate"
FT   BINDING         229
FT                   /note="Substrate"
FT   BINDING         233
FT                   /note="Substrate"
FT   BINDING         234
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT   BINDING         286
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT                   ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT   BINDING         321
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT                   ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT   BINDING         387
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00563,
FT                   ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT   HELIX           19..21
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           22..32
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           33..35
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           37..45
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   TURN            46..49
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   TURN            51..54
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   STRAND          56..61
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           65..76
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   STRAND          80..84
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   STRAND          86..89
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           93..101
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           114..123
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   STRAND          135..141
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           142..155
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           157..160
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           166..179
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   TURN            183..186
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           187..190
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   STRAND          196..198
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           201..212
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   STRAND          220..222
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           227..239
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           242..250
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   STRAND          258..262
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           266..276
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   TURN            277..279
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   STRAND          281..285
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           289..296
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   TURN            297..299
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           305..308
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   TURN            309..311
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   STRAND          313..317
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   STRAND          319..322
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           327..332
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   STRAND          337..341
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   STRAND          343..346
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           352..354
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   STRAND          357..363
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   STRAND          366..370
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   STRAND          376..380
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           381..383
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           386..389
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           396..416
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           417..419
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   STRAND          422..426
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           429..440
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   TURN            441..444
FT                   /evidence="ECO:0000244|PDB:3D64"
FT   HELIX           452..458
FT                   /evidence="ECO:0000244|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
//

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