SAHH_PSEAE
ID SAHH_PSEAE Reviewed; 469 AA.
AC Q9I685;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
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}; Synonyms=sahH;
GN OrderedLocusNames=PA0432;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00563};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00563};
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; AE004091; AAG03821.1; -; Genomic_DNA.
DR PIR; H83591; H83591.
DR RefSeq; NP_249123.1; NC_002516.2.
DR RefSeq; WP_003099900.1; NZ_QZGE01000016.1.
DR PDB; 6F3N; X-ray; 1.85 A; A/B/C/D=1-469.
DR PDB; 6F3O; X-ray; 1.75 A; A/B/C/D=1-469.
DR PDB; 6F3P; X-ray; 1.35 A; A/C=1-469.
DR PDB; 6F3Q; X-ray; 1.45 A; A/B/C/D=1-469.
DR PDBsum; 6F3N; -.
DR PDBsum; 6F3O; -.
DR PDBsum; 6F3P; -.
DR PDBsum; 6F3Q; -.
DR AlphaFoldDB; Q9I685; -.
DR SMR; Q9I685; -.
DR STRING; 287.DR97_3400; -.
DR PaxDb; Q9I685; -.
DR PRIDE; Q9I685; -.
DR EnsemblBacteria; AAG03821; AAG03821; PA0432.
DR GeneID; 877746; -.
DR KEGG; pae:PA0432; -.
DR PATRIC; fig|208964.12.peg.454; -.
DR PseudoCAP; PA0432; -.
DR HOGENOM; CLU_025194_2_1_6; -.
DR InParanoid; Q9I685; -.
DR OMA; NKYGCRE; -.
DR PhylomeDB; Q9I685; -.
DR BioCyc; PAER208964:G1FZ6-436-MON; -.
DR BRENDA; 3.3.1.1; 5087.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IBA:GO_Central.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.1480; -; 3.
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;
KW Reference proteome.
FT CHAIN 1..469
FT /note="Adenosylhomocysteinase"
FT /id="PRO_0000116977"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 165..167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 228..233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 251
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 321..323
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 375
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:6F3N"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:6F3P"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:6F3P"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:6F3P"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:6F3P"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:6F3P"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:6F3N"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:6F3P"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 142..150
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:6F3P"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:6F3P"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 198..215
FT /evidence="ECO:0007829|PDB:6F3P"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:6F3P"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:6F3P"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:6F3P"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:6F3P"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 306..311
FT /evidence="ECO:0007829|PDB:6F3P"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:6F3P"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 330..336
FT /evidence="ECO:0007829|PDB:6F3P"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:6F3P"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:6F3P"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 374..378
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 384..404
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 411..417
FT /evidence="ECO:0007829|PDB:6F3P"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:6F3O"
FT HELIX 425..438
FT /evidence="ECO:0007829|PDB:6F3P"
FT HELIX 448..454
FT /evidence="ECO:0007829|PDB:6F3P"
SQ SEQUENCE 469 AA; 51400 MW; DE28D5CC7F802BCC CRC64;
MSAVMTPAGF TDYKVADITL AAWGRRELII AESEMPALMG LRRKYAGQQP LKGAKILGCI
HMTIQTGVLI ETLVALGAEV RWSSCNIFST QDQAAAAIAA AGIPVFAWKG ETEEEYEWCI
EQTILKDGQP WDANMVLDDG GDLTEILHKK YPQMLERIHG ITEETTTGVH RLLDMLKNGT
LKVPAINVND SVTKSKNDNK YGCRHSLNDA IKRGTDHLLS GKQALVIGYG DVGKGSSQSL
RQEGMIVKVA EVDPICAMQA CMDGFEVVSP YKNGINDGTE ASIDAALLGK IDLIVTTTGN
VNVCDANMLK ALKKRAVVCN IGHFDNEIDT AFMRKNWAWE EVKPQVHKIH RTGKDGFDAH
NDDYLILLAE GRLVNLGNAT GHPSRIMDGS FANQVLAQIH LFEQKYADLP AAEKAKRLSV
EVLPKKLDEE VALEMVKGFG GVVTQLTPKQ AEYIGVSVEG PFKPDTYRY
