SAHH_BRUA2
ID SAHH_BRUA2 Reviewed; 466 AA.
AC Q2YQX8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
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}; OrderedLocusNames=BAB1_2099;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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; AM040264; CAJ12055.1; -; Genomic_DNA.
DR RefSeq; WP_002965162.1; NZ_KN046823.1.
DR PDB; 3N58; X-ray; 2.39 A; A/B/C/D=8-466.
DR PDBsum; 3N58; -.
DR AlphaFoldDB; Q2YQX8; -.
DR SMR; Q2YQX8; -.
DR STRING; 359391.BAB1_2099; -.
DR EnsemblBacteria; CAJ12055; CAJ12055; BAB1_2099.
DR GeneID; 45053024; -.
DR GeneID; 55591665; -.
DR KEGG; bmf:BAB1_2099; -.
DR PATRIC; fig|359391.11.peg.1331; -.
DR HOGENOM; CLU_025194_2_0_5; -.
DR OMA; NKYGCRE; -.
DR PhylomeDB; Q2YQX8; -.
DR UniPathway; UPA00314; UER00076.
DR EvolutionaryTrace; Q2YQX8; -.
DR Proteomes; UP000002719; 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;
KW Reference proteome.
FT CHAIN 1..466
FT /note="Adenosylhomocysteinase"
FT /id="PRO_1000024711"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 193..195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 256..261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 335..337
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 380
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:3N58"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:3N58"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 159..174
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 226..243
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 282..290
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 320..325
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:3N58"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 379..383
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 389..408
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:3N58"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 422..432
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:3N58"
FT HELIX 445..451
FT /evidence="ECO:0007829|PDB:3N58"
SQ SEQUENCE 466 AA; 50791 MW; 6AB3B4B1C2F0BE41 CRC64;
MTASQDFVVK DISLADWGRK ELDIAETEMP GLMAAREEFG KSQPLKGARI SGSLHMTIQT
AVLIETLKVL GAEVRWASCN IFSTQDHAAA AIAATGTPVF AVKGETLEEY WTYTDQIFQW
PDGEPSNMIL DDGGDATMYI LIGARAEAGE DVLSNPQSEE EEVLFAQIKK RMAATPGFFT
KQRAAIKGVT EETTTGVNRL YQLQKKGLLP FPAINVNDSV TKSKFDNKYG CKESLVDGIR
RGTDVMMAGK VAVVCGYGDV GKGSAQSLAG AGARVKVTEV DPICALQAAM DGFEVVTLDD
AASTADIVVT TTGNKDVITI DHMRKMKDMC IVGNIGHFDN EIQVAALRNL KWTNVKPQVD
LIEFPDGKRL ILLSEGRLLN LGNATGHPSF VMSASFTNQV LGQIELFTRT DAYKNEVYVL
PKHLDEKVAR LHLDKLGAKL TVLSEEQAAY IGVTPQGPFK SEHYRY
