SAHH_RHOCB
ID SAHH_RHOCB Reviewed; 463 AA.
AC P28183; D5AKH2;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 125.
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=RCAP_rcc00049;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=1631127; DOI=10.1073/pnas.89.14.6328;
RA Sganga M.W., Aksamit R.R., Cantoni G.L., Bauer C.E.;
RT "Mutational and nucleotide sequence analysis of S-adenosyl-L-homocysteine
RT hydrolase from Rhodobacter capsulatus.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6328-6332(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=8282711; DOI=10.1128/jb.176.1.61-69.1994;
RA Buggy J.J., Sganga M.W., Bauer C.E.;
RT "Nucleotide sequence and characterization of the Rhodobacter capsulatus
RT hvrB gene: HvrB is an activator of S-adenosyl-L-homocysteine hydrolase
RT expression and is a member of the LysR family.";
RL J. Bacteriol. 176:61-69(1994).
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 -!- SUBUNIT: Homotetramer.
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; M80630; AAA26094.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE83814.1; -; Genomic_DNA.
DR EMBL; L23836; AAA53540.1; -; Genomic_DNA.
DR PIR; A46035; A46035.
DR RefSeq; WP_013065796.1; NC_014034.1.
DR AlphaFoldDB; P28183; -.
DR SMR; P28183; -.
DR STRING; 272942.RCAP_rcc00049; -.
DR EnsemblBacteria; ADE83814; ADE83814; RCAP_rcc00049.
DR GeneID; 31489006; -.
DR KEGG; rcp:RCAP_rcc00049; -.
DR eggNOG; COG0499; Bacteria.
DR HOGENOM; CLU_025194_2_1_5; -.
DR OMA; NKYGCRE; -.
DR OrthoDB; 522981at2; -.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000002361; Chromosome.
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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; NAD; One-carbon metabolism; Reference proteome.
FT CHAIN 1..463
FT /note="Adenosylhomocysteinase"
FT /id="PRO_0000116983"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 190..192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 253..258
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 276
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 311
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 332..334
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 377
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT CONFLICT 157
FT /note="E -> D (in Ref. 1; AAA26094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 50594 MW; 44EBA9744B2FCA24 CRC64;
MADYIVKDIK LAEFGRKELD IAETEMPGLM ACREEFGPSQ PLKGARIAGS LHMTIQTAVL
IETLKALGAD VRWASCNIFS TQDHAAAAIA AGGTPVFAVK GETLEEYWAY TDKIFQFPEG
TCNMILDDGG DATLYILLGA RVEAGETDLI ATPTSEEEVC LFNQIKKRMV ESPGWFTQQR
AAIKGVSEET TTGVHRLYDL HKKGLLPFPA INVNDSVTKS KFDNKYGCKE SLVDGIRRAT
DVMMAGKVAV VCGYGDVGKG SAASLRGAGA RVKVTEVDPI CALQAAMDGF EVVVLEDVVA
DADIFITTTG NKDVIRIEHM REMKDMAIVG NIGHFDNEIQ VAALKNHKWT NIKDQVDMIE
MPSGARIILL SEGRLLNLGN ATGHPSFVMS ASFTNQVLAQ IELWTKGAEY QPGVYILPKS
LDEKVARLHL KKIGVKLTTL RPDQAEYIGV TVEGPFKSDH YRY
