ID E1QQJ4_VULDI Unreviewed; 438 AA.
AC E1QQJ4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Adenosylhomocysteinase {ECO:0000256|HAMAP-Rule:MF_00563};
DE EC=3.13.2.1 {ECO:0000256|HAMAP-Rule:MF_00563};
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000256|HAMAP-Rule:MF_00563};
DE Short=AdoHcyase {ECO:0000256|HAMAP-Rule:MF_00563};
GN Name=ahcY {ECO:0000256|HAMAP-Rule:MF_00563};
GN OrderedLocusNames=Vdis_1101 {ECO:0000313|EMBL:ADN50489.1};
OS Vulcanisaeta distributa (strain DSM 14429 / JCM 11212 / NBRC 100878 /
OS IC-017).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=572478 {ECO:0000313|EMBL:ADN50489.1, ECO:0000313|Proteomes:UP000006681};
RN [1] {ECO:0000313|EMBL:ADN50489.1, ECO:0000313|Proteomes:UP000006681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14429 / JCM 11212 / NBRC 100878 / IC-017
RC {ECO:0000313|Proteomes:UP000006681};
RX PubMed=21304741;
RA Mavromatis K., Sikorski J., Pabst E., Teshima H., Lapidus A., Lucas S.,
RA Nolan M., Glavina Del Rio T., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S.,
RA Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Vulcanisaeta distributa type strain (IC-
RT 017).";
RL Stand. Genomic Sci. 3:117-125(2010).
RN [2] {ECO:0000313|Proteomes:UP000006681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14429 / JCM 11212 / NBRC 100878 / IC-017
RC {ECO:0000313|Proteomes:UP000006681};
RX DOI=10.4056/sigs.1113067;
RA Mavromatis K., Sikorski J., Pabst E., Teshima H., Lapidus A., Lucas S.,
RA Nolan M., Glavina Del Rio T., Cheng J., Bruce D., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y., Jeffries C., Rohde M., Spring S., Goker M.,
RA Wirth R., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA Klenk H., Kyrpides N.;
RT "Complete genome sequence of Vulcanisaeta distributa type strain (IC-
RT 017T).";
RL Stand. Genomic Sci. 3:117-125(2010).
CC -!- FUNCTION: May play a key role in the regulation of the intracellular
CC concentration of adenosylhomocysteine. {ECO:0000256|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=3.13.2.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00563};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00563,
CC ECO:0000256|PIRSR:PIRSR001109-2};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|HAMAP-Rule:MF_00563,
CC ECO:0000256|PIRSR:PIRSR001109-2};
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC {ECO:0000256|HAMAP-Rule:MF_00563}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000256|ARBA:ARBA00007122, ECO:0000256|HAMAP-Rule:MF_00563,
CC ECO:0000256|RuleBase:RU004166}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00563}.
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DR EMBL; CP002100; ADN50489.1; -; Genomic_DNA.
DR RefSeq; WP_013336214.1; NC_014537.1.
DR AlphaFoldDB; E1QQJ4; -.
DR STRING; 572478.Vdis_1101; -.
DR GeneID; 9752032; -.
DR KEGG; vdi:Vdis_1101; -.
DR eggNOG; arCOG04137; Archaea.
DR HOGENOM; CLU_025194_2_1_2; -.
DR OrthoDB; 8479at2157; -.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000006681; 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; Adenosylhomocysteinase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR00936; ahcY; 1.
DR PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 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; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00738; ADOHCYASE_1; 1.
DR PROSITE; PS00739; ADOHCYASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00563};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00563, ECO:0000313|EMBL:ADN50489.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00563};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW Rule:MF_00563}; Reference proteome {ECO:0000313|Proteomes:UP000006681}.
FT DOMAIN 204..366
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 170..172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT BINDING 233..238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563"
FT BINDING 235..240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 257
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 313..315
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 360
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00563,
FT ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 367
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 438 AA; 48295 MW; 20E53065BBA2F71A CRC64;
MTYKVKDISL AEKGRLLIEW AERHMPVLMK IRERFTREKP LDGIRISASL HVTKETAVLV
RTLVAGGATV TLVPSNPLST QDEVAAALAE DGIYVYAWKG MNEREYYNAI GFAISQEPVV
TMDDGADLTV TLHKLALGVK SNEVNYALET AGDRDFAKLI SSVYGGTEET TTGVIRLRAM
AREGTLRYPI IAVNDSYTKY LFDNRYGTGQ STWDGILRAT NILVAGKVVV VAGYGWVGRG
IAMRAKGLGA RRVIVTEVNP VRALEAVFDG FEVMPMSEAA EIGDIFITAT GDINAITLDH
ILKMKDGAVL ANAGHFNVEI DVAGLERVAA EKRKIRDYVV EYRLPNGKRV YLLAEGRLVN
LVAAEGHPSE VMDMSFSNQA LAVEYIVKNR GKLQLGVHKL PDELDMEVAR LKLETMGIRI
DQLTEEQRRY ISSWGLGT
//
