SAHH_MYCTU
ID SAHH_MYCTU Reviewed; 495 AA.
AC P9WGV3; L0TBZ4; O08364; P60176; P81858;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 51.
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=Rv3248c; ORFNames=MTCY20B11.23c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PUPYLATION AT LYS-474, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NAD; ADENOSINE AND
RP INHIBITORS, COFACTOR, AND SUBUNIT.
RX PubMed=18815415; DOI=10.1110/ps.038125.108;
RA Reddy M.C., Kuppan G., Shetty N.D., Owen J.L., Ioerger T.R.,
RA Sacchettini J.C.;
RT "Crystal structures of Mycobacterium tuberculosis S-adenosyl-L-homocysteine
RT hydrolase in ternary complex with substrate and inhibitors.";
RL Protein Sci. 17:2134-2144(2008).
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 ECO:0000269|PubMed:18815415};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00563,
CC ECO:0000269|PubMed:18815415};
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. {ECO:0000269|PubMed:18815415}.
CC -!- INTERACTION:
CC P9WGV3; P10145: CXCL8; Xeno; NbExp=3; IntAct=EBI-11740468, EBI-3917999;
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; AL123456; CCP46067.1; -; Genomic_DNA.
DR PIR; B70593; B70593.
DR RefSeq; NP_217765.1; NC_000962.3.
DR RefSeq; WP_003417039.1; NZ_NVQJ01000003.1.
DR PDB; 2ZIZ; X-ray; 2.20 A; A/B/C/D=1-495.
DR PDB; 2ZJ0; X-ray; 2.42 A; A/B/C/D=1-495.
DR PDB; 2ZJ1; X-ray; 2.01 A; A/B/C/D=1-495.
DR PDB; 3CE6; X-ray; 1.60 A; A/B/C/D=2-495.
DR PDB; 3DHY; X-ray; 2.00 A; A/B/C/D=1-495.
DR PDBsum; 2ZIZ; -.
DR PDBsum; 2ZJ0; -.
DR PDBsum; 2ZJ1; -.
DR PDBsum; 3CE6; -.
DR PDBsum; 3DHY; -.
DR AlphaFoldDB; P9WGV3; -.
DR SMR; P9WGV3; -.
DR IntAct; P9WGV3; 1.
DR STRING; 83332.Rv3248c; -.
DR DrugBank; DB07052; 5'-S-ethyl-5'-thioadenosine.
DR PaxDb; P9WGV3; -.
DR DNASU; 888746; -.
DR GeneID; 45427242; -.
DR GeneID; 888746; -.
DR KEGG; mtu:Rv3248c; -.
DR TubercuList; Rv3248c; -.
DR eggNOG; COG0499; Bacteria.
DR OMA; NKYGCRE; -.
DR PhylomeDB; P9WGV3; -.
DR BRENDA; 3.3.1.1; 3445.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005576; C:extracellular region; IDA:CAFA.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IDA:MTBBASE.
DR GO; GO:0070403; F:NAD+ binding; IDA:MTBBASE.
DR GO; GO:0035375; F:zymogen binding; IPI:CAFA.
DR GO; GO:0046085; P:adenosine metabolic process; IDA:MTBBASE.
DR GO; GO:0044650; P:adhesion of symbiont to host cell; IMP:AgBase.
DR GO; GO:0035635; P:entry of bacterium into host cell; IMP:AgBase.
DR GO; GO:0009087; P:methionine catabolic process; IDA:MTBBASE.
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; -; 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; Isopeptide bond; NAD;
KW One-carbon metabolism; Reference proteome; Ubl conjugation.
FT CHAIN 1..495
FT /note="Adenosylhomocysteinase"
FT /id="PRO_0000116971"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 219..221
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 253
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 282..287
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 305
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 340
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 361..363
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT BINDING 409
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00563"
FT CROSSLNK 474
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:3CE6"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3CE6"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:3DHY"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:3CE6"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:3DHY"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3DHY"
FT HELIX 130..141
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 185..200
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 204..211
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 220..231
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 252..269
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 285..296
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 308..316
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 346..351
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 370..375
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:3CE6"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 408..412
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 418..437
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:3CE6"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 451..465
FT /evidence="ECO:0007829|PDB:3CE6"
FT HELIX 474..480
FT /evidence="ECO:0007829|PDB:3CE6"
SQ SEQUENCE 495 AA; 54324 MW; 386EF292620E7327 CRC64;
MTGNLVTKNS LTPDVRNGID FKIADLSLAD FGRKELRIAE HEMPGLMSLR REYAEVQPLK
GARISGSLHM TVQTAVLIET LTALGAEVRW ASCNIFSTQD HAAAAVVVGP HGTPDEPKGV
PVFAWKGETL EEYWWAAEQM LTWPDPDKPA NMILDDGGDA TMLVLRGMQY EKAGVVPPAE
EDDPAEWKVF LNLLRTRFET DKDKWTKIAE SVKGVTEETT TGVLRLYQFA AAGDLAFPAI
NVNDSVTKSK FDNKYGTRHS LIDGINRGTD ALIGGKKVLI CGYGDVGKGC AEAMKGQGAR
VSVTEIDPIN ALQAMMEGFD VVTVEEAIGD ADIVVTATGN KDIIMLEHIK AMKDHAILGN
IGHFDNEIDM AGLERSGATR VNVKPQVDLW TFGDTGRSII VLSEGRLLNL GNATGHPSFV
MSNSFANQTI AQIELWTKND EYDNEVYRLP KHLDEKVARI HVEALGGHLT KLTKEQAEYL
GVDVEGPYKP DHYRY
