METY_THEMA
ID METY_THEMA Reviewed; 430 AA.
AC Q9WZY4; G4FCU3; R4NZF8;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=O-acetyl-L-homoserine sulfhydrylase;
DE Short=OAH sulfhydrylase;
DE EC=2.5.1.- {ECO:0000269|PubMed:23637642};
DE AltName: Full=O-acetylhomoserine thiolase {ECO:0000303|PubMed:23637642};
GN OrderedLocusNames=TM_0882 {ECO:0000312|EMBL:AAD35963.1};
GN ORFNames=Tmari_0884 {ECO:0000312|EMBL:AGL49809.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485;
RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H.,
RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y.,
RA Zengler K.;
RT "The genome organization of Thermotoga maritima reflects its lifestyle.";
RL PLoS Genet. 9:E1003485-E1003485(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND PATHWAY.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=28640457; DOI=10.1111/mmi.13737;
RA Ferla M.P., Brewster J.L., Hall K.R., Evans G.B., Patrick W.M.;
RT "Primordial-like enzymes from bacteria with reduced genomes.";
RL Mol. Microbiol. 105:508-524(2017).
CC -!- FUNCTION: Catalyzes the production of homocysteine from O-
CC acetylhomoserine (OAH) and hydrogen sulfide (H2S), a step in the
CC methionine biosynthesis pathway. Is not able to form cystathionine from
CC O-acetylhomoserine and L-cysteine. {ECO:0000269|PubMed:28640457}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + O-acetyl-L-homoserine = acetate + L-
CC homocysteine; Xref=Rhea:RHEA:27822, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57716, ChEBI:CHEBI:58199;
CC Evidence={ECO:0000269|PubMed:28640457};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27823;
CC Evidence={ECO:0000305|PubMed:28640457};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q5SK88};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homocysteine from O-acetyl-L-homoserine: step 1/1.
CC {ECO:0000305|PubMed:28640457}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; AE000512; AAD35963.1; -; Genomic_DNA.
DR EMBL; CP004077; AGL49809.1; -; Genomic_DNA.
DR PIR; D72324; D72324.
DR RefSeq; NP_228690.1; NC_000853.1.
DR RefSeq; WP_004080710.1; NZ_CP011107.1.
DR PDB; 7KB0; X-ray; 1.85 A; A=1-430.
DR PDB; 7KB1; X-ray; 1.85 A; A/B/C/D=1-430.
DR PDBsum; 7KB0; -.
DR PDBsum; 7KB1; -.
DR AlphaFoldDB; Q9WZY4; -.
DR SMR; Q9WZY4; -.
DR STRING; 243274.THEMA_00225; -.
DR DNASU; 898556; -.
DR EnsemblBacteria; AAD35963; AAD35963; TM_0882.
DR EnsemblBacteria; AGL49809; AGL49809; Tmari_0884.
DR KEGG; tma:TM0882; -.
DR KEGG; tmm:Tmari_0884; -.
DR KEGG; tmw:THMA_0904; -.
DR PATRIC; fig|243274.17.peg.883; -.
DR eggNOG; COG2873; Bacteria.
DR InParanoid; Q9WZY4; -.
DR OMA; TYTLFAH; -.
DR OrthoDB; 637281at2; -.
DR UniPathway; UPA00051; UER00079.
DR Proteomes; UP000008183; Chromosome.
DR Proteomes; UP000013901; Chromosome.
DR GO; GO:0051009; F:O-acetylhomoserine sulfhydrylase activity; IEA:RHEA.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01326; OAH_OAS_sulfhy; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Methionine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..430
FT /note="O-acetyl-L-homoserine sulfhydrylase"
FT /id="PRO_0000448376"
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q5SK88"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:7KB0"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:7KB0"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:7KB1"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:7KB1"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:7KB0"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:7KB0"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:7KB0"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:7KB0"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:7KB0"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:7KB0"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:7KB0"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:7KB0"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:7KB0"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:7KB0"
FT TURN 208..213
FT /evidence="ECO:0007829|PDB:7KB1"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:7KB0"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 251..255
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 259..266
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 278..288
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 291..310
FT /evidence="ECO:0007829|PDB:7KB0"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 329..335
FT /evidence="ECO:0007829|PDB:7KB0"
FT STRAND 342..348
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:7KB0"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:7KB0"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:7KB0"
FT TURN 384..388
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 391..396
FT /evidence="ECO:0007829|PDB:7KB0"
FT STRAND 403..407
FT /evidence="ECO:0007829|PDB:7KB0"
FT HELIX 413..427
FT /evidence="ECO:0007829|PDB:7KB0"
SQ SEQUENCE 430 AA; 47031 MW; 4A3332FCA6DF4B79 CRC64;
MDWKKYGYNT RALHAGYEPP EQATGSRAVP IYQTTSYVFR DSDHAARLFA LEEPGFIYTR
IGNPTVSVLE ERIAALEEGV GALAVASGQA AITYAILNIA GPGDEIVSGS ALYGGTYNLF
RHTLYKKSGI IVKFVDETDP KNIEEAITEK TKAVYLETIG NPGLTVPDFE AIAEIAHRHG
VPLIVDNTVA PYIFRPFEHG ADIVVYSATK FIGGHGTSIG GLIVDSGKFD WTNGKFPELV
EPDPSYHGVS YVETFKEAAY IAKCRTQLLR DLGSCMSPFN AFLFILGLET LSLRMKKHCE
NALKIVEFLK SHPAVSWVNY PIAEGNKTRE NALKYLKEGY GAIVTFGVKG GKEAGKKFID
SLTLISHLAN IGDARTLAIH PASTTHQQLT EEEQLKTGVT PDMIRLSVGI EDVEDIIADL
DQALRKSQEG
