METY1_THET8
ID METY1_THET8 Reviewed; 421 AA.
AC Q5SK88; Q93I77;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=O-acetyl-L-homoserine sulfhydrylase 1 {ECO:0000303|PubMed:11566369};
DE Short=OAH-sulfhydrylase 1 {ECO:0000303|PubMed:11566369};
DE EC=2.5.1.- {ECO:0000269|PubMed:11566369};
GN Name=oah1 {ECO:0000303|PubMed:11566369};
GN OrderedLocusNames=TTHA0760 {ECO:0000312|EMBL:BAD70583.1};
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=11566369; DOI=10.1016/s0167-4838(01)00245-x;
RA Shimizu H., Yamagata S., Masui R., Inoue Y., Shibata T., Yokoyama S.,
RA Kuramitsu S., Iwama T.;
RT "Cloning and overexpression of the oah1 gene encoding O-acetyl-L-homoserine
RT sulfhydrylase of Thermus thermophilus HB8 and characterization of the gene
RT product.";
RL Biochim. Biophys. Acta 1549:61-72(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:2CTZ}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), PYRIDOXAL PHOSPHATE AT LYS-206, AND
RP COFACTOR.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Imagawa T., Kousumi Y., Tsuge H., Utsunomiya H., Ebihara A., Nakagawa N.,
RA Yokoyama S., Kuramitsu S.;
RT "Crystal structure of O-acetyl homoserine sulfhydrylase from Thermus
RT thermophilus HB8.";
RL Submitted (MAY-2005) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into
CC homocysteine in the methionine biosynthesis pathway. Has weak activity
CC with O-acetyl-L-serine, O-phospho-L-serine, L-serine, O-succinyl-L-
CC homoserine and L-homoserine. Shows low CTT beta-lyase activity and very
CC low CTT gamma-synthase activity. {ECO:0000269|PubMed:11566369}.
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:11566369};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|Ref.3, ECO:0000305|PubMed:11566369};
CC -!- ACTIVITY REGULATION: Inhibited by the carbonyl reagents hydroxylamine
CC and phenylhydrazine. Also inhibited by methionine and propargylglycine.
CC {ECO:0000269|PubMed:11566369}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.8 mM for O-acetyl-L-homoserine {ECO:0000269|PubMed:11566369};
CC KM=1.3 mM for sulfide {ECO:0000269|PubMed:11566369};
CC Vmax=165 umol/min/mg enzyme {ECO:0000269|PubMed:11566369};
CC pH dependence:
CC Optimum pH is 7.8. Shows high pH stability over a wide range of pH
CC (pH 4-12). {ECO:0000269|PubMed:11566369};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. Very stable at high
CC temperature. 90% of the activity is retained after treatment at 90
CC degrees Celsius for 60 min. {ECO:0000269|PubMed:11566369};
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:11566369}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11566369}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; AB049221; BAB68505.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70583.1; -; Genomic_DNA.
DR RefSeq; WP_011228178.1; NC_006461.1.
DR RefSeq; YP_144026.1; NC_006461.1.
DR PDB; 2CTZ; X-ray; 2.60 A; A/B=1-421.
DR PDBsum; 2CTZ; -.
DR AlphaFoldDB; Q5SK88; -.
DR SMR; Q5SK88; -.
DR STRING; 300852.55772142; -.
DR EnsemblBacteria; BAD70583; BAD70583; BAD70583.
DR GeneID; 3169894; -.
DR KEGG; ttj:TTHA0760; -.
DR PATRIC; fig|300852.9.peg.753; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_0; -.
DR OMA; TYTLFAH; -.
DR PhylomeDB; Q5SK88; -.
DR BRENDA; 2.5.1.49; 2305.
DR UniPathway; UPA00051; UER00079.
DR EvolutionaryTrace; Q5SK88; -.
DR Proteomes; UP000000532; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Methionine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..421
FT /note="O-acetyl-L-homoserine sulfhydrylase 1"
FT /id="PRO_0000445420"
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|Ref.3"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:2CTZ"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:2CTZ"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:2CTZ"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:2CTZ"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:2CTZ"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:2CTZ"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:2CTZ"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:2CTZ"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:2CTZ"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:2CTZ"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:2CTZ"
FT TURN 204..209
FT /evidence="ECO:0007829|PDB:2CTZ"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:2CTZ"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 247..251
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 255..262
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 274..284
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 287..306
FT /evidence="ECO:0007829|PDB:2CTZ"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 325..332
FT /evidence="ECO:0007829|PDB:2CTZ"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:2CTZ"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:2CTZ"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:2CTZ"
FT TURN 380..384
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 387..392
FT /evidence="ECO:0007829|PDB:2CTZ"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:2CTZ"
FT HELIX 409..419
FT /evidence="ECO:0007829|PDB:2CTZ"
SQ SEQUENCE 421 AA; 46088 MW; 99E91B056D4FA77E CRC64;
MRFETLQLHA GYEPEPTTLS RQVPIYPTTS YVFKSPEHAA NLFALKEFGN IYSRIMNPTV
DVLEKRLAAL EGGKAALATA SGHAAQFLAL TTLAQAGDNI VSTPNLYGGT FNQFKVTLKR
LGIEVRFTSR EERPEEFLAL TDEKTRAWWV ESIGNPALNI PDLEALAQAA REKGVALIVD
NTFGMGGYLL RPLAWGAALV THSLTKWVGG HGAVIAGAIV DGGNFPWEGG RYPLLTEPQP
GYHGLRLTEA FGELAFIVKA RVDGLRDQGQ ALGPFEAWVV LLGMETLSLR AERHVENTLH
LAHWLLEQPQ VAWVNYPGLP HHPHHDRAQK YFKGKPGAVL TFGLKGGYEA AKRFISRLKL
ISHLANVGDT RTLAIHPAST THSQLSPEEQ AQAGVSPEMV RLSVGLEHVE DLKAELKEAL
A
