METY2_THET8
ID METY2_THET8 Reviewed; 412 AA.
AC Q5SJ58; Q76K51;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=O-acetyl-L-homoserine sulfhydrylase 2 {ECO:0000303|PubMed:15215603};
DE Short=OAH-sulfhydrylase 2 {ECO:0000303|PubMed:15215603};
DE EC=2.5.1.- {ECO:0000269|PubMed:15215603};
GN Name=oah2 {ECO:0000303|PubMed:15215603};
GN OrderedLocusNames=TTHA1156 {ECO:0000312|EMBL:BAD70979.1};
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, AND SUBUNIT.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=15215603; DOI=10.1271/bbb.68.1357;
RA Iwama T., Hosokawa H., Lin W., Shimizu H., Kawai K., Yamagata S.;
RT "Comparative characterization of the oah2 gene homologous to the oah1 of
RT Thermus thermophilus HB8.";
RL Biosci. Biotechnol. Biochem. 68:1357-1361(2004).
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:2CB1}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), PYRIDOXAL PHOSPHATE AT LYS-202, AND
RP COFACTOR.
RA Agari Y., Satoh S., Tsuge H., Imagawa T., Utsunomiya H.;
RT "The crystal structure of O-acetyl homoserine sulfhydrylase.";
RL Submitted (DEC-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 a very low CTT gamma-synthase
CC activity. {ECO:0000269|PubMed:15215603}.
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:15215603};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|Ref.3, ECO:0000305|PubMed:15215603};
CC -!- ACTIVITY REGULATION: Inhibited by the carbonyl reagents hydroxylamine
CC and phenylhydrazine. Also inhibited by methionine and propargylglycine.
CC {ECO:0000269|PubMed:15215603}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.0 mM for O-acetyl-L-homoserine {ECO:0000269|PubMed:15215603};
CC Vmax=126 umol/min/mg enzyme {ECO:0000269|PubMed:15215603};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:15215603};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. Stable at high
CC temperature. 80% of the activity is retained after treatment at 90
CC degrees Celsius for 60 min. {ECO:0000269|PubMed:15215603};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15215603}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; AB094564; BAD02479.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70979.1; -; Genomic_DNA.
DR RefSeq; WP_011228474.1; NC_006461.1.
DR RefSeq; YP_144422.1; NC_006461.1.
DR PDB; 2CB1; X-ray; 2.00 A; A=1-412.
DR PDBsum; 2CB1; -.
DR AlphaFoldDB; Q5SJ58; -.
DR SMR; Q5SJ58; -.
DR STRING; 300852.55772538; -.
DR EnsemblBacteria; BAD70979; BAD70979; BAD70979.
DR GeneID; 3168441; -.
DR KEGG; ttj:TTHA1156; -.
DR PATRIC; fig|300852.9.peg.1136; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_0; -.
DR OMA; FNAWVLS; -.
DR PhylomeDB; Q5SJ58; -.
DR BRENDA; 2.5.1.49; 2305.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Methionine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..412
FT /note="O-acetyl-L-homoserine sulfhydrylase 2"
FT /id="PRO_0000445421"
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2CB1"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:2CB1"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:2CB1"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:2CB1"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:2CB1"
FT TURN 115..120
FT /evidence="ECO:0007829|PDB:2CB1"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:2CB1"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:2CB1"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:2CB1"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:2CB1"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:2CB1"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:2CB1"
FT TURN 200..205
FT /evidence="ECO:0007829|PDB:2CB1"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:2CB1"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 279..298
FT /evidence="ECO:0007829|PDB:2CB1"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:2CB1"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:2CB1"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:2CB1"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:2CB1"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:2CB1"
FT TURN 366..373
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 376..381
FT /evidence="ECO:0007829|PDB:2CB1"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:2CB1"
FT HELIX 398..410
FT /evidence="ECO:0007829|PDB:2CB1"
SQ SEQUENCE 412 AA; 44184 MW; 9E1D32FC22D4E470 CRC64;
MEYTTLAVLA GLPEDPHGAV GLPIYAVAAY GFKTLEEGQE RFATGEGYVY ARQKDPTAKA
LEERLKALEG ALEAVVLASG QAATFAALLA LLRPGDEVVA AKGLFGQTIG LFGQVLSLMG
VTVRYVDPEP EAVREALSAK TRAVFVETVA NPALLVPDLE ALATLAEEAG VALVVDNTFG
AAGALCRPLA WGAHVVVESL TKWASGHGSV LGGAVLSRET ELWRNYPQFL QPDLKGQIPW
EALRARCFPE RVRTLGLSLC GMALSPFNAY LLFQGLETVA LRVARMSETA RFLAERLQGH
PKVKALRYPG LPEDPAHRNA RKYLASGGPI LTLDLGDLER ASRFLGAIRL LKAANLGDAR
TLLVHPWTTT HSRLKEEARL QAGVTPGLVR VSVGLEDPLD LLALFEEALE AV
