ID   Q93I77_THETH            Unreviewed;       421 AA.
AC   Q93I77;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   06-MAR-2013, entry version 50.
DE   SubName: Full=O-acetyl-L-homoserine sulfhydrylase;
DE            EC=2.5.1.49;
GN   Name=oah1;
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HB8;
RA   Shimizu H., Yamagata S., Masui R., Inoue Y., Shibata T., Yokoyama S.,
RA   Kuramitsu S., Iwama T.;
RT   "Cloning and overexpression of the gene encoding O-acetyl-L-homoserine
RT   sulfhydrylase of Thermus thermophilus HB8 and characterization of the
RT   gene product.";
RL   Biochim. Biophys. Acta 1549:61-72(2001).
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
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DR   EMBL; AB049221; BAB68505.1; -; Genomic_DNA.
DR   RefSeq; YP_144026.1; NC_006461.1.
DR   ProteinModelPortal; Q93I77; -.
DR   SMR; Q93I77; 1-421.
DR   GeneID; 3169894; -.
DR   KEGG; ttj:TTHA0760; -.
DR   KO; K01740; -.
DR   BioCyc; MetaCyc:MONOMER-16245; -.
DR   BRENDA; 2.5.1.49; 245.
DR   GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:GOC.
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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   PANTHER; PTHR11808; PTHR11808; 1.
DR   PANTHER; PTHR11808:SF12; PTHR11808:SF12; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   TIGRFAMs; TIGR01326; OAH_OAS_sulfhy; 1.
PE   3: Inferred from homology;
KW   Transferase.
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
//

ID   Q5SK88_THET8            Unreviewed;       421 AA.
AC   Q5SK88;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   01-MAY-2013, entry version 55.
DE   SubName: Full=O-acetyl-L-homoserine sulfhydrylase;
GN   OrderedLocusNames=TTHA0760;
OS   Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HB8 / ATCC 27634 / DSM 579;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y.,
RA   Shibata T., 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   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).
RA   Imagawa T., Kousumi Y., Tsuge H., Utsunomiya H., Ebihara A.,
RA   Nakagawa N., 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   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
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DR   EMBL; AP008226; BAD70583.1; -; Genomic_DNA.
DR   RefSeq; YP_144026.1; NC_006461.1.
DR   PDB; 2CTZ; X-ray; 2.60 A; A/B=1-421.
DR   PDBsum; 2CTZ; -.
DR   ProteinModelPortal; Q5SK88; -.
DR   SMR; Q5SK88; 1-421.
DR   STRING; 300852.TTHA0760; -.
DR   EnsemblBacteria; BAD70583; BAD70583; BAD70583.
DR   GeneID; 3169894; -.
DR   KEGG; ttj:TTHA0760; -.
DR   PATRIC; 23956497; VBITheThe93045_0753.
DR   eggNOG; COG2873; -.
DR   HOGENOM; HOG000246417; -.
DR   KO; K01740; -.
DR   OMA; FRNSEHA; -.
DR   ProtClustDB; CLSK738471; -.
DR   EvolutionaryTrace; Q5SK88; -.
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:0006520; P:cellular amino acid metabolic process; 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; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   PANTHER; PTHR11808; PTHR11808; 1.
DR   PANTHER; PTHR11808:SF12; PTHR11808:SF12; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   TIGRFAMs; TIGR01326; OAH_OAS_sulfhy; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Reference proteome.
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
//