METY_CORGL
ID METY_CORGL Reviewed; 437 AA.
AC Q79VI4; Q93GI1;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=O-acetyl-L-homoserine sulfhydrylase {ECO:0000305};
DE Short=OAH-sulfhydrylase {ECO:0000305};
DE EC=2.5.1.49 {ECO:0000269|PubMed:11844756, ECO:0000269|PubMed:18050920, ECO:0000269|PubMed:20798582, ECO:0000269|Ref.4};
GN Name=metY {ECO:0000303|PubMed:11844756};
GN OrderedLocusNames=Cgl0653 {ECO:0000312|EMBL:BAB98046.1};
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP PROTEIN SEQUENCE OF 1-7, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=18050920;
RA Hwang B.J., Park S.D., Kim Y., Kim P., Lee H.S.;
RT "Biochemical analysis on the parallel pathways of methionine biosynthesis
RT in Corynebacterium glutamicum.";
RL J. Microbiol. Biotechnol. 17:1010-1017(2007).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=11844756; DOI=10.1128/jb.184.5.1277-1286.2002;
RA Hwang B.J., Yeom H.J., Kim Y., Lee H.S.;
RT "Corynebacterium glutamicum utilizes both transsulfuration and direct
RT sulfhydrylation pathways for methionine biosynthesis.";
RL J. Bacteriol. 184:1277-1286(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RA Yeom H.J., Hwang B.J., Lee M.S., Kim Y., Lee H.S.;
RT "Regulation of enzymes involved in methionine biosynthesis in
RT Corynebacterium glutamicum.";
RL J. Microbiol. Biotechnol. 14:373-378(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=20798582; DOI=10.4014/jmb.1002.02018;
RA Bolten C.J., Schroeder H., Dickschat J., Wittmann C.;
RT "Towards methionine overproduction in Corynebacterium
RT glutamicum-- methanethiol and dimethyldisulfide as reduced sulfur
RT sources.";
RL J. Microbiol. Biotechnol. 20:1196-1203(2010).
CC -!- FUNCTION: Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into
CC homocysteine in the methionine biosynthesis pathway (PubMed:11844756,
CC Ref.4, PubMed:18050920). Can also use dimethyldisulfide and
CC methanethiol as reduced sulfur sources, leading to the direct formation
CC of methionine (PubMed:20798582). Has weak cystathionine gamma-synthase
CC activity (PubMed:18050920). {ECO:0000269|PubMed:11844756,
CC ECO:0000269|PubMed:18050920, ECO:0000269|PubMed:20798582,
CC ECO:0000269|Ref.4}.
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; EC=2.5.1.49;
CC Evidence={ECO:0000269|PubMed:11844756, ECO:0000269|PubMed:18050920,
CC ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=methanethiol + O-acetyl-L-homoserine = acetate + H(+) + L-
CC methionine; Xref=Rhea:RHEA:10048, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16007, ChEBI:CHEBI:30089, ChEBI:CHEBI:57716,
CC ChEBI:CHEBI:57844; EC=2.5.1.49;
CC Evidence={ECO:0000269|PubMed:20798582};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q5SK88};
CC -!- ACTIVITY REGULATION: Inhibited by methionine and cystathionine.
CC {ECO:0000269|PubMed:18050920, ECO:0000269|Ref.4}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.4 mM for O-acetyl-L-homoserine {ECO:0000269|PubMed:18050920};
CC KM=8.6 mM for Na(2)S {ECO:0000269|PubMed:18050920};
CC Vmax=6.0 umol/min/mg enzyme toward O-acetyl-L-homoserine for the O-
CC acetyl-L-homoserine sulfhydrylase activity
CC {ECO:0000269|PubMed:18050920};
CC Vmax=8.0 umol/min/mg enzyme toward Na(2)S
CC {ECO:0000269|PubMed:18050920};
CC Vmax=1.5 umol/min/mg enzyme toward O-acetyl-L-homoserine for the
CC cystathionine gamma-synthase activity {ECO:0000269|PubMed:18050920};
CC Note=kcat is 28.0 sec(-1) with O-acetyl-L-homoserine as substrate for
CC the O-acetyl-L-homoserine sulfhydrylase activity. kcat is 37.3 sec(-
CC 1) with Na(2)S as substrate. kcat is 7.0 sec(-1) with O-acetyl-L-
CC homoserine as substrate for the cystathionine gamma-synthase
CC activity. {ECO:0000269|PubMed:18050920};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:18050920};
CC Temperature dependence:
CC Optimum temperature is 37-42 degrees Celsius.
CC {ECO:0000269|PubMed:18050920};
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:0000269|PubMed:11844756}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:18050920}.
CC -!- DEVELOPMENTAL STAGE: Activity is maximal during the early stationary
CC phase. {ECO:0000269|Ref.4}.
CC -!- INDUCTION: Expression is repressed by methionine.
CC {ECO:0000269|PubMed:11844756, ECO:0000269|Ref.4}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the metY gene is not enough to lead
CC to methionine auxotrophy, but the metB-metY double mutant is unable to
CC grow on a minimal medium lacking supplemental methionine
CC (PubMed:11844756). Deletion of the gene results in methionine
CC auxotrophy on methanethiol or dimethyldisulfide as sole sulfur source
CC (PubMed:20798582). {ECO:0000269|PubMed:11844756,
CC ECO:0000269|PubMed:20798582}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000036; BAB98046.1; -; Genomic_DNA.
DR RefSeq; NP_599886.1; NC_003450.3.
DR RefSeq; WP_003854667.1; NC_006958.1.
DR AlphaFoldDB; Q79VI4; -.
DR SMR; Q79VI4; -.
DR STRING; 196627.cg0755; -.
DR World-2DPAGE; 0001:Q79VI4; -.
DR GeneID; 58309420; -.
DR KEGG; cgl:Cgl0653; -.
DR PATRIC; fig|196627.13.peg.639; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_11; -.
DR OMA; TYTLFAH; -.
DR BioCyc; MetaCyc:G18NG-10215-MON; -.
DR UniPathway; UPA00051; UER00079.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0051009; F:O-acetylhomoserine sulfhydrylase activity; IEA:RHEA.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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 Amino-acid biosynthesis; Direct protein sequencing;
KW Methionine biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..437
FT /note="O-acetyl-L-homoserine sulfhydrylase"
FT /id="PRO_0000445418"
FT MOD_RES 216
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q5SK88"
SQ SEQUENCE 437 AA; 46752 MW; 51B63B03543EF291 CRC64;
MPKYDNSNAD QWGFETRSIH AGQSVDAQTS ARNLPIYQST AFVFDSAEHA KQRFALEDLG
PVYSRLTNPT VEALENRIAS LEGGVHAVAF SSGQAATTNA ILNLAGAGDH IVTSPRLYGG
TETLFLITLN RLGIDVSFVE NPDDPESWQA AVQPNTKAFF GETFANPQAD VLDIPAVAEV
AHRNSVPLII DNTIATAALV RPLELGADVV VASLTKFYTG NGSGLGGVLI DGGKFDWTVE
KDGKPVFPYF VTPDAAYHGL KYADLGAPAF GLKVRVGLLR DTGSTLSAFN AWAAVQGIDT
LSLRLERHNE NAIKVAEFLN NHEKVEKVNF AGLKDSPWYA TKEKLGLKYT GSVLTFEIKG
GKDEAWAFID ALKLHSNLAN IGDVRSLVVH PATTTHSQSD EAGLARAGVT QSTVRLSVGI
ETIDDIIADL EGGFAAI
