METZ_MYCTU
ID METZ_MYCTU Reviewed; 406 AA.
AC P9WGB5; L0T3J4; P95199; Q7D9W7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=O-succinylhomoserine sulfhydrylase {ECO:0000255|HAMAP-Rule:MF_02056, ECO:0000303|Ref.3};
DE Short=OSH sulfhydrylase {ECO:0000255|HAMAP-Rule:MF_02056};
DE Short=OSHS sulfhydrylase {ECO:0000255|HAMAP-Rule:MF_02056};
DE EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_02056};
GN Name=metZ {ECO:0000255|HAMAP-Rule:MF_02056}; OrderedLocusNames=Rv0391;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH PLP, COFACTOR, AND
RP SUBUNIT.
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "Crystal structure of O-succinylhomoserine sulfhydrylase from Mycobacterium
RT tuberculosis covalently bound to pyridoxal-5-phosphate.";
RL Submitted (JUN-2010) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the formation of L-homocysteine from O-succinyl-L-
CC homoserine (OSHS) and hydrogen sulfide. {ECO:0000255|HAMAP-
CC Rule:MF_02056}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + O-succinyl-L-homoserine = L-homocysteine +
CC succinate; Xref=Rhea:RHEA:27826, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57661, ChEBI:CHEBI:58199;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02056};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02056, ECO:0000269|Ref.3};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000269|Ref.3};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homocysteine from O-succinyl-L-homoserine: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_02056}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_02056,
CC ECO:0000305|Ref.3}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. MetZ
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02056, ECO:0000305}.
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DR EMBL; AL123456; CCP43121.1; -; Genomic_DNA.
DR PIR; F70632; F70632.
DR RefSeq; NP_214905.1; NC_000962.3.
DR RefSeq; WP_003401927.1; NZ_NVQJ01000002.1.
DR PDB; 3NDN; X-ray; 1.85 A; A/B/C/D=1-406.
DR PDBsum; 3NDN; -.
DR AlphaFoldDB; P9WGB5; -.
DR SMR; P9WGB5; -.
DR STRING; 83332.Rv0391; -.
DR PaxDb; P9WGB5; -.
DR DNASU; 886431; -.
DR GeneID; 886431; -.
DR KEGG; mtu:Rv0391; -.
DR TubercuList; Rv0391; -.
DR eggNOG; COG0626; Bacteria.
DR OMA; FNAWVLS; -.
DR PhylomeDB; P9WGB5; -.
DR UniPathway; UPA00051; UER00449.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProtKB-UniRule.
DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IBA:GO_Central.
DR GO; GO:0071268; P:homocysteine biosynthetic process; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_02056; MetZ; 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR006234; O-succ-hSer_sulfhydrylase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808; PTHR11808; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01325; O_suc_HS_sulf; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Methionine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..406
FT /note="O-succinylhomoserine sulfhydrylase"
FT /id="PRO_0000416406"
FT MOD_RES 219
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02056,
FT ECO:0000269|Ref.3"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:3NDN"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3NDN"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:3NDN"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:3NDN"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:3NDN"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:3NDN"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:3NDN"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:3NDN"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:3NDN"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:3NDN"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:3NDN"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:3NDN"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 242..250
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 269..288
FT /evidence="ECO:0007829|PDB:3NDN"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 307..313
FT /evidence="ECO:0007829|PDB:3NDN"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 332..342
FT /evidence="ECO:0007829|PDB:3NDN"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:3NDN"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:3NDN"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 371..377
FT /evidence="ECO:0007829|PDB:3NDN"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:3NDN"
FT HELIX 394..405
FT /evidence="ECO:0007829|PDB:3NDN"
SQ SEQUENCE 406 AA; 43345 MW; E5C405B25297D04B CRC64;
MTDESSVRTP KALPDGVSQA TVGVRGGMLR SGFEETAEAM YLTSGYVYGS AAVAEKSFAG
ELDHYVYSRY GNPTVSVFEE RLRLIEGAPA AFATASGMAA VFTSLGALLG AGDRLVAARS
LFGSCFVVCS EILPRWGVQT VFVDGDDLSQ WERALSVPTQ AVFFETPSNP MQSLVDIAAV
TELAHAAGAK VVLDNVFATP LLQQGFPLGV DVVVYSGTKH IDGQGRVLGG AILGDREYID
GPVQKLMRHT GPAMSAFNAW VLLKGLETLA IRVQHSNASA QRIAEFLNGH PSVRWVRYPY
LPSHPQYDLA KRQMSGGGTV VTFALDCPED VAKQRAFEVL DKMRLIDISN NLGDAKSLVT
HPATTTHRAM GPEGRAAIGL GDGVVRISVG LEDTDDLIAD IDRALS
