METZ_PSEAE
ID METZ_PSEAE Reviewed; 403 AA.
AC P55218;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=O-succinylhomoserine sulfhydrylase {ECO:0000255|HAMAP-Rule:MF_02056, ECO:0000303|PubMed:7704274};
DE Short=OSH sulfhydrylase {ECO:0000255|HAMAP-Rule:MF_02056, ECO:0000305};
DE Short=OSHS sulfhydrylase {ECO:0000255|HAMAP-Rule:MF_02056, ECO:0000305};
DE EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_02056, ECO:0000269|PubMed:7704274};
GN Name=metZ {ECO:0000255|HAMAP-Rule:MF_02056, ECO:0000303|PubMed:7704274};
GN OrderedLocusNames=PA3107;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, GENE NAME,
RP AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=7704274; DOI=10.1099/13500872-141-2-431;
RA Foglino M., Borne F., Bally M., Ball G., Patte J.-C.;
RT "A direct sulfhydrylation pathway is used for methionine biosynthesis in
RT Pseudomonas aeruginosa.";
RL Microbiology 141:431-439(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the formation of L-homocysteine from O-succinyl-L-
CC homoserine (OSHS) and hydrogen sulfide. Cannot use the other activated
CC form of L-homoserine, O-acetyl-L-homoserine, as a substrate.
CC {ECO:0000269|PubMed:7704274}.
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 ECO:0000269|PubMed:7704274};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P9WGB5,
CC ECO:0000255|HAMAP-Rule:MF_02056};
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, ECO:0000269|PubMed:7704274}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P9WGB5,
CC ECO:0000255|HAMAP-Rule:MF_02056}.
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; U10904; AAA83435.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06495.1; -; Genomic_DNA.
DR PIR; F83256; F83256.
DR PIR; S39822; S39822.
DR RefSeq; NP_251797.1; NC_002516.2.
DR RefSeq; WP_003113933.1; NZ_QZGE01000009.1.
DR AlphaFoldDB; P55218; -.
DR SMR; P55218; -.
DR STRING; 287.DR97_4826; -.
DR PaxDb; P55218; -.
DR PRIDE; P55218; -.
DR EnsemblBacteria; AAG06495; AAG06495; PA3107.
DR GeneID; 880476; -.
DR KEGG; pae:PA3107; -.
DR PATRIC; fig|208964.12.peg.3259; -.
DR PseudoCAP; PA3107; -.
DR HOGENOM; CLU_018986_2_0_6; -.
DR InParanoid; P55218; -.
DR OMA; FNAWVLS; -.
DR PhylomeDB; P55218; -.
DR BioCyc; MetaCyc:MON-13931; -.
DR BioCyc; PAER208964:G1FZ6-3163-MON; -.
DR UniPathway; UPA00051; UER00449.
DR Proteomes; UP000002438; 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:0009086; P:methionine biosynthetic process; IMP:PseudoCAP.
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.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Methionine biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..403
FT /note="O-succinylhomoserine sulfhydrylase"
FT /id="PRO_0000114785"
FT MOD_RES 219
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P9WGB5, ECO:0000255|HAMAP-
FT Rule:MF_02056"
SQ SEQUENCE 403 AA; 43185 MW; A7BE172B1DFCED80 CRC64;
MTQDWDAGRL DSDLEGAAFD TLAVRAGQRR TPEGEHGEAL FTTSSYVFRT AADAAARFAG
EVPGNVYSRY TNPTVRTFEE RIAALEGAEQ AVATASGMSA ILALVMSLCS SGDHVLVSRS
VFGSTISLFD KYFKRFGIQV DYPPLSDLAA WEAACKPNTK LFFVESPSNP LAELVDIAAL
AEIAHAKGAL LAVDNCFCTP ALQQPLKLGA DVVIHSATKY IDGQGRGMGG VVAGRGEQMK
EVVGFLRTAG PTLSPFNAWL FLKGLETLRI RMQAHSASAL ALAEWLERQP GIERVYYAGL
PSHPQHELAR RQQSGFGAVV SFDVKGGRDA AWRFIDATRM VSITTNLGDT KTTIAHPATT
SHGRLSPEDR ARAGIGDSLI RVAVGLEDLD DLKADMARGL AAL