ID D7A3W5_STAND Unreviewed; 401 AA.
AC D7A3W5;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=O-succinylhomoserine sulfhydrylase {ECO:0000256|HAMAP-Rule:MF_02056};
DE Short=OSH sulfhydrylase {ECO:0000256|HAMAP-Rule:MF_02056};
DE Short=OSHS sulfhydrylase {ECO:0000256|HAMAP-Rule:MF_02056};
DE EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_02056};
GN Name=metZ {ECO:0000256|HAMAP-Rule:MF_02056};
GN OrderedLocusNames=Snov_4486 {ECO:0000313|EMBL:ADH91742.1};
OS Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM
OS 12100 / NBRC 12443 / NCIMB 10456).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Ancylobacter.
OX NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH91742.1, ECO:0000313|Proteomes:UP000006633};
RN [1] {ECO:0000313|EMBL:ADH91742.1, ECO:0000313|Proteomes:UP000006633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC
RC 12443 / NCIMB 10456 {ECO:0000313|Proteomes:UP000006633};
RX PubMed=23450099; DOI=10.4056/sigs.3006378;
RA Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A., Copeland A.,
RA Berry K.W., Glavina Del Rio T., Hammon N., Dalin E., Tice H., Pitluck S.,
RA Richardson P., Bruce D., Goodwin L.A., Han C., Tapia R., Detter J.C.,
RA Chang Y.J., Jeffries C.D., Land M., Hauser L., Kyrpides N.C., Goker M.,
RA Ivanova N., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the facultatively chemolithoautotrophic and
RT methylotrophic alpha Proteobacterium Starkeya novella type strain (ATCC
RT 8093(T)).";
RL Stand. Genomic Sci. 7:44-58(2012).
CC -!- FUNCTION: Catalyzes the formation of L-homocysteine from O-succinyl-L-
CC homoserine (OSHS) and hydrogen sulfide. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02056};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_02056, ECO:0000256|RuleBase:RU362118};
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:0000256|HAMAP-Rule:MF_02056}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_02056}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. MetZ
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02056}.
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DR EMBL; CP002026; ADH91742.1; -; Genomic_DNA.
DR RefSeq; WP_013169240.1; NC_014217.1.
DR AlphaFoldDB; D7A3W5; -.
DR STRING; 639283.Snov_4486; -.
DR KEGG; sno:Snov_4486; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_5; -.
DR OrthoDB; 7316598at2; -.
DR UniPathway; UPA00051; UER00449.
DR Proteomes; UP000006633; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
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:0071268; P:homocysteine biosynthetic process; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 NCBIfam; TIGR01325; O_suc_HS_sulf; 1.
DR PANTHER; PTHR11808:SF90; CYSTATHIONINE GAMMA-LYASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02056};
KW Lyase {ECO:0000313|EMBL:ADH91742.1};
KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02056};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_02056}; Transferase {ECO:0000256|HAMAP-Rule:MF_02056}.
FT MOD_RES 217
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02056,
FT ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 401 AA; 43098 MW; 93BD30F71C0E6FAB CRC64;
MTAEPKLTPA EIAQLRPDTR LVHGGILRSP FGETSEALFL TQGYVYETAE QAEARFKGED
AGFIYTRYSN PTAAMFEGRL ALLEGAEVCR STASGMAAVT AALLCQLKAG DHVVAARALF
GSCRYVVEEL LPRFGVTSTL VDGTDIAAWK AAVRPETKVF FLESPTNPTL ELIDIAAVAQ
VSKVAGACLI VDNVFATPML QSPLQLGADV VVYSATKHID GQGRCLAGAV LCSEKFLTDH
LQTFLRQTGP SVSPFNAWVM LKGLETLPLR VERSQASAAT LADRIADLPG ITKVIYPYRA
DHPQHELAKR QMRGGGTLVT FEVEGGKAGA FRFLNGLKVA RISNNLGDAK SLITHPATTT
HQRFTPEARA QMGISDGMVR LSVGLEHVDD LTDDVARALR G
//
