ID V4YTF0_9PROT Unreviewed; 407 AA.
AC V4YTF0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 ECO:0000313|EMBL:ESS14947.1};
GN ORFNames=MOLA814_00520 {ECO:0000313|EMBL:ESS14947.1};
OS Betaproteobacteria bacterium MOLA814.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1408164 {ECO:0000313|EMBL:ESS14947.1, ECO:0000313|Proteomes:UP000017838};
RN [1] {ECO:0000313|EMBL:ESS14947.1, ECO:0000313|Proteomes:UP000017838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOLA814 {ECO:0000313|EMBL:ESS14947.1,
RC ECO:0000313|Proteomes:UP000017838};
RX PubMed=24356832;
RA Courties A., Riedel T., Jarek M., Intertaglia L., Lebaron P., Suzuki M.T.;
RT "Genome Sequence of Strain MOLA814, a Proteorhodopsin-Containing
RT Representative of the Betaproteobacteria Common in the Ocean.";
RL Genome Announc. 1:e01062-13(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESS14947.1}.
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DR EMBL; AYMW01000001; ESS14947.1; -; Genomic_DNA.
DR AlphaFoldDB; V4YTF0; -.
DR STRING; 1408164.MOLA814_00520; -.
DR PATRIC; fig|1408164.3.peg.841; -.
DR eggNOG; COG0626; Bacteria.
DR OrthoDB; 9805807at2; -.
DR UniPathway; UPA00051; UER00449.
DR Proteomes; UP000017838; Unassembled WGS sequence.
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.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02056};
KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02056};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_02056}; Reference proteome {ECO:0000313|Proteomes:UP000017838};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02056, ECO:0000313|EMBL:ESS14947.1}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 214
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02056,
FT ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 407 AA; 43004 MW; 38662A0FA4C3E3F9 CRC64;
MSSPHLPDTS SWHAETHAQH TGMPPSQYGE NAEALFLTSG YVQPSAEVAA ARFAGEEEGY
TYSRLGNPTV SSFEQRLAAM EGTQAAIATS TGMSSILLMC MGLLKSGDHV ICSHSMFGST
IKLIGTEFAK FGVTTTFVSQ TDVSQWAAAV QPTTKLLFAE TPTNPLTDVC DIAALADIAH
KAGAWLAVDN CFATPILQRP VEFGADIVTH SGTKYLDGQG RVMAGALCAS EELVSEVFSP
VIRSAGMTLS PFNAWVVLKG LETLGIRMRA QSGNALALAQ WLQTQDAVDQ VFFPGLDSHP
QHELAMRQQG GLGGAVLSFS LKANNAQEGR AKAFATLNAM QLAKLCTNLG DTKTLVAHPA
STSHGRLSDA QRANAGVGQS LIRVAVGLEH IPDLQNDIQR AMAIGCA
//
