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Database: UniProt
Entry: L0M239_ENTBF
LinkDB: L0M239_ENTBF
Original site: L0M239_ENTBF 
ID   L0M239_ENTBF            Unreviewed;       406 AA.
AC   L0M239;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=Cysteine desulfurase {ECO:0000256|HAMAP-Rule:MF_01831};
DE            EC=2.8.1.7 {ECO:0000256|HAMAP-Rule:MF_01831};
DE   AltName: Full=Selenocysteine beta-lyase {ECO:0000256|HAMAP-Rule:MF_01831};
DE            Short=SCL {ECO:0000256|HAMAP-Rule:MF_01831};
DE   AltName: Full=Selenocysteine lyase {ECO:0000256|HAMAP-Rule:MF_01831};
DE            EC=4.4.1.16 {ECO:0000256|HAMAP-Rule:MF_01831};
DE   AltName: Full=Selenocysteine reductase {ECO:0000256|HAMAP-Rule:MF_01831};
GN   Name=sufS {ECO:0000256|HAMAP-Rule:MF_01831};
GN   OrderedLocusNames=D782_1967 {ECO:0000313|EMBL:AGB77954.1};
OS   Enterobacteriaceae bacterium (strain FGI 57).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae.
OX   NCBI_TaxID=693444 {ECO:0000313|EMBL:AGB77954.1, ECO:0000313|Proteomes:UP000011002};
RN   [1] {ECO:0000313|EMBL:AGB77954.1, ECO:0000313|Proteomes:UP000011002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGI 57 {ECO:0000313|EMBL:AGB77954.1,
RC   ECO:0000313|Proteomes:UP000011002};
RX   PubMed=23469353; DOI=10.1128/genomeA.00238-12;
RA   Aylward F.O., Tremmel D.M., Bruce D.C., Chain P., Chen A.,
RA   Walston Davenport K., Detter C., Han C.S., Han J., Huntemann M.,
RA   Ivanova N.N., Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M.,
RA   Pagani I., Pati A., Pitluck S., Deshpande S., Goodwin L., Woyke T.,
RA   Currie C.R.;
RT   "Complete genome of Enterobacteriaceae bacterium strain FGI 57, a strain
RT   associated with leaf-cutter ant fungus gardens.";
RL   Genome Announc. 1:E00238-12(2013).
CC   -!- FUNCTION: Cysteine desulfurases mobilize the sulfur from L-cysteine to
CC       yield L-alanine, an essential step in sulfur metabolism for
CC       biosynthesis of a variety of sulfur-containing biomolecules. Component
CC       of the suf operon, which is activated and required under specific
CC       conditions such as oxidative stress and iron limitation. Acts as a
CC       potent selenocysteine lyase in vitro, that mobilizes selenium from L-
CC       selenocysteine. Selenocysteine lyase activity is however unsure in
CC       vivo. {ECO:0000256|HAMAP-Rule:MF_01831}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-
CC         alanine; Xref=Rhea:RHEA:11632, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:29317, ChEBI:CHEBI:57843,
CC         ChEBI:CHEBI:57972; EC=4.4.1.16; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01831};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC         alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC         COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:64428; EC=2.8.1.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00001357, ECO:0000256|HAMAP-
CC         Rule:MF_01831};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_01831, ECO:0000256|RuleBase:RU004504};
CC   -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01831}.
CC   -!- SUBUNIT: Homodimer. Interacts with SufE and the SufBCD complex composed
CC       of SufB, SufC and SufD. The interaction with SufE is required to
CC       mediate the direct transfer of the sulfur atom from the S-
CC       sulfanylcysteine. {ECO:0000256|HAMAP-Rule:MF_01831}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01831}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily. {ECO:0000256|ARBA:ARBA00010447,
CC       ECO:0000256|HAMAP-Rule:MF_01831}.
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DR   EMBL; CP003938; AGB77954.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0M239; -.
DR   STRING; 693444.D782_1967; -.
DR   KEGG; ebf:D782_1967; -.
DR   PATRIC; fig|693444.3.peg.1892; -.
DR   eggNOG; COG0520; Bacteria.
DR   HOGENOM; CLU_003433_2_5_6; -.
DR   OMA; HKLCGPT; -.
DR   OrthoDB; 9808002at2; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000011002; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009000; F:selenocysteine lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR   CDD; cd06453; SufS_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_01831; SufS_aminotrans_5; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR010970; Cys_dSase_SufS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01979; sufS; 1.
DR   PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR   PANTHER; PTHR43586:SF25; CYSTEINE DESULFURASE; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01831};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01831};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01831}; Reference proteome {ECO:0000313|Proteomes:UP000011002};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01831}.
FT   DOMAIN          26..394
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   ACT_SITE        364
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01831"
FT   MOD_RES         226
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01831"
SQ   SEQUENCE   406 AA;  44021 MW;  45D4EADAE1F462A5 CRC64;
     MTFSVQQVRA DFPVLSREVN GQPLAYLDSA ASAQKPEQVI RAEAEFYRHG YAAVHRGIHT
     LSAEATQRME EVRQKAANFL NARSAEELVF VRGTTEGINL VANSWGSDNV RAGDNIVITA
     MEHHANIVPW QMLCARTGAE LRVIPLNVDG TLQMDIAPTL FDERTRLLAV TQVSNVLGTG
     NPVAALIALA HQYGAKALID GAQAVMHHPV DVQALDCDFY AFSGHKLYGP TGIGVLYVKE
     AILQAMPPWE GGGSMIATVS LTEGTTWAKA PWRFEAGTPN TGGIIGLGAA FDYLNALGLE
     AVGEYEQTLM HYALAALADV PDLHLYGPAN RLGVIAFNLG THHAYDVGSF LDNYGIAVRT
     GHHCAMPLMA FYQVPAMCRA SLAMYNTFEE VDRLVTGLRR IHHLLG
//
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