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
//