ID A4JG04_BURVG Unreviewed; 407 AA.
AC A4JG04;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Cysteine desulfurase IscS {ECO:0000256|HAMAP-Rule:MF_00331};
DE EC=2.8.1.7 {ECO:0000256|HAMAP-Rule:MF_00331};
GN Name=iscS {ECO:0000256|HAMAP-Rule:MF_00331};
GN OrderedLocusNames=Bcep1808_2205 {ECO:0000313|EMBL:ABO55207.1};
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482 {ECO:0000313|EMBL:ABO55207.1, ECO:0000313|Proteomes:UP000002287};
RN [1] {ECO:0000313|Proteomes:UP000002287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486 {ECO:0000313|Proteomes:UP000002287};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Master enzyme that delivers sulfur to a number of partners
CC involved in Fe-S cluster assembly, tRNA modification or cofactor
CC biosynthesis. Catalyzes the removal of elemental sulfur atoms from
CC cysteine to produce alanine. Functions as a sulfur delivery protein for
CC Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as
CC well as other S acceptor proteins. {ECO:0000256|HAMAP-Rule:MF_00331}.
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_00331};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00331, ECO:0000256|RuleBase:RU004504};
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00331}.
CC -!- SUBUNIT: Homodimer. Forms a heterotetramer with IscU, interacts with
CC other sulfur acceptors. {ECO:0000256|HAMAP-Rule:MF_00331}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00331}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490, ECO:0000256|HAMAP-Rule:MF_00331}.
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DR EMBL; CP000614; ABO55207.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JG04; -.
DR KEGG; bvi:Bcep1808_2205; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_2_4; -.
DR UniPathway; UPA00266; -.
DR Proteomes; UP000002287; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:UniProtKB-UniRule.
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_00331; Cys_desulf_IscS; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR010240; Cys_deSase_IscS.
DR InterPro; IPR016454; Cysteine_dSase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR02006; IscS; 1.
DR PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|HAMAP-Rule:MF_00331};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00331};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00331};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00331};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00331};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00331}; Reference proteome {ECO:0000313|Proteomes:UP000002287};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00331}.
FT DOMAIN 10..370
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT ACT_SITE 331
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT BINDING 78..79
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT BINDING 158
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT BINDING 186
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT BINDING 206..208
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT BINDING 246
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT BINDING 331
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared with IscU"
FT /note="via persulfide group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
SQ SEQUENCE 407 AA; 45502 MW; BAD809FD96B89BC8 CRC64;
MTQQTLHLPI YMDYSATTPV DPRVVDKMVP YLRERFGNPA SRSHAYGWDA EHAVEEAREQ
VAALVNADPR EIIWTSGATE SDNLAIKGAA HFYKGKGKHI ITVKTEHKAV LDTCRELERE
GFEVTYLDVK EDGLLDLDVF KAALRPDTIL VSVMHVNNEI GVIQDIATIG EICREKGIVF
HVDAAQSTGK VEIDLAKLKV DLMSFSAHKT YGPKGIGALY VRRKPRVRIE AQMHGGGHER
GMRSGTLATH QIVGMGEAFR IAREEMATEN ERIRMLRDKL LRGLSQIEET YVNGDMEHRV
PHNLNISFNF VEGESLIMAI KDVAVSSGSA CTSASLEPSY VLRALGRNDE LAHSSIRFTV
GRFTTEEEVD FVIDLLNSKI AKLRELSPLW EMHQEGIDLS TIEWAAH
//
