ID A0A1X1C019_9GAMM Unreviewed; 384 AA.
AC A0A1X1C019;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=HA41_04325 {ECO:0000313|EMBL:ORM54681.1};
OS Pantoea conspicua.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=472705 {ECO:0000313|EMBL:ORM54681.1, ECO:0000313|Proteomes:UP000193933};
RN [1] {ECO:0000313|EMBL:ORM54681.1, ECO:0000313|Proteomes:UP000193933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24534 {ECO:0000313|EMBL:ORM54681.1,
RC ECO:0000313|Proteomes:UP000193933};
RX PubMed=28255640;
RA Palmer M., Steenkamp E.T., Coetzee M.P., Chan W.Y., van Zyl E.,
RA De Maayer P., Coutinho T.A., Blom J., Smits T.H., Duffy B., Venter S.N.;
RT "Phylogenomic resolution of the bacterial genus Pantoea and its
RT relationship with Erwinia and Tatumella.";
RL Antonie Van Leeuwenhoek 0:0-0(2017).
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}.
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:ORM54681.1}.
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DR EMBL; MLFN01000007; ORM54681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1C019; -.
DR STRING; 472705.GCA_001743465_03827; -.
DR OrthoDB; 9808002at2; -.
DR UniPathway; UPA00266; -.
DR Proteomes; UP000193933; Unassembled WGS sequence.
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}; Transferase {ECO:0000256|HAMAP-Rule:MF_00331}.
FT DOMAIN 5..368
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT ACT_SITE 328
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT BINDING 75..76
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT BINDING 155
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT BINDING 183
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT BINDING 203..205
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT BINDING 243
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT BINDING 328
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 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
SQ SEQUENCE 384 AA; 41823 MW; 4CFB0C3EE8A0F59D CRC64;
MKLPIYLDYA ATTPADPRVA SKMMQFLTLD GTFGNPASRS HRFGWQSEEA VDVARNQVAE
LVNADPREIV FTSGATESDN LAIKGAAHAH QARGKHIITS QTEHKAVLDS CQQLAQEGFD
VTYLKPAASG IISPEMLRDA LRDDTILVSI MHVNNEIGVI QDIAAFGELC RERDILFHVD
ATQSVGKLPI NLSLLPVDLM SFSAHKLYGP KGIGALYVRR KPRVQIAAQI HGGGHERGMR
SGTLPVHQIV GMGEAYQIAA QERETEMARL HSLRDRLWQG ISTLPGVTLN GDLQRSAANI
LNLSFADVEG ESLIMALKDL ALSSGSACTS ASLEPSYVLR ALGVSEELAH SSLRFSLGRF
TTEEEIDYAI ALVQKSVTRL RALM
//