ID A0A010ZJ59_9BACT Unreviewed; 392 AA.
AC A0A010ZJ59;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=Cloev_0832 {ECO:0000313|EMBL:EXG78704.1};
OS Cloacibacillus evryensis DSM 19522.
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Cloacibacillus.
OX NCBI_TaxID=866499 {ECO:0000313|EMBL:EXG78704.1, ECO:0000313|Proteomes:UP000023044};
RN [1] {ECO:0000313|EMBL:EXG78704.1, ECO:0000313|Proteomes:UP000023044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19522 {ECO:0000313|EMBL:EXG78704.1,
RC ECO:0000313|Proteomes:UP000023044};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JUL-2013) 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; Evidence={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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:EXG78704.1}.
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DR EMBL; JFBR01000001; EXG78704.1; -; Genomic_DNA.
DR RefSeq; WP_008710780.1; NZ_KK073872.1.
DR AlphaFoldDB; A0A010ZJ59; -.
DR PATRIC; fig|866499.3.peg.885; -.
DR HOGENOM; CLU_003433_0_0_0; -.
DR OrthoDB; 9808002at2; -.
DR UniPathway; UPA00266; -.
DR Proteomes; UP000023044; 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 GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 1.10.260.50; -; 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_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; IPR017772; Cys_deSase_NifS_bac/arc.
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; TIGR03402; FeS_nifS; 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|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:UP000023044};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00331}.
FT DOMAIN 6..372
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 73..74
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 241
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 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
SQ SEQUENCE 392 AA; 42397 MW; B3EFAD76F3BA63C5 CRC64;
MAPREVYLDN SATTKVDPRV TEAMLPYFSE KYGNPNSLHK FGREARAAVD NARAQVAALI
NAKPSDIIFT GAGSEADNLA IKGAAWALKE KGRGNHIITS AVEHHAILDT VKWLGKMGFE
YTILPVDDKG MVSPADLEAA IRPETILATI MFANNEIGTI QPVKELGEVC RRRGVMFHVD
GVQAAGHIMI DIQQLPVDMM TMAAHKMYGP KGLGALYVRK GIKLIPTLHG GGQEFGLRSG
TENVPGIVGF GVAAEIAKER LARGDDKKLA RLRDYFIDGV LSRIPESHLT GAVGDDRLPF
HTSFTIKYIE GEGMLLLLDA AGIAASSGSA CTSGSLEPSY VLLALGLDHT TAHGSVRLTM
SHDTTKEDID YVLEKFPAIV EKLRAMSPFY KK
//
