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Entry: A0A1Y2L823_9PROT
LinkDB: A0A1Y2L823_9PROT
Original site: A0A1Y2L823_9PROT 
ID   A0A1Y2L823_9PROT        Unreviewed;       407 AA.
AC   A0A1Y2L823;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=TALK_16405 {ECO:0000313|EMBL:OSQ46196.1};
OS   Thalassospira alkalitolerans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Thalassospiraceae; Thalassospira.
OX   NCBI_TaxID=1293890 {ECO:0000313|EMBL:OSQ46196.1, ECO:0000313|Proteomes:UP000193396};
RN   [1] {ECO:0000313|EMBL:OSQ46196.1, ECO:0000313|Proteomes:UP000193396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 18968 {ECO:0000313|EMBL:OSQ46196.1,
RC   ECO:0000313|Proteomes:UP000193396};
RA   Lai Q., Shao Z.;
RT   "The draft genome sequence of Thalassospira alkalitolerans JCM 18968.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the removal of elemental sulfur atoms from cysteine
CC       to produce alanine. Seems to participate in the biosynthesis of the
CC       nitrogenase metalloclusters by providing the inorganic sulfur required
CC       for the Fe-S core formation. {ECO:0000256|ARBA:ARBA00003120}.
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:OSQ46196.1}.
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DR   EMBL; JFKB01000012; OSQ46196.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2L823; -.
DR   STRING; 1293890.TALK_16405; -.
DR   OrthoDB; 9808002at2; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000193396; 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|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};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00331, ECO:0000313|EMBL:OSQ46196.1}.
FT   DOMAIN          9..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         77..78
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT   BINDING         157
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT   BINDING         185
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT   BINDING         205..207
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT   BINDING         245
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         208
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
SQ   SEQUENCE   407 AA;  45049 MW;  F239C46E7CE2DE9E CRC64;
     MNELKAKPIY LDYQATTPTD PRVVDAMLPY FTEKFGNPHS RNHSYGWEAE DAVEVARDQV
     AKIIGASSKE IIFTSGATES NNLALKGVMK FYGKKKPHLI TVVTEHKCVL DSARHLEQEG
     YKVTYLGVKE NGLIDLDQLK AAITDETAIV SVMGVNNEIG VIQPIKAIGE ICRERGVFFH
     TDCAQAVGKI PLDVDDMKID LMSISAHKLY GPKGVGALYV RRRPRVRVIA QITGGGQERG
     MRSGTLPTPL LVGFGKACEI AQNEMAEENA RLTELRDYTL KRFRDRLDDV FLNGDEEQRV
     SGNLNISFAY VEGESLQMGI KNIAVSSGSA CTSASLEPSY VLRALGVDEE LAHTSLRIGI
     GRFTTKEELD EAIDAISTEV ERLREMSPLW EMAQEGIDIK SIEWAEH
//
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