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Database: UniProt
Entry: A0A0J5GG92_9NEIS
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Original site: A0A0J5GG92_9NEIS 
ID   A0A0J5GG92_9NEIS        Unreviewed;       405 AA.
AC   A0A0J5GG92;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=ACG97_08200 {ECO:0000313|EMBL:KMJ53479.1};
OS   Vogesella sp. EB.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Vogesella.
OX   NCBI_TaxID=1526735 {ECO:0000313|EMBL:KMJ53479.1, ECO:0000313|Proteomes:UP000054352};
RN   [1] {ECO:0000313|EMBL:KMJ53479.1, ECO:0000313|Proteomes:UP000054352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EB {ECO:0000313|EMBL:KMJ53479.1,
RC   ECO:0000313|Proteomes:UP000054352};
RA   Arrua Day P., Revale S., Alvarez H.M.;
RT   "Genome wide analysis of metabolism in the polyhydroxybutyrate-producing
RT   Vogesella sp. strain EB.";
RL   Submitted (JUN-2015) 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}.
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:KMJ53479.1}.
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DR   EMBL; LFDT01000010; KMJ53479.1; -; Genomic_DNA.
DR   RefSeq; WP_047966863.1; NZ_LFDT01000010.1.
DR   AlphaFoldDB; A0A0J5GG92; -.
DR   STRING; 1526735.ACG97_08200; -.
DR   PATRIC; fig|1526735.3.peg.1760; -.
DR   OrthoDB; 9808002at2; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000054352; 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}; Reference proteome {ECO:0000313|Proteomes:UP000054352};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00331, ECO:0000313|EMBL:KMJ53479.1}.
FT   DOMAIN          8..369
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   ACT_SITE        329
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT   BINDING         76..77
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT   BINDING         156
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT   BINDING         184
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT   BINDING         204..206
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT   BINDING         244
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
FT   BINDING         329
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         207
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00331"
SQ   SEQUENCE   405 AA;  44875 MW;  5B847ACF46DA7FB6 CRC64;
     MSELKHPIYL DYSATTPVDP RVAEVMIPFL TENFGNPASR SHAYGWTAEE AVENARAQVA
     ALVNCDPKEI VWTSGATESI NLALKGAAQF YKSKGKHLIT LKTEHKATLD TMRELERQGF
     EVTYLDVQDN GLLDLAALEA ALRPDTILVS VLFVNNEIGV IQDIPAIGEM LRSRGILLHV
     DSAQATGKID IDLDKLKVDL MSFSAHKTYG PKGIGALYIR RKPRVRLEAQ MHGGGHERGF
     RSGTLATHQI AGMGEAYRIA RESMHAENER IRMLRDRLWA GLQGIEETYL NGDIDARVPH
     NLNVSFNFVE GESLIMAIKD LAVSSGSACT SASLEPSYVL RALGRNDELA HSSIRFSIGR
     FTTEADVDYA IKLLQEKIGK LREMSPLWEM FKDGVDLNSI EWAAH
//
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