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Database: UniProt
Entry: N9VPJ4_9GAMM
LinkDB: N9VPJ4_9GAMM
Original site: N9VPJ4_9GAMM 
ID   N9VPJ4_9GAMM            Unreviewed;       404 AA.
AC   N9VPJ4;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   12-SEP-2018, entry version 49.
DE   RecName: Full=Cysteine desulfurase IscS {ECO:0000256|HAMAP-Rule:MF_00331, ECO:0000256|SAAS:SAAS00739704};
DE            EC=2.8.1.7 {ECO:0000256|HAMAP-Rule:MF_00331, ECO:0000256|SAAS:SAAS00645802};
GN   Name=iscS {ECO:0000256|HAMAP-Rule:MF_00331};
GN   ORFNames=G114_01969 {ECO:0000313|EMBL:ENY73493.1};
OS   Aeromonas diversa CDC 2478-85.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=1268237 {ECO:0000313|EMBL:ENY73493.1, ECO:0000313|Proteomes:UP000023775};
RN   [1] {ECO:0000313|EMBL:ENY73493.1, ECO:0000313|Proteomes:UP000023775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2478-85 {ECO:0000313|EMBL:ENY73493.1,
RC   ECO:0000313|Proteomes:UP000023775};
RX   PubMed=23792745; DOI=10.1128/genomeA.00330-13;
RA   Farfan M., Spataro N., Sanglas A., Albarral V., Loren J.G., Bosch E.,
RA   Fuste M.C.;
RT   "Draft Genome Sequence of the Aeromonas diversa Type Strain.";
RL   Genome Announc. 1:S69-S82(2013).
CC   -!- FUNCTION: Master enzyme that delivers sulfur to a number of
CC       partners involved in Fe-S cluster assembly, tRNA modification or
CC       cofactor biosynthesis. Catalyzes the removal of elemental sulfur
CC       atoms from cysteine to produce alanine. Functions as a sulfur
CC       delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S
CC       scaffold assembly protein, as well as other S acceptor proteins.
CC       {ECO:0000256|HAMAP-Rule:MF_00331}.
CC   -!- CATALYTIC ACTIVITY: L-cysteine + acceptor = L-alanine + S-
CC       sulfanyl-acceptor. {ECO:0000256|HAMAP-Rule:MF_00331,
CC       ECO:0000256|SAAS:SAAS00645799}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00331,
CC         ECO:0000256|RuleBase:RU004504, ECO:0000256|SAAS:SAAS00635993};
CC   -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00331, ECO:0000256|SAAS:SAAS00739618}.
CC   -!- SUBUNIT: Forms a heterotetramer with IscU, interacts with other
CC       sulfur acceptors. {ECO:0000256|SAAS:SAAS00739701}.
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. {ECO:0000256|HAMAP-
CC       Rule:MF_00331, ECO:0000256|SAAS:SAAS00645780}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ENY73493.1}.
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DR   EMBL; APVG01000003; ENY73493.1; -; Genomic_DNA.
DR   RefSeq; WP_005346689.1; NZ_CDCE01000029.1.
DR   EnsemblBacteria; ENY73493; ENY73493; G114_01969.
DR   PATRIC; fig|1268237.3.peg.384; -.
DR   OrthoDB; POG091H02DU; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000023775; 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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR11601:SF34; PTHR11601:SF34; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR02006; IscS; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|HAMAP-Rule:MF_00331,
KW   ECO:0000256|SAAS:SAAS00739693}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000023775};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00331};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00331, ECO:0000256|SAAS:SAAS00645781};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00331,
KW   ECO:0000256|SAAS:SAAS00645784};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00331,
KW   ECO:0000256|SAAS:SAAS00645783};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00331,
KW   ECO:0000256|SAAS:SAAS00635955};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00331,
KW   ECO:0000256|SAAS:SAAS00645795, ECO:0000313|EMBL:ENY73493.1}.
FT   DOMAIN        5    368       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   REGION       75     76       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00331}.
FT   REGION      203    205       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00331}.
FT   COILED      256    276       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    328    328       Cysteine persulfide intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00331}.
FT   METAL       328    328       Iron-sulfur (2Fe-2S); via persulfide
FT                                group; shared with IscU.
FT                                {ECO:0000256|HAMAP-Rule:MF_00331}.
FT   BINDING     155    155       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00331}.
FT   BINDING     183    183       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00331}.
FT   BINDING     243    243       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00331}.
FT   MOD_RES     206    206       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00331}.
SQ   SEQUENCE   404 AA;  44990 MW;  03325FFC568EE6EB CRC64;
     MKLPIYLDYS ATCPVDPRVA EKMMQCLTMD GLFGNPASRS HRFGWQAEEA VDLARNQVAE
     LIGADPREIV FTSGATESDN LAIKGVAHFY AGKGKHIITS KTEHKAVLDT CRQLEREGFD
     VTYLEPMPNG LFTLAMIENA MRDDTILVSM MHVNNEIGVI QDIQGIGELC RARKVLLHVD
     AAQSVGKVEI DVEAMKIDLL SLSAHKIYGP KGIGALYVRR KPRVRIEAQM HGGGHERGMR
     SGTLATHQIV GMGEAFRIAR EEMASEEARI RVLRDRLWNG IKDMEEVYVN GDMEHRVPGN
     LNVSFAYVEG ESLIMALKDL AVSSGSACTS ASLEPSYVLR ALGMNDELAH SSIRFTIGRF
     TTEEEIDYAV ELIRNSIGRL REMSPLWEMF KDGVDLNTVE WAHH
//
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