GenomeNet

Database: UniProt
Entry: R6GYN2_9FIRM
LinkDB: R6GYN2_9FIRM
Original site: R6GYN2_9FIRM 
ID   R6GYN2_9FIRM            Unreviewed;       375 AA.
AC   R6GYN2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN   ORFNames=BN704_01003 {ECO:0000313|EMBL:CDB26839.1};
OS   Firmicutes bacterium CAG:552.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263029 {ECO:0000313|EMBL:CDB26839.1, ECO:0000313|Proteomes:UP000018403};
RN   [1] {ECO:0000313|EMBL:CDB26839.1, ECO:0000313|Proteomes:UP000018403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:552 {ECO:0000313|Proteomes:UP000018403};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004504};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. NifS/IscS subfamily.
CC       {ECO:0000256|ARBA:ARBA00006490}.
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:CDB26839.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CBDH010000088; CDB26839.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6GYN2; -.
DR   STRING; 1263029.BN704_01003; -.
DR   Proteomes; UP000018403; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
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   PANTHER; PTHR11601:SF63; CYSTEINE DESULFURASE; 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   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018403}.
FT   DOMAIN          5..355
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   375 AA;  40378 MW;  C502CAB54283BBBB CRC64;
     MEKIIFLDNA STTPLCEDAK KGIEFAVNKY YNPSALYGEA LSVKNEIENA RAVIAKRLGA
     SANEIFFTSC ATESNNWVFE SGFKNKKGNI VVSSMEHASV YQCAMRQKSR GADVRFVPLQ
     SDGRIDIDKL YDLLDENTSL VSIIHCSNET GVINDLKAIS SAIKSKCRNA LFHSDGVQAL
     CKTNNKVGEL GVDMYSLSAH KIGGMKGIGA LYIKKGVSLQ PYIAGGGQEY GMRSGTENVA
     GILSFAAAVK NYENKFNAQR AQTLRNIFIS VLSNCDVKIN GTATGSNCIL SLSIKGIKAE
     VLQHMLSDKG VLIGLGSACS SKSRNNRVLS AMGVSPKLIE GSIRISTGID TTEQDATNAA
     EIIKQEIYTL RGNLS
//
DBGET integrated database retrieval system