ID A0A0R2IJW3_9LACO Unreviewed; 387 AA.
AC A0A0R2IJW3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:KRN65315.1};
GN ORFNames=IV80_GL000369 {ECO:0000313|EMBL:KRN65315.1};
OS Pediococcus cellicola.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=319652 {ECO:0000313|EMBL:KRN65315.1, ECO:0000313|Proteomes:UP000051568};
RN [1] {ECO:0000313|EMBL:KRN65315.1, ECO:0000313|Proteomes:UP000051568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17757 {ECO:0000313|EMBL:KRN65315.1,
RC ECO:0000313|Proteomes:UP000051568};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KRN65315.1}.
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DR EMBL; JQBR01000010; KRN65315.1; -; Genomic_DNA.
DR RefSeq; WP_057752203.1; NZ_JQBR01000010.1.
DR AlphaFoldDB; A0A0R2IJW3; -.
DR STRING; 319652.IV80_GL000369; -.
DR PATRIC; fig|319652.3.peg.373; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000051568; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
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; 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: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.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000051568}.
FT DOMAIN 4..369
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 387 AA; 42312 MW; 00C6E2E342FE3894 CRC64;
MKQVYFDNAA TTPMAPEVVE KISAEMSQDF GNASSTHAFG RKARSVLDQS RQVIADSINA
NEDEIIFTSG GTESDNTAIV QTAIARKKLG KHIITTAIEH PAVLKPMAYL ESIGYDVTYL
PVDQNGLINM DDLKAALRDD TILVSVMTGN NEVGSHMPIH EIGELLKDHQ AWFHTDAVQA
YGLLDIDVKR DHIDLMSTSA HKLNGPKFLG FLYKRDGINF PSFLKGGEQE DKRRAGTENV
PGIAGFAKAV SLLTPASKAA LQEKYQAFKQ QIVDGLQQAN IDFEVNGSLD PNNLQHVFNL
WIKGVSTYVM QTNLDLNGIA VSGGSACTAG SLEPSHVLIA MYGEDSPRIG ESIRISFGKY
NTQDDVAYLV DNLVQIIQRL KTKEGVK
//
