ID A0A2C1ZBI9_9BACI Unreviewed; 380 AA.
AC A0A2C1ZBI9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Cysteine desulfurase NifS {ECO:0000313|EMBL:PGV54472.1};
GN ORFNames=COD92_04530 {ECO:0000313|EMBL:PGV54472.1};
OS Bacillus sp. AFS037270.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033499 {ECO:0000313|EMBL:PGV54472.1, ECO:0000313|Proteomes:UP000225442};
RN [1] {ECO:0000313|EMBL:PGV54472.1, ECO:0000313|Proteomes:UP000225442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS037270 {ECO:0000313|EMBL:PGV54472.1,
RC ECO:0000313|Proteomes:UP000225442};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004504};
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:PGV54472.1}.
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DR EMBL; NUNF01000010; PGV54472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C1ZBI9; -.
DR Proteomes; UP000225442; 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; 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: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 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}.
FT DOMAIN 4..365
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 380 AA; 41559 MW; 16649D277568BD9E CRC64;
MERIYLDHAA TSPMHPKVID KMVTIMNATF GNPSSIHSFG REARHYIDLA RAVLARSIGA
QETEIIFTGG GTEADNMALF GVAESYQTMG RHIITTQVEH HAVLHACKKL EKMGYEVTYL
PVDETGRIAI TDLQAALRDD TILVSVMYGN NEVGTIQPIN EIGQLLQGHQ AIFHTDAVQA
YGVEDIDVND SKIDLLSVSA HKINGPKGVG FLFARSTVKI APRLFGGEQE RKRRAGTENV
ASIVGFHEAV LIANEERSIK REKFIELKET LIEKLHDGQV EFNINGSLEY SLPHVLNLSF
PGTSVEAMLV NLDLAGVAVS SGSACTAGSI EPSHVLVAMF GKQSERLTNS IRFSFGFTTT
KEEVSKTAGE IAKIVKRLKK
//
