ID A0A329MRI2_9BACL Unreviewed; 391 AA.
AC A0A329MRI2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Cysteine desulfurase NifS {ECO:0000313|EMBL:RAV22162.1};
GN ORFNames=DQG23_07700 {ECO:0000313|EMBL:RAV22162.1};
OS Paenibacillus contaminans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=450362 {ECO:0000313|EMBL:RAV22162.1, ECO:0000313|Proteomes:UP000250369};
RN [1] {ECO:0000313|EMBL:RAV22162.1, ECO:0000313|Proteomes:UP000250369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CKOBP-6 {ECO:0000313|EMBL:RAV22162.1,
RC ECO:0000313|Proteomes:UP000250369};
RX PubMed=19126735; DOI=10.1099/ijs.0.001495-0;
RA Chou J.H., Lee J.H., Lin M.C., Chang P.S., Arun A.B., Young C.C.,
RA Chen W.M.;
RT "Paenibacillus contaminans sp. nov., isolated from a contaminated
RT laboratory plate.";
RL Int. J. Syst. Evol. Microbiol. 59:125-129(2009).
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:RAV22162.1}.
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; QMFB01000003; RAV22162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329MRI2; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000250369; 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 Coiled coil {ECO:0000256|SAM:Coils}; 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:UP000250369}.
FT DOMAIN 4..373
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT COILED 256..283
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 391 AA; 41898 MW; C9AAD4ACB79CC284 CRC64;
MNDIYLDHAA TTPLHPAVFE RMLPHLSGVS GFGNPSSTHR FGMAARLAVS DARDRLAAAL
HCDSRQLIFT SGGTESDNLA IFGSIAAAAS KGKGQKGHII TSQIEHHAVL HTCEQLQRAG
HEVTYLPVDT TGLIRIEDLE RAIRPDTVLI SIMFGNNEVG TLQPIRAIGE LARSRGILFH
VDAVQALGHI DLQASQLPVD FMSFSAHKIQ GPKGTGALYC APHVHLSPQL FGGSQERKRR
AGTENVAGIV GFAAAAELAV QNIGQLQQNC AKLRQKMVET FQKFLGDGGF VENGHPDASH
RLPHIVNVSF PGVDTETLLM NLDLEGIAAA SGSACTSGSL EVSHVLQAMQ LPEEVLRSAV
RFSFGAGQPE DEIVLAAERA ATIVSRIRNR K
//
