ID A0A085L9A9_9FIRM Unreviewed; 382 AA.
AC A0A085L9A9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:KFD41555.1};
GN ORFNames=DK28_0207675 {ECO:0000313|EMBL:KFD41555.1};
OS Peptococcaceae bacterium SCADC1_2_3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1487582 {ECO:0000313|EMBL:KFD41555.1, ECO:0000313|Proteomes:UP000027084};
RN [1] {ECO:0000313|EMBL:KFD41555.1, ECO:0000313|Proteomes:UP000027084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCADC1_2_3 {ECO:0000313|EMBL:KFD41555.1};
RA Tan B.F., Charchuk R., Li C., Nesbo C., Abu-Laban N., Foght J.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KFD41555.1, ECO:0000313|Proteomes:UP000027084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCADC1_2_3 {ECO:0000313|EMBL:KFD41555.1};
RA Tan B., Charchuk R., Li C., Nesbo C., Abu-Laban N., Foght J.;
RT "Draft genome sequence of an unculturable Firmicutes affiliated with
RT Peptococcaceae sorted using a microfluidic device from methanogenic alkane-
RT degrading cultures.";
RL Submitted (JUL-2014) 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:KFD41555.1}.
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DR EMBL; JJNX02000029; KFD41555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085L9A9; -.
DR STRING; 1487582.HY00_03420; -.
DR Proteomes; UP000027084; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000027084}.
FT DOMAIN 4..367
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 382 AA; 41651 MW; EEF54B2AEF8B6D25 CRC64;
MSKIYFDHSA TTPVHPVAAI ELYRFLTDNF GNPTSIHYFG RQAREAVEEA REKVALAIGA
LDKEIIFTSG GTEADNMAIH GLAYANRHRG NHIITSAVEH HAVLNTVKAL TREGFTASIL
PVDRYGRINV NDVAAAITDK TILITIMHAN NEVGTIMPLM EIGRLAKERG IYFHTDAVQS
FGKIPVRVDD LGVDLLSISG HKIYGPKGIG ALYLCQGTRW EQTLFHGGAQ EQLRRAGTEN
TPGIVALGKV AEIAVNELEQ EANRLIKLRD KLIKGITQKI KGAYLTGHPT ERLPNHASFC
FEFMEGESLL LNLDQRGIAA SSGAACTAGS LEPSHVLTAM GIPFEIAHNS LRLSLGRDNT
ALEVEHFLEV FSSITGELQV NP
//
