ID A0A0N9UBS7_SPHMC Unreviewed; 367 AA.
AC A0A0N9UBS7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558};
GN ORFNames=AN936_10295 {ECO:0000313|EMBL:ALH80745.1};
OS Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=33050 {ECO:0000313|EMBL:ALH80745.1, ECO:0000313|Proteomes:UP000058074};
RN [1] {ECO:0000313|EMBL:ALH80745.1, ECO:0000313|Proteomes:UP000058074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EY-1 {ECO:0000313|EMBL:ALH80745.1,
RC ECO:0000313|Proteomes:UP000058074};
RX PubMed=26634754;
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete Genome Sequence of Polypropylene Glycol- and Polyethylene Glycol-
RT Degrading Sphingopyxis macrogoltabida Strain EY-1.";
RL Genome Announc. 3:0-0(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:64428; EC=2.8.1.7;
CC Evidence={ECO:0000256|ARBA:ARBA00001357};
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}.
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DR EMBL; CP012700; ALH80745.1; -; Genomic_DNA.
DR RefSeq; WP_054588058.1; NZ_CP012700.1.
DR AlphaFoldDB; A0A0N9UBS7; -.
DR KEGG; smag:AN936_10295; -.
DR PATRIC; fig|33050.5.peg.2128; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000058074; Chromosome.
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 GO; GO:0008483; F:transaminase activity; 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 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Aminotransferase {ECO:0000313|EMBL:ALH80745.1};
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:UP000058074};
KW Transferase {ECO:0000313|EMBL:ALH80745.1}.
FT DOMAIN 2..350
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 367 AA; 38135 MW; 6478F69852FC3C70 CRC64;
MIYLDYQATT PLAPEAREAM LRWLEGAGAD DFGGDGFANP SSTHKAGRAA AAAVEVARDQ
VAALLPQGGR VIFTSGATEA LNWALFNGAK AKPGGVAGLS IEHAASLQCL ERLSAQNLPV
DSAGLALPPD AALIPENGIV ATMLVNNEVG TVQPVADFAA AAHAKNSLLL CDAVQGYGRV
AIPDGADLIA LSAHKIHGPK GIGALWVRDG IDLEPLMFGG AQEQGMRSGT VSPALCAGFG
AAAALAAERF DADAAHVERL WSLALDMLPE WTINGDAERR YHGNLNVRRE GVNGLRLMSD
AREVAFSLGS ACGSGSGKVS HVLRAMGVSE ADARASIRLG WGRYTSEQDL RDGLTAIREA
ARLQGVN
//
