ID A0A1N7LI87_9PROT Unreviewed; 421 AA.
AC A0A1N7LI87;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558, ECO:0000256|RuleBase:RU004506};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
GN ORFNames=SAMN05421779_103343 {ECO:0000313|EMBL:SIS73513.1};
OS Insolitispirillum peregrinum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Insolitispirillum.
OX NCBI_TaxID=80876 {ECO:0000313|EMBL:SIS73513.1, ECO:0000313|Proteomes:UP000185678};
RN [1] {ECO:0000313|EMBL:SIS73513.1, ECO:0000313|Proteomes:UP000185678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11589 {ECO:0000313|EMBL:SIS73513.1,
RC ECO:0000313|Proteomes:UP000185678};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium atoms
CC from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to
CC produce L-alanine. {ECO:0000256|RuleBase:RU004506}.
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 ECO:0000256|RuleBase:RU004506};
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. Csd subfamily. {ECO:0000256|ARBA:ARBA00010447,
CC ECO:0000256|RuleBase:RU004506}.
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; FTOA01000003; SIS73513.1; -; Genomic_DNA.
DR RefSeq; WP_076399982.1; NZ_FTOA01000003.1.
DR AlphaFoldDB; A0A1N7LI87; -.
DR STRING; 80876.SAMN05421779_103343; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000185678; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006534; P:cysteine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd06453; SufS_like; 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; IPR010970; Cys_dSase_SufS.
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 NCBIfam; TIGR01979; sufS; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF27; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 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 Lyase {ECO:0000313|EMBL:SIS73513.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004506};
KW Reference proteome {ECO:0000313|Proteomes:UP000185678};
KW Transferase {ECO:0000256|RuleBase:RU004506}.
FT DOMAIN 41..409
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 421 AA; 45207 MW; 442A09A46053F3FD CRC64;
MGIAVSDSLR SDLATTVFDV EAVRRDFPIL TSQVHGKRLA YLDSGASAQK PLAVLDAMRN
AYEHEYANVH RGAYWLSETA TQNYEAARSK VRAFINAADD CEVIFTRGAT EAINLVAQTY
ARSLLKPGDE IIISALEHHS NIVPWQMVRD DKGLVLKVVP ITDDGRFDME AFEALLTDRT
RLVAIAHVSN VLGTVLPVAE IAAKAHAAGA IVLVDGCQGI VHRPVDVQAL GCDFYAFSGH
KLYGPTGIGI LWGREALLDR MPPWMGGGDM ISSVTFEASE WAALPAKFEA GTPAIVQAIG
LGAAVDYVRS INHAAALEHE EALLAYAIDG MQAIDGLTLH GTAPGKSGII AFSMSYAHPH
DIATVLDRAG VAIRAGHHCC QPLMDRCGVP AMARASFGVY TNKDDIDQLL KALHTVQTLF
A
//
