ID A0A1H7UP44_9ACTN Unreviewed; 422 AA.
AC A0A1H7UP44;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
GN ORFNames=SAMN05660976_03901 {ECO:0000313|EMBL:SEL98792.1};
OS Nonomuraea pusilla.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=46177 {ECO:0000313|EMBL:SEL98792.1, ECO:0000313|Proteomes:UP000198953};
RN [1] {ECO:0000313|EMBL:SEL98792.1, ECO:0000313|Proteomes:UP000198953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43357 {ECO:0000313|EMBL:SEL98792.1,
RC ECO:0000313|Proteomes:UP000198953};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOBF01000008; SEL98792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7UP44; -.
DR STRING; 46177.SAMN05660976_03901; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000198953; 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; 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 SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:SEL98792.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004506};
KW Reference proteome {ECO:0000313|Proteomes:UP000198953};
KW Transferase {ECO:0000256|RuleBase:RU004506}.
FT DOMAIN 29..410
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 422 AA; 45571 MW; C316C228FCEC6A2F CRC64;
MTSAGFDVDR IRKDFPFLSR ELPGGRPLVY LDSGNSSQKP AQVIETMREH LALHYGNVGR
AMHVLGSEST EAYEGARDKV AAFVGAPSRD EVIFTKNASE ALNLVAHAFG PHLWRGAEGD
PRFALGPGDE IVISEMEHHS NIVPWQLLAQ RTGATLKWFG VTDEGRLDLS GDVITERTKI
VSIAHQSNVL GTVNPVAEVL RLARAAGALV MLDASQSVPH HPVNVAELGV DFVAFTGHKM
VGPSGIGVLW GRRELLEAMP PFLGGGEMIE AVWMDHSTYA PVPHKFEAGT PPIVEAIGLG
AAVDYLTEIG MDAIEAHERS LTAYALDALR EVPGLRLIGP DSLDLRGGTL SFTLEGIHPH
DVGQILDDSF GVAVRVGHHC ARPLHLRFGI PATTRASFYL YNTTGEIDAL VRGLHHVQKV
FA
//
