ID D6ZTZ1_BIFLJ Unreviewed; 424 AA.
AC D6ZTZ1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 75.
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 OrderedLocusNames=BLJ_0881 {ECO:0000313|EMBL:ADH00347.1};
OS Bifidobacterium longum subsp. longum (strain JDM301).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=759350 {ECO:0000313|EMBL:ADH00347.1, ECO:0000313|Proteomes:UP000006740};
RN [1] {ECO:0000313|EMBL:ADH00347.1, ECO:0000313|Proteomes:UP000006740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDM301 {ECO:0000313|EMBL:ADH00347.1,
RC ECO:0000313|Proteomes:UP000006740};
RX PubMed=20525832; DOI=10.1128/JB.00538-10;
RA Wei Y.X., Zhang Z.Y., Liu C., Zhu Y.Z., Zhu Y.Q., Zheng H., Zhao G.P.,
RA Wang S., Guo X.K.;
RT "Complete genome sequence of Bifidobacterium longum JDM301.";
RL J. Bacteriol. 192:4076-4077(2010).
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; CP002010; ADH00347.1; -; Genomic_DNA.
DR RefSeq; WP_013140643.1; NC_014169.1.
DR AlphaFoldDB; D6ZTZ1; -.
DR KEGG; bll:BLJ_0881; -.
DR HOGENOM; CLU_003433_2_5_11; -.
DR OMA; HKLCGPT; -.
DR Proteomes; UP000006740; Chromosome.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
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:SF8; 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 Pyridoxal phosphate {ECO:0000256|RuleBase:RU004506};
KW Transferase {ECO:0000256|RuleBase:RU004506}.
FT DOMAIN 24..410
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 424 AA; 45577 MW; 307A3ED9DF54873C CRC64;
MVDFKEIRGE FPILNQEIHG HPLVYLDSAA TSQKPNAVID AEADFYRTIN AGVHRGAHEL
AARSTMAFEE ARAKVAKLVG ANTAEGEEEV VVTGGATAGL NLLATAFGNA SLGRGGEAAK
RFALKPGDEI VVARAEHHSV LLPFQELAYR TGATFKWIDL TEDGRVRTDN LDEVITERTK
VVAVTHVGNT TGAITNIAPI IKRAHEVGSI FILDACQSVP HLKVDFHALD VDFAAWSAHK
MYGPTGVGFL YGKRELLEAL PPANFGGSMV ELAYMDHEAQ YMAPPARFEA GTQPVAQVVA
AGVAAEWMMN IGLENIEAHE KTIAAELLKL GDIDGIRILG PRENVDRIGT VAFDVAGVHP
HDVGQFIDAQ GIAIRVGHHC AQPVHRHFGL YASNRASSGV YNSVEDAQAL VEAAKGIRKF
FGVE
//