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Database: UniProt
Entry: D6ZTZ1_BIFLJ
LinkDB: D6ZTZ1_BIFLJ
Original site: D6ZTZ1_BIFLJ 
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
//
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