ID A0A2A2EGD7_9BIFI Unreviewed; 423 AA.
AC A0A2A2EGD7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=B1400_1476 {ECO:0000313|EMBL:PAU68123.1};
OS Bifidobacterium italicum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1960968 {ECO:0000313|EMBL:PAU68123.1, ECO:0000313|Proteomes:UP000217986};
RN [1] {ECO:0000313|EMBL:PAU68123.1, ECO:0000313|Proteomes:UP000217986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70 {ECO:0000313|EMBL:PAU68123.1,
RC ECO:0000313|Proteomes:UP000217986};
RX PubMed=28837128; DOI=10.1038/ismej.2017.138;
RA Milani C., Mangifesta M., Mancabelli L., Lugli G.A., James K., Duranti S.,
RA Turroni F., Ferrario C., Ossiprandi M.C., van Sinderen D., Ventura M.;
RT "Unveiling bifidobacterial biogeography across the mammalian branch of the
RT tree of life.";
RL ISME J. 11:2834-2847(2017).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAU68123.1}.
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DR EMBL; MVOG01000031; PAU68123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2EGD7; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000217986; Unassembled WGS sequence.
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: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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004506};
KW Transferase {ECO:0000256|RuleBase:RU004506}.
FT DOMAIN 24..409
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 423 AA; 45101 MW; DA8357D2050F8172 CRC64;
MTDIETIRSQ FPILGQRING HPLVYLDSGA TAQKPQCVID AESGFYETIN AGVHRGAHTL
AARSTVAFEQ ARAKVARLVG ASSQEGGEEL VVTMGATDAL NLLATAIGNA SLGRGGPGAE
RFALKPGDEI VVSRAEHHSV LLPFQELAAR TGAALRWLEV DEDGRVMADL APETIGERTR
IVAVTHIGNV TGAITDIAPI VRRAHEVGAL FVLDACQSVP HIPVDFHALD VDFAAFSAHK
MYGPTGVGFL YGRRELLEAL PPARFGGSMV ELAYMDRPAL YMDPPARFEA GTQPVAQVVA
AGVAADWMMG VGMERIAAHE REITDELLGL GQVDGVRILG PRTSEGRIGT VAFEVDGVHP
HDVGQYLDAA GIAIRVGHHC AQPIHRHFGV FASNRASAGV YNTPDEARAL IEAVKGVRPF
FLR
//
