ID A0A1H1L8A6_9FLAO Unreviewed; 412 AA.
AC A0A1H1L8A6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN04515667_0387 {ECO:0000313|EMBL:SDR70736.1};
OS Formosa sp. Hel1_31_208.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1798225 {ECO:0000313|EMBL:SDR70736.1, ECO:0000313|Proteomes:UP000199458};
RN [1] {ECO:0000313|EMBL:SDR70736.1, ECO:0000313|Proteomes:UP000199458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_31_208 {ECO:0000313|EMBL:SDR70736.1,
RC ECO:0000313|Proteomes:UP000199458};
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; LT629733; SDR70736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1L8A6; -.
DR STRING; 1798225.SAMN04515667_0387; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000199458; Chromosome i.
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:SDR70736.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004506};
KW Reference proteome {ECO:0000313|Proteomes:UP000199458};
KW Transferase {ECO:0000256|RuleBase:RU004506}.
FT DOMAIN 32..400
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 412 AA; 45555 MW; 678D25CB31819F4B CRC64;
MNNTIEHIKF NVDKIREDFP ILNRKINGKP LIYFDNAATS QTPKQVIDVI VDYYSNYNAN
IHRGVHTLSQ EATDLYEGAR LKLQNHFNAK HSYEIILTSG TTHGLNLVAN GFSNLLDKND
EVLVSALEHH SNIVPWQMLC ERTGATLRVI PMNQEGELIM SDYEGLLSEN TKLVFVNHIS
NALGTINPIQ DIISKAHEVG AAVVVDGAQS CPHIKPDLQA LDVDFYVCGA HKMCGPTGVG
MLYGKKEWLE KLPPYQGGGE MIDQVTFEKT TYAGLPHKFE AGTPNICGGI AFGAAIDYMN
DIGFDRIAPY EQELLEYATN QLSQIEGLKI YGTAKNKTSV ISFNIEGVHP YDIGTILDKM
GIAVRTGHHC AQPIMDYYKI PGTVRASFAF YNTKAEIDAL VAGVKKAKMM LS
//
