ID I0WJX5_9FLAO Unreviewed; 411 AA.
AC I0WJX5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=W5A_01670 {ECO:0000313|EMBL:EID76691.1};
OS Imtechella halotolerans K1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Imtechella.
OX NCBI_TaxID=946077 {ECO:0000313|EMBL:EID76691.1, ECO:0000313|Proteomes:UP000005938};
RN [1] {ECO:0000313|EMBL:EID76691.1, ECO:0000313|Proteomes:UP000005938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1 {ECO:0000313|EMBL:EID76691.1,
RC ECO:0000313|Proteomes:UP000005938};
RX PubMed=22740661; DOI=10.1128/JB.00506-12;
RA Kumar S., Vikram S., Subramanian S., Raghava G.P., Pinnaka A.K.;
RT "Genome Sequence of the Halotolerant Bacterium Imtechella halotolerans
RT K1T.";
RL J. Bacteriol. 194:3731-3731(2012).
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:EID76691.1}.
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DR EMBL; AJJU01000002; EID76691.1; -; Genomic_DNA.
DR RefSeq; WP_008236726.1; NZ_AJJU01000002.1.
DR AlphaFoldDB; I0WJX5; -.
DR STRING; 946077.W5A_01670; -.
DR PATRIC; fig|946077.3.peg.343; -.
DR eggNOG; COG0520; Bacteria.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000005938; 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; IPR016454; Cysteine_dSase.
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 PIRSF; PIRSF005572; NifS; 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 Reference proteome {ECO:0000313|Proteomes:UP000005938};
KW Transferase {ECO:0000256|RuleBase:RU004506}.
FT DOMAIN 31..399
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 411 AA; 45290 MW; E9542C0D1AA8BEA2 CRC64;
MSTAHINTLD IKAIRNDFPI LARMVNGKPL VYFDNAATSQ KPQLVIDAIV HYYSYLNANI
HRGVHSLSQE ATDAYENARI KLQKHFNAAH SHEIIFTSGT THGINMVANG FSSLLNKGDE
LIVSAMEHHS NIVPWQMLCE RTGATLKVIP MNENGELVIS EYEKILSEKT KLVFVNHISN
ALGTINPIKD IIRKAHAFGA AVLIDGAQAA PHIKADVQAL DVDFYVVSAH KMCGPTGVGI
LYGKEAWLKK LPPYQGGGEM IAEVSFEKTT YADLPHKFEA GTPNICGGIV FGTAIDYINK
LGMENIASYE NQLLEYATKR LLEINGLKIY GTATNKTSVI SFNIDGIHPY DIGSILDKLG
IAVRTGHHCA QPIMDFYKIP GTVRASFSFY NTKEEIDYLV EGIIQAKNML L
//
