ID A0A2M9R3E5_9FLAO Unreviewed; 405 AA.
AC A0A2M9R3E5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=CDL10_01310 {ECO:0000313|EMBL:PJR03285.1};
OS Avrilella dinanensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Avrilella.
OX NCBI_TaxID=2008672 {ECO:0000313|EMBL:PJR03285.1, ECO:0000313|Proteomes:UP000231960};
RN [1] {ECO:0000313|EMBL:PJR03285.1, ECO:0000313|Proteomes:UP000231960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UR159 {ECO:0000313|EMBL:PJR03285.1,
RC ECO:0000313|Proteomes:UP000231960};
RA Leyer C., Sassi M., Minet J., Kayal S., Cattoir V.;
RT "Description of Avrilella dinanensis gen. nov. sp. nov.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily.
CC {ECO:0000256|ARBA:ARBA00010447}.
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:PJR03285.1}.
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DR EMBL; NIPO01000001; PJR03285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9R3E5; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000231960; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
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; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000231960}.
FT DOMAIN 25..392
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 405 AA; 44824 MW; BAFCFAEC256D4A54 CRC64;
MSFDIQKIRQ DFPILAQRVN DKPLVYFDNG ATSQKPQVVI DAEARYYNEI NANIHRGVHH
LSQVATDAYE EARVKIQQHL NAKNSFEILF TAGTTFGINL VANGFGQILQ PGDEIIVSHL
EHHSNIVPWQ LACERSGATL KVIPMLADGS LDMEAYTALL NDKTKIVTVN HISNALGTIN
PVKFIIEKAH EVGAAVLIDG AQAVPHLKPD VQDLDCEFYA FSGHKMCGPT GTGVLYGKEQ
WLNQLPPYQG GGEMIKEVTF EKTTYACLPH KFEAGTPNIA GGIVLGTAVD YLNGIGFDNI
VAYEHQLLEY ATKRLSELED IEFYGTAKEK ASVISFNFKG IHPYDVGAII DKLGIAVRTG
HHCAQPIMDY FNIPGTIRAS FAFYNTKEEI DQMIEALKKA LMMLR
//
