ID A0A1V4HHB2_9BACL Unreviewed; 386 AA.
AC A0A1V4HHB2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=BC351_06815 {ECO:0000313|EMBL:OPH53567.1};
OS Paenibacillus ferrarius.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1469647 {ECO:0000313|EMBL:OPH53567.1, ECO:0000313|Proteomes:UP000190626};
RN [1] {ECO:0000313|Proteomes:UP000190626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CY1 {ECO:0000313|Proteomes:UP000190626};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) 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:OPH53567.1}.
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DR EMBL; MBTG01000023; OPH53567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4HHB2; -.
DR STRING; 1469647.BC351_06815; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000190626; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:InterPro.
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; IPR010969; Cys_dSase-rel_unknwn_funct.
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; TIGR01977; am_tr_V_EF2568; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF4; ISOPENICILLIN N EPIMERASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 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:UP000190626}.
FT DOMAIN 5..373
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 386 AA; 41778 MW; E11028DE7DBCBFDE CRC64;
MENVMYFDQA ASSWPKPPAV MTAMMACMEE YAANPGRGSH QMAVKASRAL FETRKNLARL
FGVKNPNDIS FALNTTHALN QAIKGFVKPG DHVICTNIEH NSVRRPLEHL KATSQVELTY
IHNDEYGDIS LDELKRAFKS NTALVVVNHS SNLLGTIMPV GEIGELCRTH GAKLLVDAAQ
SAGILPIHVG SMNIDMLAFP GHKGLLGPQG TGGLYIHPDI DLDPLLHGGT GSQSEAIQQP
TVRPDRYEAG TQNTVGIAGL NEGVKFVLAE TVEKIHEKEW RQTQLLMEGL LGIQGVTVLG
PQLGQNKTGI VSFNIDDADS SEVAFILDQS FQIAVRSGYH CSPLAHEAAG TLARGAVRAS
IGYFTTDHEV DVLIQAVKEI HSQYAK
//
