ID B7XTH1_BORGR Unreviewed; 422 AA.
AC B7XTH1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=BGAPBR_0084 {ECO:0000313|EMBL:EED28806.1};
OS Borreliella garinii PBr.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=498743 {ECO:0000313|EMBL:EED28806.1, ECO:0000313|Proteomes:UP000006103};
RN [1] {ECO:0000313|EMBL:EED28806.1, ECO:0000313|Proteomes:UP000006103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBr {ECO:0000313|EMBL:EED28806.1,
RC ECO:0000313|Proteomes:UP000006103};
RX PubMed=22123755; DOI=10.1128/JB.05951-11;
RA Casjens S.R., Mongodin E.F., Qiu W.-G., Dunn J.J., Luft B.J.,
RA Fraser-Liggett C.M., Schutzer S.E.;
RT "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT Lyme disease agent isolates.";
RL J. Bacteriol. 193:6995-6996(2011).
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 ECO:0000256|RuleBase:RU004504};
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:EED28806.1}.
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DR EMBL; ABJV02000003; EED28806.1; -; Genomic_DNA.
DR RefSeq; WP_004792150.1; NZ_ABJV02000003.1.
DR AlphaFoldDB; B7XTH1; -.
DR STRING; 29519.BLA33_03865; -.
DR Proteomes; UP000006103; 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:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 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 PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF8; CYSTEINE DESULFURASE-RELATED; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EED28806.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000313|EMBL:EED28806.1}.
FT DOMAIN 33..410
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 422 AA; 48107 MW; 5680401A0051827B CRC64;
MDFKQIKSNA EKVKFLRKDF PILNKQFDNK HIIYFDNAAT SQKPKKVIYS SIEYYENYNA
NVHRSGHKFA IQSSIKIEKT RELVKNFINA ESSKNIIFTS GTTDGINTIA SSFFYSKYFK
KKDEIILTTL EHNSNLLPWA KLAKLANLTI KFAKFNEMGI ITPEEIERLI TEKTKLISIS
GINNTLGTMN DLESIGKIAK KYNISLFVDA AQMAPHIKID VKKIGCDFLV FSGHKMLAPT
GIGILYISNN MAEKLDSPKL GGNTVEEIFI ENEKIKFKSL NTPNKFESGT PNIAGIIGLK
EAIKYINNIS MDFILEHDQQ LIEYGVKKLQ ELDEVEFLLN TNLKRNSIIS FTVKNIHSHD
IETYLDTIGI ATRAGKTCSY VAFFPENLNK DHLLRISFYF YNTQEEIDTF ILGLKKVIKE
LS
//
