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Database: UniProt
Entry: A0A063BEQ2_9BURK
LinkDB: A0A063BEQ2_9BURK
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ID   A0A063BEQ2_9BURK        Unreviewed;       670 AA.
AC   A0A063BEQ2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN   ORFNames=LIG30_2044 {ECO:0000313|EMBL:KDB08876.1};
OS   Burkholderia sp. lig30.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1192124 {ECO:0000313|EMBL:KDB08876.1, ECO:0000313|Proteomes:UP000027020};
RN   [1] {ECO:0000313|EMBL:KDB08876.1, ECO:0000313|Proteomes:UP000027020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LIG30 {ECO:0000313|Proteomes:UP000027020};
RA   Woo H.L., Utturkar S.M., Klingeman D.M., Simmons B.A., DeAngelis K.M.,
RA   Brown S.D., Hazen T.C.;
RT   "Draft Genome of the Lignin-degrading Burkholderia sp. Strain LIG30,
RT   Isolated from Wet Tropical Forest Soil.";
RL   Submitted (MAR-2014) 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:KDB08876.1}.
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DR   EMBL; JGVW01000066; KDB08876.1; -; Genomic_DNA.
DR   RefSeq; WP_038711447.1; NZ_JGVW01000066.1.
DR   AlphaFoldDB; A0A063BEQ2; -.
DR   STRING; 1192124.LIG30_2044; -.
DR   PATRIC; fig|1192124.4.peg.1872; -.
DR   eggNOG; COG0520; Bacteria.
DR   OrthoDB; 9808002at2; -.
DR   Proteomes; UP000027020; 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; NF041166; f2_encap_cargo1; 1.
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:UP000027020};
KW   Transferase {ECO:0000313|EMBL:KDB08876.1}.
FT   DOMAIN          290..659
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   670 AA;  70009 MW;  EBC967B803B4873A CRC64;
     MTTPTPTVNP DALPHAPLPA GLPDPATLAR LATEFFSALP GQAAAPGLSA GSGAVGGVPS
     ALPAAAPILA SVGNPAPAGS PLAGPGGTGT GVPGLALPQG KVPGANLAPS APTHVLSLGN
     RAPALAPHAA AQNGLPDNAV SVAPALEPRV GGALLGVPQA NGLASRDAAA PATPSPYYFT
     DATQHGWQAG AQDIVVPDHG PASAGAFGLP DEDALRELLA LRRDVPLSRA AGQDVPRYFI
     DDARAVEPHA LAGGAPQGDA YRGAHPPFDV NAIRRDFPIL QERVNGKQLV WFDNAATTHK
     PQAVIDRLAY FYAHENSNIH RAAHTLAGRA TDAYEHARDT VRRFIGAASS DEIVFVRGTT
     EAINLIAKTW GAQNVGEGDE IVVSHLEHHA NIVPWQQLAA QKGATLRVIP VDDSGQVLLD
     EYRKLLNDRT KIVSVTQVSN ALGTVVPVKE IVELAHRAGA KALVDGAQSI SHMRVDVQAL
     DADFFVFSGH KIYGPTGIGV VYGKRAILDD MPPWQGGGNM IADVTFERTL FQPPPNRFEA
     GTGNIADAVG LGAALDYVSR VGIDNIARYE HDLLAYATSV LAPVPGVRLV GTARDQASVL
     SFVLKGYETE EVGRALNEEG IAVRSGHHCA QPILRRFGLE ATVRPSLAFY NTCDEVDALV
     SVVRRLASRR
//
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