ID J2GCX7_9SPHN Unreviewed; 334 AA.
AC J2GCX7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
DE Flags: Fragment;
GN ORFNames=PMI02_02737 {ECO:0000313|EMBL:EJL27730.1};
OS Novosphingobium sp. AP12.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1144305 {ECO:0000313|EMBL:EJL27730.1, ECO:0000313|Proteomes:UP000007515};
RN [1] {ECO:0000313|EMBL:EJL27730.1, ECO:0000313|Proteomes:UP000007515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP12 {ECO:0000313|EMBL:EJL27730.1,
RC ECO:0000313|Proteomes:UP000007515};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJL27730.1}.
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DR EMBL; AKKE01000076; EJL27730.1; -; Genomic_DNA.
DR RefSeq; WP_007683384.1; NZ_AKKE01000076.1.
DR AlphaFoldDB; J2GCX7; -.
DR PATRIC; fig|1144305.3.peg.2634; -.
DR eggNOG; COG0520; Bacteria.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000007515; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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 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.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:EJL27730.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000007515}.
FT DOMAIN 2..322
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EJL27730.1"
SQ SEQUENCE 334 AA; 36108 MW; 846F5E773933D89D CRC64;
AARRRVAAFM NAHEDEIVYT RGATESINLA AQTWGAANLK AGDRILLSML EHHSNIVPWQ
LLREKTGVEI DICPLTDDGR IDLAAAERML TPAHKLVAFA HVSNVLGSVL DVAAAAKLAH
AVGAKLLIDG CQAAPRLALD MAAFECDFYA FSAHKLYGPT GIGVLWARKE ILDSMPPWQG
GGAMIDRVTF EKTTFAPAPQ RFEAGTPNII EALGMATAMD WLSDIGLGRA ERHERDLAAL
LRSELRKRND VTLFGPDDAL GIVSFALDGV HPHDLGTILD EEGVAIRAGH HCAQPLMEHL
GVPATARASF GLYSDEADIE ALLKGIERTR RIFG
//