ID B3PJC2_CELJU Unreviewed; 638 AA.
AC B3PJC2;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN OrderedLocusNames=CJA_2234 {ECO:0000313|EMBL:ACE82891.1};
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE82891.1, ECO:0000313|Proteomes:UP000001036};
RN [1] {ECO:0000313|EMBL:ACE82891.1, ECO:0000313|Proteomes:UP000001036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE82891.1,
RC ECO:0000313|Proteomes:UP000001036};
RX PubMed=18556790; DOI=10.1128/JB.01701-07;
RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
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}.
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DR EMBL; CP000934; ACE82891.1; -; Genomic_DNA.
DR RefSeq; WP_012487834.1; NC_010995.1.
DR AlphaFoldDB; B3PJC2; -.
DR STRING; 498211.CJA_2234; -.
DR KEGG; cja:CJA_2234; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_7_0_6; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000001036; Chromosome.
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:UP000001036}.
FT DOMAIN 256..625
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT REGION 49..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 638 AA; 69076 MW; AE64ADCD7491D06C CRC64;
MSEYQGPADL QDLPSLENLA ALANEMFQSL PNAVPFLSGI SALQAASATN PGARPQAGAS
AAQPAVTSPT LDKQLAAVPG YYFADNANQY PLAGISLDQL GQQVSPQAFG LPGDDELREL
LADHRFITHL ETPSEKAVTP VSGVPHTLES QSTNYHQAQL SGSDRTAVQS LSLPGEKDVQ
ALLSAEFGFA RLDAPTGTVS PVPDSHFYFL DSGVQPVFGN GPKQNLFAPQ QQGFDVQAIR
RDFPILAERV NGKPLVWFDN AATTHKPKAV IDRISYFYEH ENSNIHRAAH ELAARATDAY
EGARNKVAKF IGARSADDII FVRGATEAIN LLANTFGKQR VGEGDEIIVS QLEHHANIVP
WYLLAQRVGA KIRVIPVDDT GQILLDDYRK LINSRTRIIA VTQVSNALGT VTPIKDIIDI
GHSFGVPVIV DGAQSVSHMR VNVQALDADF FVFSGHKIFG PTGIGVVYGK AEHLKQLEPW
QGGGNMIADV TFDKVIFQDP PNRFEAGTGN IADAVGLGAA LDYVDRVGIE RIARYEHDLL
AYATQRIQHI PGVRIIGTAA NKASVLSFTL AGYKTEEVGT ELNREGIAVR SGHHCAQPIL
RRFGVETTVR PSFAFYNTCE EIDLLISVVD RLARVRKG
//
