ID D3RTD1_ALLVD Unreviewed; 599 AA.
AC D3RTD1;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN OrderedLocusNames=Alvin_1507 {ECO:0000313|EMBL:ADC62440.1};
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477 {ECO:0000313|EMBL:ADC62440.1, ECO:0000313|Proteomes:UP000001441};
RN [1] {ECO:0000313|EMBL:ADC62440.1, ECO:0000313|Proteomes:UP000001441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D
RC {ECO:0000313|Proteomes:UP000001441};
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(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 -!- 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; CP001896; ADC62440.1; -; Genomic_DNA.
DR RefSeq; WP_012970714.1; NC_013851.1.
DR AlphaFoldDB; D3RTD1; -.
DR STRING; 572477.Alvin_1507; -.
DR KEGG; alv:Alvin_1507; -.
DR eggNOG; COG0520; Bacteria.
DR eggNOG; COG2166; Bacteria.
DR HOGENOM; CLU_003433_2_5_6; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000001441; 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; 3.90.1010.10; -; 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; IPR003808; Fe-S_metab-assoc_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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 Pfam; PF02657; SufE; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF82649; SufE/NifU; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001441}.
FT DOMAIN 36..407
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 470..592
FT /note="Fe-S metabolism associated"
FT /evidence="ECO:0000259|Pfam:PF02657"
FT REGION 418..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 599 AA; 64358 MW; 5B40BCD14FF60EBF CRC64;
MLNTAPAHAD HPALDVEAIR AQFPILTTPT DGQPLIYLDS AASTQQPECV IDAVADYHRG
HHANIHRGAY QLSRTATRMY EAARERVARF LNAADPVECL FTRGTTESIN LVAAIWGRAT
LQPGDEILIS TLEHHSNIVP WQMVAATTGA RLRVIPIDDA GDLDLDAYRR LLSPRTRLVA
VNQVSNALGT INPVAEIIAE AHAAGALVLI DGAQWVAHGP TDVQALDADF YVFSGHKLYG
PTGIGVLYGK RRLLESMPPY QGGGDMIERV TFEHTTYAGL PNRFEAGTPH ISGAVGLAAA
IDWVESIGLE AIGAHEQALL HQATGRLAQI PGLTIKGTAR HKSGVISWVM NDPPIATLDI
GTALDLRGIC IRTGHHCCQP LMDRLGVNST ARASFGVYNR LDEVEALAEA LSEIRASASR
QRHASGVSQV TPGAAGESLN PGSGEGPEPT LSYPAAMADS PRAAADEIAE VFELLPDWPM
RHQHIIDLGD RLPPMPDSLK TEANAVHGCQ SQVHIAARVR PGTTDVIEFL ADSDANIVRG
LIALLQQLYS GQPARDILAF DVEAFFKQIG LDQHLSLTRR NGLEAMVRRV RQLAGTIAG
//
