ID K9XUR5_STAC7 Unreviewed; 387 AA.
AC K9XUR5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN OrderedLocusNames=Sta7437_2277 {ECO:0000313|EMBL:AFZ35821.1};
OS Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC Stanieria.
OX NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ35821.1, ECO:0000313|Proteomes:UP000010473};
RN [1] {ECO:0000313|Proteomes:UP000010473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490}.
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DR EMBL; CP003653; AFZ35821.1; -; Genomic_DNA.
DR RefSeq; WP_015193489.1; NC_019748.1.
DR AlphaFoldDB; K9XUR5; -.
DR STRING; 111780.Sta7437_2277; -.
DR KEGG; scs:Sta7437_2277; -.
DR PATRIC; fig|111780.3.peg.2376; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_2_3; -.
DR OMA; KGLYWAR; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000010473; Chromosome.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
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; 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; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000010473};
KW Transferase {ECO:0000313|EMBL:AFZ35821.1}.
FT DOMAIN 5..369
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 387 AA; 42423 MW; 61EABA42AE219B71 CRC64;
MSRPIYFDCH ATTPVDQRVL DAMLPYFTQC FGNPSSITHV YGWEAEAAVK LARTAIAEAI
NGTPEEIVFT SGATEANNLA IKGVAEAYFN QGKHIITVQT EHRAVLDPCK YLENLGFEVT
YLPVQPDGLI DLQQLQQAIR PDTILVSVMA ANNEIGVLQP LAEIGEICHA HQVLFHSDAA
QAIAKIPLDV QQMKIDLMSL TAHKVYGPKG IGALYLRRRH PRVKIAAQIQ GGGQERGIRS
GTLVTPQIVG FAKAVELGIA EMASESQRQF QLREQLWSIL KKIDKIYLNG HPLQRLPGNL
NVSFEEVDGS ALLLALQQTV ALSSGSACSA INTTPSHVLM ALGHSEQLAY ASLRFGIGRF
NTLEEIEQVG KLVISTCQSL RRSKQYF
//