ID D7DYA1_NOSA0 Unreviewed; 398 AA.
AC D7DYA1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:ADI65979.1};
DE EC=2.8.1.7 {ECO:0000313|EMBL:ADI65979.1};
GN OrderedLocusNames=Aazo_4811 {ECO:0000313|EMBL:ADI65979.1};
OS Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC Trichormus.
OX NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI65979.1, ECO:0000313|Proteomes:UP000001511};
RN [1] {ECO:0000313|EMBL:ADI65979.1, ECO:0000313|Proteomes:UP000001511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0708 {ECO:0000313|EMBL:ADI65979.1,
RC ECO:0000313|Proteomes:UP000001511};
RX PubMed=20628610; DOI=10.1371/journal.pone.0011486;
RA Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K.,
RA Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.;
RT "Genome erosion in a nitrogen-fixing vertically transmitted endosymbiotic
RT multicellular cyanobacterium.";
RL PLoS ONE 5:E11486-E11486(2010).
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; CP002059; ADI65979.1; -; Genomic_DNA.
DR RefSeq; WP_013192989.1; NC_014248.1.
DR AlphaFoldDB; D7DYA1; -.
DR STRING; 551115.Aazo_4811; -.
DR KEGG; naz:Aazo_4811; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_0_3; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000001511; Chromosome.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.260.50; -; 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; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001511};
KW Transferase {ECO:0000313|EMBL:ADI65979.1}.
FT DOMAIN 3..366
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 398 AA; 42309 MW; 55ECFDEF9C6CD31A CRC64;
MQIYLDYSAT TPTRPEAIAT MQAVLNQQWG NPSSLHEWGN RAALVVEQAR IQVAGLINAV
PESIIFTSGG TEADNLAVMG VARCYPVPQH IIISSVEHSA VSEPVRMLEN WGWEVTRLGV
DGKGRINPED LKAALQHNTV LVSVIYGQSE VGTVQPIAEL GRITKIHGAL FHTDAVQVAG
RLAIDVNNLG IDLLSLSSHK IYGPLGAGAL YVRPGMNLIP LLGGGGQEQG LRSGTQATPA
IAGFGVAAEL AGQELETERL RLTELRDRLF TKLADIPSLI PTGDRIHRLP HHLSFSLEYA
DGEKISGKTL VRQLNLAGIG ISAGAACNSG KLSPSPILLA MGYSQIAALG GIRLTLGKQT
TAADVDWTAI VLKQVLQRLT ADLSLVIQST SITCQLAI
//
