ID G4FK93_9SYNE Unreviewed; 395 AA.
AC G4FK93;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:EHA63403.1};
DE EC=2.8.1.7 {ECO:0000313|EMBL:EHA63403.1};
GN ORFNames=Syn8016DRAFT_0444 {ECO:0000313|EMBL:EHA63403.1};
OS Synechococcus sp. WH 8016.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=166318 {ECO:0000313|EMBL:EHA63403.1, ECO:0000313|Proteomes:UP000002752};
RN [1] {ECO:0000313|EMBL:EHA63403.1, ECO:0000313|Proteomes:UP000002752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8016 {ECO:0000313|Proteomes:UP000002752};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Palenik B., Woyke T.J.;
RT "The draft genome of Synechococcus sp. WH 8016.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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:EHA63403.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGIK01000001; EHA63403.1; -; Genomic_DNA.
DR RefSeq; WP_006852585.1; NZ_AGIK01000001.1.
DR AlphaFoldDB; G4FK93; -.
DR STRING; 166318.Syn8016DRAFT_0444; -.
DR PATRIC; fig|166318.3.peg.494; -.
DR eggNOG; COG1104; Bacteria.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000002752; Unassembled WGS sequence.
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 Transferase {ECO:0000313|EMBL:EHA63403.1}.
FT DOMAIN 10..369
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 395 AA; 42127 MW; 84C9E4D362739FF3 CRC64;
MTGPEGPYFY LDGCATAPLR ESVIACMGKV QQESWGNPSS LHRIGCDAAE SLERARLSIG
ESLGADRSDI LFSSGATESA HLALLGLAKT ESPGRLVISA VEHPAVAAAA QQLAESGWTV
ERWPVDADGQ IEMKHLERLL EPPTKIVSLI WGQSEVGTLQ PIQAVGEACR SKHIPFHTDA
TQVLSQGCPN WNELPVDLLT ASAHKCGGPR GIGLLLLRPE IAERIQPLLA GGHQENGLRA
GTECPVLAQG MAAAFREIAP CQANQVKTSG SGIAPVRDAL LALLRQNDAI RVSGHPTDRL
PHHLSVLVSD RHGQPMSGRA LVRALDREGI AASSGSACSS GRESDSPVLE AMGVDPRWRR
SGLRLSLGYW IDPATLPEIN DRIQNAIARM NQQSV
//
