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Database: UniProt
Entry: A0A3M0GF22_9FLAO
LinkDB: A0A3M0GF22_9FLAO
Original site: A0A3M0GF22_9FLAO 
ID   A0A3M0GF22_9FLAO        Unreviewed;       404 AA.
AC   A0A3M0GF22;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN   ORFNames=EAX61_03775 {ECO:0000313|EMBL:RMB63515.1};
OS   Dokdonia sinensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Dokdonia.
OX   NCBI_TaxID=2479847 {ECO:0000313|EMBL:RMB63515.1, ECO:0000313|Proteomes:UP000281985};
RN   [1] {ECO:0000313|EMBL:RMB63515.1, ECO:0000313|Proteomes:UP000281985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH27 {ECO:0000313|EMBL:RMB63515.1,
RC   ECO:0000313|Proteomes:UP000281985};
RA   Zhou L.Y., Du Z.J.;
RT   "Dokdonia luteus sp. nov., isolated from sea water.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RMB63515.1}.
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DR   EMBL; REFV01000002; RMB63515.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0GF22; -.
DR   OrthoDB; 9804366at2; -.
DR   Proteomes; UP000281985; Unassembled WGS sequence.
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; IPR016454; Cysteine_dSase.
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:SF8; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000281985}.
FT   DOMAIN          24..392
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   404 AA;  44111 MW;  5006C9F24084C585 CRC64;
     MLDIKKIRKD FPILKREVNG QPLIYFDNAA TSQTPQVVID AIVDYYSNYN ANIHRGVHAL
     SQEATDKYEQ ARIKIQKHFN AAQPYEIIFT SGTTHAINLV ASGFASILKK GEEVLVSALE
     HHSNIVPWQM LCEKTGAVLK VIPQTESGEL DMDAFAKAVT PNLKLVFVNH VSNALGTVNP
     IEHIIAEAHK VGAAALIDGA QATPHIKPDV QALNADFYVT SAHKICGPTG VGILYGKEEW
     LTKLPPYQGG GEMIDQVSFE KTTYAGLPHK FEAGTPNICG GIATGVALDY MNGLGFDNIA
     SYEEELLQYA TKQLLEIEGL KIYGTSAKKT AVISFNVGAI HPYDIGTILD KMGIAVRTGH
     HCAQPIMDYY KIPGTVRASF SFYNTKEEID TFVNGLKRAV GMLS
//
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