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
//