ID A0A1Y1R4F0_9GAMM Unreviewed; 567 AA.
AC A0A1Y1R4F0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=B0D91_07765 {ECO:0000313|EMBL:OQX37036.1};
OS Oceanospirillales bacterium LUC14_002_19_P2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales.
OX NCBI_TaxID=1940822 {ECO:0000313|EMBL:OQX37036.1, ECO:0000313|Proteomes:UP000192421};
RN [1] {ECO:0000313|EMBL:OQX37036.1, ECO:0000313|Proteomes:UP000192421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LUC14_002_19_P2 {ECO:0000313|EMBL:OQX37036.1};
RA Lim S.J., Davis B.G., Gill D.E., Engel A.S., Anderson L.C., Campbell B.J.;
RT "Novel co-symbiosis in the unique lucinid bivalve Phacoides pectinatus.";
RL Submitted (FEB-2017) 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:OQX37036.1}.
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DR EMBL; MUIA01000205; OQX37036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1R4F0; -.
DR Proteomes; UP000192421; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 3.90.1010.10; -; 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; IPR010970; Cys_dSase_SufS.
DR InterPro; IPR003808; Fe-S_metab-assoc_dom.
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:SF27; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF02657; SufE; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF82649; SufE/NifU; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:OQX37036.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000192421}.
FT DOMAIN 24..393
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 439..560
FT /note="Fe-S metabolism associated"
FT /evidence="ECO:0000259|Pfam:PF02657"
SQ SEQUENCE 567 AA; 62702 MW; D842896D0C88439D CRC64;
MRELTELRAE FPILRQRANG YPLIYLDNAA TTQKPEGVIS AVNNYYREAN ANVHRASHFL
SARATHAFED ARDTVRRFLN AGHTDEIIWT RGATEAINLV AHSWGLSTLK AGDEILISAM
EHHANIVPWQ QVCRFTGASL KVIPIHASGE LDMAAFRQLL GPQTRLVSIC QVSNAIGTVN
PIPDIIREAH TVGARILIDG SQAVAHFLVD IQALDCDFYV FSGHKVYGPT GIGVLYGKRD
LLQDMPPWQT GGEMIERISF EGTTFNSPPF RFEAGTPNVV GALGLAAAIN FLGQCDHNKI
QAHEKSLLKQ ATEGLNTIPG LQIIGTAPQK TSVISFVMEG LHNQDIGTLL DQQGIAVRTG
HHCTMPLMSV LNLSGTVRAS IALYNTETEI QNFVEAVAAL QKDSLSFTTE TEPATTAATT
IPDAFTYESP QVGDTGSVIE ELQVLRGWQE RYRHIMLLGK KLPALPDPMK QEENRLHGCE
SIVWLHHYYD ETTMRLYFAI DSDARIVRGL ITLILSALNG RTPEEIENFD MEACFDQLGL
MHHLSPSRGN GIRAIVKEIQ LTAHRYR
//
