ID M1XP62_NATM8 Unreviewed; 413 AA.
AC M1XP62;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN Name=sufS1 {ECO:0000313|EMBL:CCQ35767.1};
GN OrderedLocusNames=Nmlp_1568 {ECO:0000313|EMBL:CCQ35767.1};
OS Natronomonas moolapensis (strain DSM 18674 / CECT 7526 / JCM 14361 /
OS 8.8.11).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=268739 {ECO:0000313|EMBL:CCQ35767.1, ECO:0000313|Proteomes:UP000011867};
RN [1] {ECO:0000313|EMBL:CCQ35767.1, ECO:0000313|Proteomes:UP000011867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18674 / JCM 14361 / 8.8.11
RC {ECO:0000313|Proteomes:UP000011867};
RX PubMed=23516216; DOI=10.1128/genomeA.00095-13;
RA Dyall-Smith M.L., Pfeiffer F., Oberwinkler T., Klee K., Rampp M., Palm P.,
RA Gross K., Schuster S.C., Oesterhelt D.;
RT "Genome of the haloarchaeon Natronomonas moolapensis, a neutrophilic member
RT of a previously haloalkaliphilic genus.";
RL Genome Announc. 1:e0009513-e0009513(2013).
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};
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DR EMBL; HF582854; CCQ35767.1; -; Genomic_DNA.
DR RefSeq; WP_015408610.1; NC_020388.1.
DR AlphaFoldDB; M1XP62; -.
DR STRING; 268739.Nmlp_1568; -.
DR GeneID; 14650778; -.
DR KEGG; nmo:Nmlp_1568; -.
DR eggNOG; arCOG00065; Archaea.
DR HOGENOM; CLU_003433_2_5_2; -.
DR OrthoDB; 5817at2157; -.
DR Proteomes; UP000011867; Chromosome.
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; 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-RELATED; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000011867};
KW Transferase {ECO:0000313|EMBL:CCQ35767.1}.
FT DOMAIN 30..401
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 413 AA; 45618 MW; 7684F0BB57D258A5 CRC64;
MSKQAETLNV ERIREDFPIL EREFDGTQLV YLDNAATTHT PEPVVETITD YYRTYNANVH
RGIHQLSQEA SIAYEEAHDR VAEFIGASGG REEIVFTKNT TESMNLVAYA WGLNELGPGD
EVVLTEMEHH ASLVTWQQIA KRTGAECKYI PITDEGRLDM EAADELITDD TKMVSVVHVS
NTLGTINPVS ELADVAHDHG AYIFVDGAQS VPNRPVDVEA IDADFLAFSG HKMAGPTGIG
VLYGKRHILE GMEPYLYGGE MILKVDFEDS TWNELPWKYE AGTPVICQGI ALASACDYLD
DIGMERIERH EAELAAYAYD RLREHDDVEV YGPPGDDRGG LVAFNLEGVH AHDLSSILND
SAVAVRAGDH CTQPLHDVLG ATASARASFY IYNTRAEVDR LVEAVDDARQ LFA
//
