ID B8EJ13_METSB Unreviewed; 400 AA.
AC B8EJ13;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558, ECO:0000256|RuleBase:RU364075};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU364075};
DE AltName: Full=Nitrogenase metalloclusters biosynthesis protein NifS {ECO:0000256|ARBA:ARBA00031911, ECO:0000256|RuleBase:RU364075};
GN OrderedLocusNames=Msil_3620 {ECO:0000313|EMBL:ACK52505.1};
OS Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB
OS 13906 / BL2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Methylocella.
OX NCBI_TaxID=395965 {ECO:0000313|EMBL:ACK52505.1, ECO:0000313|Proteomes:UP000002257};
RN [1] {ECO:0000313|EMBL:ACK52505.1, ECO:0000313|Proteomes:UP000002257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2
RC {ECO:0000313|Proteomes:UP000002257};
RX PubMed=20472789; DOI=10.1128/JB.00506-10;
RA Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT "Complete genome sequence of the aerobic facultative methanotroph
RT Methylocella silvestris BL2.";
RL J. Bacteriol. 192:3840-3841(2010).
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur atoms from cysteine
CC to produce alanine. Seems to participate in the biosynthesis of the
CC nitrogenase metalloclusters by providing the inorganic sulfur required
CC for the Fe-S core formation. {ECO:0000256|ARBA:ARBA00003120}.
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 ECO:0000256|RuleBase:RU364075};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004504};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490, ECO:0000256|RuleBase:RU364075}.
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DR EMBL; CP001280; ACK52505.1; -; Genomic_DNA.
DR RefSeq; WP_012592573.1; NC_011666.1.
DR AlphaFoldDB; B8EJ13; -.
DR STRING; 395965.Msil_3620; -.
DR KEGG; msl:Msil_3620; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_0_5; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000002257; Chromosome.
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 GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR017772; Cys_deSase_NifS_bac/arc.
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; TIGR03402; FeS_nifS; 1.
DR PANTHER; PTHR11601:SF63; CYSTEINE DESULFURASE; 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, ECO:0000256|RuleBase:RU364075};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364075};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364075};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU364075};
KW Reference proteome {ECO:0000313|Proteomes:UP000002257};
KW Transferase {ECO:0000256|RuleBase:RU364075}.
FT DOMAIN 4..367
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 400 AA; 42437 MW; F215D96616DEA3AB CRC64;
MKPIYLDNNA TTRVDPAVLE SMLPFFTEQF GNASSTHSFG ESVAGAIKTA RKQLQELLGA
AHDHEIIYTS GGTESNTTAI MAALEAMPGR DEIITSAVEH PSVLQLCEHL EKTGRAKVHV
IGVDSYGRLD LDGYRAALSD KVALVSIMWA NNETGTIVPV DALADLAKAA GALFHTDAVQ
AIGKLPVALK DTAIDMLSLS GHKLHAPKGI GALYVKRGVR FKPLIRGGHQ ERGRRAGTEN
VPAIVGLGKA AELAIQNFAD EQGRVRALRD RLEQAILASV ANCAVNGDLH DRLPNTSNIA
FDYIEGEAIL LHLTRAGIAA STGSACTAGS TEPSHVLRAM NVPEAALHGA IRFSLSRDNN
AADVDRVIEA LPPIVDKLRA LSPFWSDGKS PSGDATPLYA
//
