ID A0A177H5R8_9RHOB Unreviewed; 349 AA.
AC A0A177H5R8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558};
GN Name=nifS {ECO:0000313|EMBL:OAH05930.1};
GN ORFNames=pfor_36c3337 {ECO:0000313|EMBL:OAH05930.1};
OS Rhodobacteraceae bacterium SB2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1689867 {ECO:0000313|EMBL:OAH05930.1, ECO:0000313|Proteomes:UP000077333};
RN [1] {ECO:0000313|EMBL:OAH05930.1, ECO:0000313|Proteomes:UP000077333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB2 {ECO:0000313|EMBL:OAH05930.1,
RC ECO:0000313|Proteomes:UP000077333};
RA Poehlein A., Billerbeck S., Voget S., Wemheuer B., Giebel H.-A.,
RA Brinkhoff T., Daniel R., Simon M.;
RT "A new prominent pelagic Roseobacter clade subcluster - CHAB-I-5:
RT biogeography and genomic comparison to other roseobacters.";
RL Submitted (MAY-2016) 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. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490}.
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:OAH05930.1}.
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DR EMBL; LGRT01000037; OAH05930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177H5R8; -.
DR STRING; 1689867.pfor_36c3337; -.
DR PATRIC; fig|1689867.3.peg.3367; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000077333; Unassembled WGS sequence.
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 Gene3D; 1.10.260.50; -; 2.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR InterPro; IPR000192; Aminotrans_V_dom.
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 PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR Pfam; PF00266; Aminotran_5; 2.
DR PIRSF; PIRSF005572; NifS; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000077333};
KW Transferase {ECO:0000313|EMBL:OAH05930.1}.
FT DOMAIN 4..80
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 135..331
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 349 AA; 36567 MW; C75516608DE69D2C CRC64;
MNRVYLDYNA SAPLREEARE AMVHAMALAG NPSSVHAEGR QARAIVETAR QQVAAALGAQ
GADVIFTSGA TEAAGLALTG RGIRCADIEH EAVSSWCQSD LSCGLDGGVA CQAPGATALQ
LANSETGILQ QLPDGLALCD MTQAFGKLPV PFHWSGVTMA LVSAHKIGGP KGVGALIVKR
GTEVAAQIKG GGQEMGRRSG TENVIGIAGF GAAAEAAQRD LADGVWEQVE KLRNILEKAV
AQSASETIFV GQGGRRLPNT SYMISEGWRG ETQVMQMDLA GFSVSAGSAC SSGKVKRSRV
LQAMGFSAEQ AACALRVSLG PQNKQEDIER FVEVWGAHQH RLQGRRRSA
//
