ID C7MXB3_SACVD Unreviewed; 398 AA.
AC C7MXB3;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Cysteine desulfurase family protein {ECO:0000313|EMBL:ACU95922.1};
GN OrderedLocusNames=Svir_08620 {ECO:0000313|EMBL:ACU95922.1};
OS Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / NBRC
OS 12207 / P101).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=471857 {ECO:0000313|EMBL:ACU95922.1, ECO:0000313|Proteomes:UP000000841};
RN [1] {ECO:0000313|EMBL:ACU95922.1, ECO:0000313|Proteomes:UP000000841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101
RC {ECO:0000313|Proteomes:UP000000841};
RX PubMed=21304650; DOI=10.4056/sigs.20263;
RA Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Chain P., D'haeseleer P., Chen A., Palaniappan K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Rohde M., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Saccharomonospora viridis type strain
RT (P101).";
RL Stand. Genomic Sci. 1:141-149(2009).
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}.
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DR EMBL; CP001683; ACU95922.1; -; Genomic_DNA.
DR RefSeq; WP_012796351.1; NC_013159.1.
DR AlphaFoldDB; C7MXB3; -.
DR STRING; 471857.Svir_08620; -.
DR KEGG; svi:Svir_08620; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_0_11; -.
DR Proteomes; UP000000841; 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 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; 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; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
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:UP000000841}.
FT DOMAIN 2..373
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 398 AA; 41833 MW; 1985F5C21CC7886C CRC64;
MTYLDHAATT PMVPEALEAM TEALSTLGNA SSLHSSGRRA RRVVEEARES VAEATGARPS
EVIFTAGGTE SNNLAVKGMF WARRRSDPRR RRVLAGSVEH HAVLDAVQWL ADHEGAEVTW
LQVDQHGQVR PEVLRAAIEE NPDDVALATV MWANNEVGTI NPLPELAAVC AEYDIPVHTD
AVQAIGAVDV DFGSSGAGAL ALTGHKLGGP YGAGVLLLGR DTPCVPLLHG GGQERDVRSG
TLDVPSIHAL ATAVRISVQR RREHVERLTK LRNDLVAAVR AEVPDVVLNG PPQDSDDRLP
GIAHLTFPGC AGDSLLMLLD AKGIECSTGS ACTAGVAEPS HVLLAMGADA ASARSSLRFS
LGHTSTQADI DALAAEIGGV VARARQAGLS GMRKSRTE
//
