ID A0A0Q9KN55_9MICO Unreviewed; 394 AA.
AC A0A0Q9KN55;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:KRE38658.1};
GN ORFNames=ASG73_06555 {ECO:0000313|EMBL:KRE38658.1};
OS Janibacter sp. Soil728.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=1736393 {ECO:0000313|EMBL:KRE38658.1, ECO:0000313|Proteomes:UP000051572};
RN [1] {ECO:0000313|EMBL:KRE38658.1, ECO:0000313|Proteomes:UP000051572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE38658.1,
RC ECO:0000313|Proteomes:UP000051572};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE38658.1, ECO:0000313|Proteomes:UP000051572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE38658.1,
RC ECO:0000313|Proteomes:UP000051572};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004504};
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:KRE38658.1}.
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DR EMBL; LMRZ01000003; KRE38658.1; -; Genomic_DNA.
DR RefSeq; WP_055992820.1; NZ_LMRZ01000003.1.
DR AlphaFoldDB; A0A0Q9KN55; -.
DR STRING; 1736393.ASG73_06555; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000051572; 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; -; 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; 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.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 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}.
FT DOMAIN 3..376
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 394 AA; 40759 MW; 221A21D7F5199B88 CRC64;
MTTYLDHAAT TPMTPAAREA MVEQLAITGN ASSLHGPGRD ARRVVEESRE RIAAALGARP
SEILFTSGGT ESDNLAITGS LRAARAADPR RSRVVVSGVE HHAVLDVVDH AVEHEGARAT
FVAPGECGTV KPDAVRAAIE EDASTVGLVS VMWANNEVGT VQDVASMAQI AHEHGLAFHT
DAVQAAGHLP VDFAASGVDL MSVSAHKLGG PIGIGALVAK RDARLVALSH GGGQERGIRS
GTLDTPAIRA FAVALTEAVE HREAEAERVG ALRDRFLAGT QALDLGIRVT GCWEAGDITT
RLPGNAHITI PGCEGDSMLY LLDAADVAVS TGSACQAGIP QPSHVVLAMG RSEEEARGSL
RVSFGWTSTQ ADVDAVLAAL PEAVTRARRA SGAA
//
