ID A0A0Q5SZN5_9BACT Unreviewed; 388 AA.
AC A0A0Q5SZN5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:KQS27688.1};
GN ORFNames=ASG33_14740 {ECO:0000313|EMBL:KQS27688.1};
OS Dyadobacter sp. Leaf189.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=1736295 {ECO:0000313|EMBL:KQS27688.1, ECO:0000313|Proteomes:UP000051810};
RN [1] {ECO:0000313|EMBL:KQS27688.1, ECO:0000313|Proteomes:UP000051810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf189 {ECO:0000313|EMBL:KQS27688.1,
RC ECO:0000313|Proteomes:UP000051810};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS27688.1, ECO:0000313|Proteomes:UP000051810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf189 {ECO:0000313|EMBL:KQS27688.1,
RC ECO:0000313|Proteomes:UP000051810};
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:KQS27688.1}.
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DR EMBL; LMPS01000005; KQS27688.1; -; Genomic_DNA.
DR RefSeq; WP_056286773.1; NZ_LMPS01000005.1.
DR AlphaFoldDB; A0A0Q5SZN5; -.
DR STRING; 1736295.ASG33_14740; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000051810; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051810}.
FT DOMAIN 3..364
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 388 AA; 42186 MW; A4445D234AE5B0C1 CRC64;
MKIYCDNAAT TALDPEVIDA IIPYLSENYG NPSSTHWAGI KAREGVESAR RIVAALLGAS
PAEIYFTSGA TEANNLALTG AIRAYEISHV ITSKIEHKAV LQTLARYEKE GDIEISFVRL
DERGNVDLYH LENLLRANPR TLISLMHANN EIGNLTDIHA ISILAQRYNA IFHTDTTQTI
GKIRFDLSRE NVDFLVGSAH KFHGPKGVGF IYINKKHRIA PLILGGGQEG GQRGGTENVI
GIVGLARALE VAYRDLDEDQ LQVSKLKHYL VSKLAVSRIE GICYNGDGKS VENSIPNVLN
VSFPCLSAGS IVEQLDQAGI AASGGSACSS QGTSHVIAAL PCQKNKENVR FSFSKLNTFD
EVDYIVKVLT GIYEGVPAFY NESRLAII
//
