ID A0A0Q6V4H2_9ACTN Unreviewed; 374 AA.
AC A0A0Q6V4H2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:KQV73620.1};
GN ORFNames=ASC61_00510 {ECO:0000313|EMBL:KQV73620.1};
OS Aeromicrobium sp. Root344.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736521 {ECO:0000313|EMBL:KQV73620.1, ECO:0000313|Proteomes:UP000051702};
RN [1] {ECO:0000313|EMBL:KQV73620.1, ECO:0000313|Proteomes:UP000051702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root344 {ECO:0000313|EMBL:KQV73620.1,
RC ECO:0000313|Proteomes:UP000051702};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV73620.1, ECO:0000313|Proteomes:UP000051702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root344 {ECO:0000313|EMBL:KQV73620.1,
RC ECO:0000313|Proteomes:UP000051702};
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 -!- 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:KQV73620.1}.
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DR EMBL; LMDH01000001; KQV73620.1; -; Genomic_DNA.
DR RefSeq; WP_056207829.1; NZ_LMDH01000001.1.
DR AlphaFoldDB; A0A0Q6V4H2; -.
DR STRING; 1736521.ASC61_00510; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000051702; 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; 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:UP000051702}.
FT DOMAIN 2..357
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 374 AA; 39028 MW; E81FA7369D9341A0 CRC64;
MIYLDEAATT PLKREVLEAM WPYFGPDFGN PSSHHEVGES ASRALEQARA DVAQALGARA
SEITFTSGGT ESDNAAIKGI ALAAPRGKHV IVSSIEHPAV LESAEFLGRL GYDVTVLDVD
HDGMVQPAAL TEALRDDTTL VSIQYANNEV GTIQQVESLS RLAAAKGVPF HTDAVQAAGW
LDLDVDRLGV QAMSVSGHKL GAPKGIGILY VRRGTRWEPL IHGGGQESGR RSGTENVAAA
VGMATAFTLT GGSNDETIAR RDAFIDRVLA DVPGAELTGH RNHRLPGSAS FVFPGTNGET
ILLELEARGI VCSSGSACAA GSDEPSHVLT AMGYDGPVAQ TAVRFTFGRT TTAEDLDTAA
TELARAVAAV SALG
//
