ID A0A0Q7ZDG2_9ACTN Unreviewed; 372 AA.
AC A0A0Q7ZDG2;
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=Aminotransferase V {ECO:0000313|EMBL:KQZ69820.1};
GN ORFNames=ASD66_08915 {ECO:0000313|EMBL:KQZ69820.1};
OS Nocardioides sp. Root151.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736475 {ECO:0000313|EMBL:KQZ69820.1, ECO:0000313|Proteomes:UP000051274};
RN [1] {ECO:0000313|EMBL:KQZ69820.1, ECO:0000313|Proteomes:UP000051274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root151 {ECO:0000313|EMBL:KQZ69820.1,
RC ECO:0000313|Proteomes:UP000051274};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ69820.1, ECO:0000313|Proteomes:UP000051274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root151 {ECO:0000313|EMBL:KQZ69820.1,
RC ECO:0000313|Proteomes:UP000051274};
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:KQZ69820.1}.
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DR EMBL; LMGG01000004; KQZ69820.1; -; Genomic_DNA.
DR RefSeq; WP_056890783.1; NZ_LMGG01000004.1.
DR AlphaFoldDB; A0A0Q7ZDG2; -.
DR Proteomes; UP000051274; 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 GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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 Aminotransferase {ECO:0000313|EMBL:KQZ69820.1};
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:UP000051274};
KW Transferase {ECO:0000313|EMBL:KQZ69820.1}.
FT DOMAIN 6..355
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 372 AA; 38879 MW; 71021E48561A1D5E CRC64;
MTGSAYLDAA SSEPLHPAAR DTLMAALEHG YADPRRLHGP ARNARLMLDN AREVVAACLG
VRPDEVTFTP SGTHAVHLGV LGLLAGRARV SPVLAHSAVE HSSVVHAAQW HAARGGEVVE
LPVDREGRSS TELPDGPLGL VALQAANHEV GTIQPVEQVA EAARETPLFM DACAAAGRVA
LPDGWAAAAV SAHKWGGPAG VGALVVRKGA RWRQPFPGDD RIDERTTGFE NVPGALAAAA
ALQAMTAERD DLAARQHALV DEIRTRVAAT VPDVEVVGSA DHRLPHLVTF SCLYVDGEAL
VTELDRRGFG VASGSACTAS TLEPSHVLAA MGVLTHGNVR VSLTRDVDRT QVDAFLDVLP
EVVAAIRAEA GL
//
