ID A0A1F6Y7Z0_9BACT Unreviewed; 395 AA.
AC A0A1F6Y7Z0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Aminotransferase class V domain-containing protein {ECO:0000259|Pfam:PF00266};
GN ORFNames=A3G06_02810 {ECO:0000313|EMBL:OGJ02504.1};
OS Candidatus Nomurabacteria bacterium RIFCSPLOWO2_12_FULL_46_14.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801797 {ECO:0000313|EMBL:OGJ02504.1, ECO:0000313|Proteomes:UP000176192};
RN [1] {ECO:0000313|EMBL:OGJ02504.1, ECO:0000313|Proteomes:UP000176192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGJ02504.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MFVV01000044; OGJ02504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6Y7Z0; -.
DR STRING; 1801797.A3G06_02810; -.
DR Proteomes; UP000176192; 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; 2.
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}.
FT DOMAIN 31..161
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 178..378
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 395 AA; 43872 MW; BF6771344AD3CE48 CRC64;
MVSIYTTFMP KSNYRTRKIY LDYASGALKI AANPGAIHSL GVAEKDKLNK ARARIARLIG
ARPDEIIFTS GATEANNLAI LGLPRGHVVT TNIEHASVME TAKHQAAVTY VPVQPNGIID
PKKVRNALRP NTVLVSVIYA NNEIGTIQPI KEIAKEIRHY NKMYPYPTSP YRRGRIKGGI
IFHTDAVQAT NYLELNVEKL GVDLMTFNAA KIYGHHGIGV LYKKRNVRLS SLFFGGNQEF
GLRPGTENVA AAQNLARTLK QADKIKKQEV KRLTKLRDYF INKLEHSQIF KNTRMILNGD
KERRLPNNVN ITIPGIPGDL LVIELSAQGV MVGSKSACKE GEAGASQVIK AINPLAQDTD
GSVRFSLGRE TTKADIDRTL QTLFQILKKL KIWYN
//