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Database: UniProt
Entry: A0A1F6Y7Z0_9BACT
LinkDB: A0A1F6Y7Z0_9BACT
Original site: A0A1F6Y7Z0_9BACT 
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}.
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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
//
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