ID A0A133VDQ8_9EURY Unreviewed; 390 AA.
AC A0A133VDQ8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Aminotransferase class V domain-containing protein {ECO:0000259|Pfam:PF00266};
GN ORFNames=AKJ48_02160 {ECO:0000313|EMBL:KXB04561.1};
OS candidate division MSBL1 archaeon SCGC-AAA261O19.
OC Archaea; Euryarchaeota; candidate division MSBL1.
OX NCBI_TaxID=1698277 {ECO:0000313|EMBL:KXB04561.1, ECO:0000313|Proteomes:UP000070076};
RN [1] {ECO:0000313|EMBL:KXB04561.1, ECO:0000313|Proteomes:UP000070076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC-AAA261O19 {ECO:0000313|EMBL:KXB04561.1};
RX PubMed=26758088; DOI=10.1038/srep19181;
RA Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT pools of the Red Sea.";
RL Sci. Rep. 6:19181-19181(2016).
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:KXB04561.1}.
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; LHYB01000023; KXB04561.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133VDQ8; -.
DR PATRIC; fig|1698277.3.peg.291; -.
DR Proteomes; UP000070076; 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; 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:UP000070076}.
FT DOMAIN 18..375
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 390 AA; 41879 MW; 9D816ED58ECD1836 CRC64;
MDENTGSGLV SSEGDGWVYL DHAATTPLAE EAVSAMRPFL EGRHENPSAS YGGSAKRAVE
DARGKVASLF DTDRENVIFT GCGSESDNMA VKGVFETEDG DHIVTSTIEH PAVRNACSFL
ERKGADVTWV SPDEDGRINP SDVENAVRED TILISIMHAN NETGVIQPLR EIGEIADEND
VLFHSDTVQS AGKIPTPADE IGLDLASLSA HKFYGPKGVG ALYVRDGTEL EPLIHGGGQE
RGLRGGTENV SGIVGMGKAA ELALADLEER KNRLSGLRER LIEEVRGRTG ARLVGDPENR
LPGYALFCFE DMSGPEIVEA LAERGIAASS GSACHSGDPE PSRVLKEMGV ERKYATGTLR
ISMGRKTTEE DVDKVVKNLE EITEEVRSSK
//
