ID A0A1G2MK63_9BACT Unreviewed; 397 AA.
AC A0A1G2MK63;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Aminotransferase class V domain-containing protein {ECO:0000259|Pfam:PF00266};
GN ORFNames=A3C72_03435 {ECO:0000313|EMBL:OHA24325.1};
OS Candidatus Taylorbacteria bacterium RIFCSPHIGHO2_02_FULL_43_32b.
OC Bacteria; Candidatus Taylorbacteria.
OX NCBI_TaxID=1802306 {ECO:0000313|EMBL:OHA24325.1, ECO:0000313|Proteomes:UP000177130};
RN [1] {ECO:0000313|EMBL:OHA24325.1, ECO:0000313|Proteomes:UP000177130}
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:OHA24325.1}.
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; MHRK01000013; OHA24325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2MK63; -.
DR STRING; 1802306.A3C72_03435; -.
DR Proteomes; UP000177130; 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}.
FT DOMAIN 7..384
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 397 AA; 43440 MW; C320A260549020D7 CRC64;
MSRNRLYFDS AATTPIDPKV LREYVWHLKN TTGNASSISK EGVAAKKVLE TSRKEVAASL
GARPLEVVFT SGGTESNNLA IMGTFESLGG SDFKTQNGKK FHAITTEIEH SSVLECFRQL
EKKGLQVTYL PVSSGGVIDS NVLKKALRPE TALVSIQYAN GEIGVIQPIR EISKVIRDFN
SRFAIHASRL KTQFHTDVSQ AASYLNLSVE RLGVDLMTLD SHKIYGPKGV GALYLRSGVK
ISQITFGGGQ EGGMRSGTEN VPAIAAFAKA LQICAVQREK ESLRLATLRD QIYSGILENI
GMEILVNGEM KNRLPNNLNI SIRDIDTEFL TLQLDAKGIA VSTKSACVDS DVGSYVVKAL
GGHPWRSKNT LRISLGRFTT IDQCRNFVRV LRGFLKK
//
