ID D0GKD4_9FUSO Unreviewed; 380 AA.
AC D0GKD4;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Aminotransferase, class V {ECO:0000313|EMBL:EEY35451.1};
GN ORFNames=HMPREF0554_0677 {ECO:0000313|EMBL:EEY35451.1};
OS Pseudoleptotrichia goodfellowii F0264.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Pseudoleptotrichia.
OX NCBI_TaxID=596323 {ECO:0000313|EMBL:EEY35451.1, ECO:0000313|Proteomes:UP000004226};
RN [1] {ECO:0000313|EMBL:EEY35451.1, ECO:0000313|Proteomes:UP000004226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0264 {ECO:0000313|EMBL:EEY35451.1,
RC ECO:0000313|Proteomes:UP000004226};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (OCT-2009) 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:EEY35451.1}.
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; ADAD01000074; EEY35451.1; -; Genomic_DNA.
DR RefSeq; WP_006806945.1; NZ_ADAD01000074.1.
DR AlphaFoldDB; D0GKD4; -.
DR eggNOG; COG1104; Bacteria.
DR Proteomes; UP000004226; Unassembled WGS sequence.
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; 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 Aminotransferase {ECO:0000313|EMBL:EEY35451.1};
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:UP000004226};
KW Transferase {ECO:0000313|EMBL:EEY35451.1}.
FT DOMAIN 4..366
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 380 AA; 42265 MW; C710ED7DE912F01C CRC64;
MKQVYLDNAA STKMMPKVIE KIAESYGEIY ANPSSTHRLG QKAKGIIEKT RNIIAGCLGA
EANEIIFTSG GAEGNNLILR GALNAYEYKG KHIITSKIEH STVLKTCQQL EREGYEVTYI
DVDKNGVIDI EQLKNSVRKD TVIVSIMYVN NETGVKQPIE EIGKILEGTS VLFHTDAVQA
VGKEIILPKN VRISALTATA HKFYGPKGAG FIFLDKNFLV EKEIWGGSQE RNRRAGTENI
QGIIGLGTAL EEVYKTMYEE KGKEDELHTY MENRLRNEIE KIKINGENAP RIKTITNLCI
EGCDVQTLLI ALDLRGIYVS GGSACMSGAH ENSHVLKAMG LPEKELKSSF RISIGKYTTK
EEIDYFIDNL KEIVKIERGE
//