ID Q39T67_GEOMG Unreviewed; 404 AA.
AC Q39T67;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=dTDP-4-dehydro-6-deoxyglucose aminotransferase {ECO:0000313|EMBL:ABB32557.1};
GN OrderedLocusNames=Gmet_2332 {ECO:0000313|EMBL:ABB32557.1};
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB32557.1, ECO:0000313|Proteomes:UP000007073};
RN [1] {ECO:0000313|EMBL:ABB32557.1, ECO:0000313|Proteomes:UP000007073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC {ECO:0000313|Proteomes:UP000007073};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABB32557.1, ECO:0000313|Proteomes:UP000007073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC {ECO:0000313|Proteomes:UP000007073};
RX PubMed=19473543; DOI=10.1186/1471-2180-9-109;
RA Aklujkar M., Krushkal J., DiBartolo G., Lapidus A., Land M.L., Lovley D.R.;
RT "The genome sequence of Geobacter metallireducens: features of metabolism,
RT physiology and regulation common and dissimilar to Geobacter
RT sulfurreducens.";
RL BMC Microbiol. 9:109-109(2009).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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; CP000148; ABB32557.1; -; Genomic_DNA.
DR RefSeq; WP_004513288.1; NC_007517.1.
DR AlphaFoldDB; Q39T67; -.
DR STRING; 269799.Gmet_2332; -.
DR KEGG; gme:Gmet_2332; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_1_1_7; -.
DR Proteomes; UP000007073; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF9; PROTEIN RV3402C; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ABB32557.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000007073};
KW Transferase {ECO:0000313|EMBL:ABB32557.1}.
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 404 AA; 44747 MW; 294CC512A86FF674 CRC64;
MKLKTSCDEL AVMGGSPAFS DTLHVGRPNI GDRSEFLERV NGILDRRWLT NNGICVQEFE
RRLEALLGVK HCIAMCNATV ALEITIRALG MTGEVIVPSF TFVATPHSLQ WQQITPVFCD
IDPETHSIDP RRVESLITPR TTGIIGVHLW GKPCKIEALA EIAGRRNLRL LFDAAHAFGC
SHNGRMIGSF GDAEVFSFHA TKFFNTFEGG AVATNDDDLA ARIRLMKNFG FAGYDNVVYI
GTNGKMSEIS AAMGLTSLDH LEEIITINRR NYAAYASGLA NVQGIRLVPY EGADRYNYQY
VVLEVDEQAA GIHRDMLLQA LHAENIMARR YFYPGCHRME PYRSYFPNAG MLLPETERLA
ERVLSLPTGT AVSEEDIVDI CSIIRLVLKN GVEVTNALAN GKNT
//
