ID K9CGD0_9FIRM Unreviewed; 365 AA.
AC K9CGD0;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EKU70823.1};
GN ORFNames=HMPREF9161_01372 {ECO:0000313|EMBL:EKU70823.1};
OS Selenomonas sp. F0473.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=999423 {ECO:0000313|EMBL:EKU70823.1, ECO:0000313|Proteomes:UP000009883};
RN [1] {ECO:0000313|EMBL:EKU70823.1, ECO:0000313|Proteomes:UP000009883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0473 {ECO:0000313|EMBL:EKU70823.1,
RC ECO:0000313|Proteomes:UP000009883};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Blanton J.M., Baranova O.V.,
RA Mathney J., Dewhirst F.E., Izard J., Tanner A.C., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Selenomonas sp. Oral taxon 133 strain F0473.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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:EKU70823.1}.
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DR EMBL; AGZT01000007; EKU70823.1; -; Genomic_DNA.
DR RefSeq; WP_009728971.1; NZ_JH992902.1.
DR AlphaFoldDB; K9CGD0; -.
DR STRING; 999423.HMPREF9161_01372; -.
DR PATRIC; fig|999423.3.peg.1440; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_6_0_9; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000009883; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000009883}.
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 184
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 365 AA; 41219 MW; 7633898FD997082E CRC64;
MIMANNLLRQ FSLHAEEYEK KAVEVLRSGW YVLGNEVTSF ENEWATYIGA KYCVGLASGL
DALWISFRLL GIKEGDEVIV SANAYIACVM GITMNGATPV FVEPDRYDNI DAEKIEAAVT
PRTKAILAVH LYGQACDMTK IIDIARRHHL EVVEDCAQSH GNRWQGKIVG TFGRVGCFSF
YPTKGCGAFG DAGCIVTDDE DLAKKFRVFR NYGSEKKYHN TVVGCNSRLD ELQAGLLRVK
LAHMDELNAE RNRIADRYLE GITNPRVNLP QMRPGADSTW HQFVIHTALR DELQEYLTAR
GIGTMIHYPI PPHLSEAYRY LGHQRGDFPI AERYADEVLS LPMYNGMTKD EQDEVIRAVN
EFYFS
//
