ID R5FIA0_9FIRM Unreviewed; 538 AA.
AC R5FIA0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Aminotransferase class III {ECO:0000313|EMBL:CCY04543.1};
GN ORFNames=BN468_00993 {ECO:0000313|EMBL:CCY04543.1};
OS Faecalibacterium sp. CAG:1138.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=1262896 {ECO:0000313|EMBL:CCY04543.1, ECO:0000313|Proteomes:UP000018132};
RN [1] {ECO:0000313|EMBL:CCY04543.1, ECO:0000313|Proteomes:UP000018132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:1138 {ECO:0000313|Proteomes:UP000018132};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:CCY04543.1}.
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DR EMBL; CAXL010000050; CCY04543.1; -; Genomic_DNA.
DR AlphaFoldDB; R5FIA0; -.
DR STRING; 1262896.BN468_00993; -.
DR Proteomes; UP000018132; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CCY04543.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000018132};
KW Transferase {ECO:0000313|EMBL:CCY04543.1}.
SQ SEQUENCE 538 AA; 59097 MW; 24915EEA3C3F7E71 CRC64;
MSNGNGISKW PDANQIYKEL ADLTSKPIWC VSDEYLKKVL DHYEINCKGS KEITTEAKKY
IPGGVQHNLA FNYPFPLCMD KAEGAYLYDR DGNKYFDFLQ AGGPTILGSN YLPVREKVFE
LLNTCGPVTG LFHEGELLLA KKINELMPAC EMFRMLGSGT ESVMAAIRVA RCATKHKRII
KVGGAYHGWS DQMVYGLKIP GSRQFLESHG IPGSYKTTDE VRPNDLKMLE KMLRRNKLKG
GTAAVIVEPV GPESGTRPVD FDYNEKARIL AKKYGALFIF DEVVTGFRVG IHGAAGYFFG
DKYKVDDTPV FVDGKPWMID DKKIENGKVV KFRRQGTGRD MYPDLTVFGK IVAGGYPSAG
GVGGKKEYIG LMAAGLAGMG KKAYVGGTLA ANPLSSYAGY LAICEIEKQN ACEKAGHAGD
RLTAGLKELI KKHGLPFVVY NTGSIVHLEC TGAMSFDFSS FNILKSLIPM LKKKPEMLRR
KVAMEQMGAA YAANGIITLA GSRLYTSMAD TDEVVDAALE KFDEVFAHVT ECTRNLDK
//
