ID C7GZ64_9FIRM Unreviewed; 445 AA.
AC C7GZ64;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Aminotransferase, class III {ECO:0000313|EMBL:EEU03959.1};
GN ORFNames=GCWU000322_00267 {ECO:0000313|EMBL:EEU03959.1};
OS Eubacterium saphenum ATCC 49989.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis.
OX NCBI_TaxID=592031 {ECO:0000313|EMBL:EEU03959.1, ECO:0000313|Proteomes:UP000018436};
RN [1] {ECO:0000313|EMBL:EEU03959.1, ECO:0000313|Proteomes:UP000018436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49989 {ECO:0000313|EMBL:EEU03959.1,
RC ECO:0000313|Proteomes:UP000018436};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (AUG-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 -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004746}.
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:EEU03959.1}.
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DR EMBL; ACON01000001; EEU03959.1; -; Genomic_DNA.
DR AlphaFoldDB; C7GZ64; -.
DR STRING; 592031.GCWU000322_00267; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_615031_0_0_9; -.
DR Proteomes; UP000018436; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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; 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; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF21; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:EEU03959.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000018436};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEU03959.1}.
SQ SEQUENCE 445 AA; 50322 MW; 0F80BA18D4918861 CRC64;
MLCEKERFVM DYLKGDERYL WHSNRDFNPL NFDKNILLTE AFENTFKDQY GNEYIDMLSA
GGCALFSLSD VEEATKVAGE VKLGAGYFEG FTNKYIIDLA EDLSNILPVG LGRFIFSNSS
QSAKHIAMKM SLMANAISGY KEKKSILFVP LGTSKNLALY TCDGDALRDA DIIFGKADNM
QTESVNDVLS SDIDQYFQGL KRIFKQKGHR ISAILVEPYT LFSYGSDLYK AEYMRELRNL
CDKHKIHMII NEQYTGLGKT CKYFYSDYLN VTPEFLLLGE SLTSGIAPIG LTVTTESIYE
IFNSDRQKTL KFIHNSPNTG NAFSAAIANN FVLKLSKRGY LDDVKERAKK LYVNLKNDLE
EHRNVSKIIN LGFINLIQMV DVKSNEAFDE SMKISERIVK KALENGIILA SKENMLVLNP
ALDMSLDDIK KATKRIQKSI VEVLG
//
