ID R6FLT9_9CLOT Unreviewed; 380 AA.
AC R6FLT9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative perosamine synthetase {ECO:0000313|EMBL:CDB14258.1};
GN ORFNames=BN542_02399 {ECO:0000313|EMBL:CDB14258.1};
OS Clostridium sp. CAG:221.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262780 {ECO:0000313|EMBL:CDB14258.1, ECO:0000313|Proteomes:UP000018176};
RN [1] {ECO:0000313|EMBL:CDB14258.1, ECO:0000313|Proteomes:UP000018176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:221 {ECO:0000313|Proteomes:UP000018176};
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 DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, 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:CDB14258.1}.
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DR EMBL; CBDC010000008; CDB14258.1; -; Genomic_DNA.
DR AlphaFoldDB; R6FLT9; -.
DR Proteomes; UP000018176; 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:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 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|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2}.
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 191
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 380 AA; 42538 MW; 7D06555FD925B0C6 CRC64;
MSNKRIFLSS PHMGEFERKF VKEAFDTNWI APLGPNVNEF EKELSEYVGI KSAAALTSGT
SAIHLAVKLL DITKGDYVLC SSLTFCASCN PIVYEGGIPV FIDSEPESFN MSPKALKKAL
EDLKVKGITP KAAIVVNLYG NSANMDEIKE LCDEYNVKII EDAAESLGST YKGKMSGTFG
EIGIYSFNGN KIITTSGGGA LVSNNEEYVK KARFLSTQAK EPMPYYEHKE IGYNYRMSNV
VAGIGRGQLR VLDNRVKEKN HIFNTYKEAF KDIDDINMMP ITEGCTSNQW LSVITLKEES
KVKPTDIIDA LEKENIESRR IWKPMNLQPV YKDNMFYNHN ENGISVGEDI FNRGVCLPSD
TKMTNDDLKR VINIITSLFN
//
