ID R6CR64_9FIRM Unreviewed; 402 AA.
AC R6CR64;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Cys/Met metabolism pyridoxal-phosphate-dependent protein {ECO:0000313|EMBL:CDA73976.1};
GN ORFNames=BN718_02054 {ECO:0000313|EMBL:CDA73976.1};
OS Ruminococcus sp. CAG:579.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1262963 {ECO:0000313|EMBL:CDA73976.1, ECO:0000313|Proteomes:UP000018387};
RN [1] {ECO:0000313|EMBL:CDA73976.1, ECO:0000313|Proteomes:UP000018387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:579 {ECO:0000313|Proteomes:UP000018387};
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 ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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:CDA73976.1}.
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DR EMBL; CBCK010000188; CDA73976.1; -; Genomic_DNA.
DR AlphaFoldDB; R6CR64; -.
DR STRING; 1262963.BN718_02054; -.
DR Proteomes; UP000018387; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000018387}.
FT MOD_RES 214
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 402 AA; 44403 MW; 3B5AF93B474195EC CRC64;
MSEKKVHNYD GLSFTTRAIH VGNEPDPGTG AIEPAINMAN SFLLPYDPST MNWSASEDKI
YTRNGGVNQG LLEKKIANLE GGEDCVVLAS GVAALSALFF TKLKKGDHVI FSTVTYIATY
RIFNELWTEK WGIETSIVDC TDLEKVKAAI RPNTKLIHFE TPGNPTLCIC DIEGIVKLAH
EHGILVSADN TFSSPYNTRP LEYGVDFVVE SLTKYINGHG DSMGGAIIGN HEDMDKIRYQ
AQVNIGGVIS PFNAWLIMRG AVTFPLRMQV HNDNALAIAE WLEKQPCVSF VAYPGLKSHK
GHELAVKQMK NGFGGVLSFG LKGEHDLYNR VVTHLNIFTS AVSLGHDASL IVFLGEDDER
MYLYPQEFHG GFYRVAIGIE DKKDLIDDLR QAFKAEGLET VD
//
