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Database: UniProt
Entry: F4H6E1_CELFA
LinkDB: F4H6E1_CELFA
Original site: F4H6E1_CELFA 
ID   F4H6E1_CELFA            Unreviewed;       431 AA.
AC   F4H6E1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Cys/Met metabolism pyridoxal-phosphate-dependent protein {ECO:0000313|EMBL:AEE44453.1};
GN   OrderedLocusNames=Celf_0308 {ECO:0000313|EMBL:AEE44453.1};
OS   Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 /
OS   NCIMB 8980 / NCTC 7547).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=590998 {ECO:0000313|EMBL:AEE44453.1, ECO:0000313|Proteomes:UP000008460};
RN   [1] {ECO:0000313|EMBL:AEE44453.1, ECO:0000313|Proteomes:UP000008460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 /
RC   NCTC 7547 {ECO:0000313|Proteomes:UP000008460};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA   Woyke T.;
RT   "Complete sequence of Cellulomonas fimi ATCC 484.";
RL   Submitted (APR-2011) 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}.
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DR   EMBL; CP002666; AEE44453.1; -; Genomic_DNA.
DR   RefSeq; WP_013769483.1; NC_015514.1.
DR   AlphaFoldDB; F4H6E1; -.
DR   STRING; 590998.Celf_0308; -.
DR   KEGG; cfi:Celf_0308; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_635683_0_0_11; -.
DR   Proteomes; UP000008460; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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   PANTHER; PTHR11808:SF50; CYSTATHIONINE BETA-LYASE; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU362118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008460}.
SQ   SEQUENCE   431 AA;  45710 MW;  6D6FF1706A9CFB0B CRC64;
     MLAEFVRRHL RSLEPVAGPG DAARAARVDY LLAVADRTGP TELLSAYESI VHDRAAAHAG
     LDGVASGYAS MAELWDDVAR QEVGTSDRIL WDSYLNGHRV RVERALASAT GADTLLLTVS
     GMSAIDAVLT SALVPAGATV AVSDGAYFES ATYLDAQRRA GRVSVATFDP TSTASVGRAL
     ARADVLLLEP ADNAFPVREL DLAATAAVVR RVRPDVLVVV DTSLFGPAIP LSRLTGLFDR
     VVAVQSGSKY LTTRVSAGVV AADAQLGPVL RERVRQTGIG LPEAAVRLLV PGELASARER
     FDVQARGAQV LARAVDPRDW VSCRQPQVRL GDEVVRAPVL FLEPAPHTTP HVAAITDRWV
     RLAADDGGAL QVRAGFGWAL TTCRAYGADQ LNRPEGRSYV RVSVGLEPAA DLVRLGELLA
     ATTHDVLERA A
//
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