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Database: UniProt
Entry: R7H892_9FIRM
LinkDB: R7H892_9FIRM
Original site: R7H892_9FIRM 
ID   R7H892_9FIRM            Unreviewed;       113 AA.
AC   R7H892;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=L-dopachrome isomerase {ECO:0000256|ARBA:ARBA00042730};
DE            EC=5.3.2.1 {ECO:0000256|ARBA:ARBA00039086};
DE            EC=5.3.3.12 {ECO:0000256|ARBA:ARBA00038932};
DE   AltName: Full=L-dopachrome tautomerase {ECO:0000256|ARBA:ARBA00041631};
DE   AltName: Full=Phenylpyruvate tautomerase {ECO:0000256|ARBA:ARBA00041912};
GN   ORFNames=BN645_00608 {ECO:0000313|EMBL:CDE34412.1};
OS   Ruminococcus sp. CAG:403.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1262958 {ECO:0000313|EMBL:CDE34412.1, ECO:0000313|Proteomes:UP000017925};
RN   [1] {ECO:0000313|EMBL:CDE34412.1, ECO:0000313|Proteomes:UP000017925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:403 {ECO:0000313|Proteomes:UP000017925};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phenylpyruvate = enol-phenylpyruvate; Xref=Rhea:RHEA:17097,
CC         ChEBI:CHEBI:16815, ChEBI:CHEBI:18005; EC=5.3.2.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00036735};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-dopachrome = 5,6-dihydroxyindole-2-carboxylate;
CC         Xref=Rhea:RHEA:13041, ChEBI:CHEBI:16875, ChEBI:CHEBI:57509;
CC         EC=5.3.3.12; Evidence={ECO:0000256|ARBA:ARBA00036823};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:CDE34412.1}.
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DR   EMBL; CBIS010000223; CDE34412.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7H892; -.
DR   STRING; 1262958.BN645_00608; -.
DR   Proteomes; UP000017925; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.429.10; Macrophage Migration Inhibitory Factor; 1.
DR   InterPro; IPR001398; Macrophage_inhib_fac.
DR   InterPro; IPR014347; Tautomerase/MIF_sf.
DR   PANTHER; PTHR11954; D-DOPACHROME DECARBOXYLASE; 1.
DR   PANTHER; PTHR11954:SF6; MACROPHAGE MIGRATION INHIBITORY FACTOR; 1.
DR   Pfam; PF01187; MIF; 1.
DR   SUPFAM; SSF55331; Tautomerase/MIF; 1.
PE   4: Predicted;
KW   Cytokine {ECO:0000256|ARBA:ARBA00022514};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017925};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
SQ   SEQUENCE   113 AA;  12534 MW;  5170A19D862C73B1 CRC64;
     MPFIHIKTNK KVTAEQAHCI KSHLDLAIAA IPGKTADWLM VEVEENCNLF FRNSNDPAAM
     VEVSLYGKAS ENALSVFTSN ITGILLDVLS ISTDRTYVSY ALTEHWGWNG SNF
//
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