GenomeNet

Database: UniProt
Entry: A0A1N7GZA8_9ACTN
LinkDB: A0A1N7GZA8_9ACTN
Original site: A0A1N7GZA8_9ACTN 
ID   A0A1N7GZA8_9ACTN        Unreviewed;       286 AA.
AC   A0A1N7GZA8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Maleylpyruvate isomerase {ECO:0000313|EMBL:SIS17923.1};
GN   ORFNames=SAMN05421833_13473 {ECO:0000313|EMBL:SIS17923.1};
OS   Microbispora rosea.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Microbispora.
OX   NCBI_TaxID=58117 {ECO:0000313|EMBL:SIS17923.1, ECO:0000313|Proteomes:UP000186096};
RN   [1] {ECO:0000313|EMBL:SIS17923.1, ECO:0000313|Proteomes:UP000186096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12950 {ECO:0000313|EMBL:SIS17923.1,
RC   ECO:0000313|Proteomes:UP000186096};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FTNI01000034; SIS17923.1; -; Genomic_DNA.
DR   RefSeq; WP_076441487.1; NZ_FTNI01000034.1.
DR   AlphaFoldDB; A0A1N7GZA8; -.
DR   STRING; 58117.SAMN05421833_13473; -.
DR   OrthoDB; 5118203at2; -.
DR   Proteomes; UP000186096; Unassembled WGS sequence.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 1.20.120.450; dinb family like domain; 1.
DR   InterPro; IPR034660; DinB/YfiT-like.
DR   InterPro; IPR017517; Maleyloyr_isom.
DR   InterPro; IPR024344; MDMPI_metal-binding.
DR   NCBIfam; TIGR03083; maleylpyruvate isomerase family mycothiol-dependent enzyme; 1.
DR   Pfam; PF11716; MDMPI_N; 1.
DR   SUPFAM; SSF109854; DinB/YfiT-like putative metalloenzymes; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:SIS17923.1};
KW   Pyruvate {ECO:0000313|EMBL:SIS17923.1}.
FT   DOMAIN          11..147
FT                   /note="Mycothiol-dependent maleylpyruvate isomerase metal-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF11716"
FT   REGION          228..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..286
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   286 AA;  31018 MW;  6CEA540733CAD649 CRC64;
     MSVIDETERE LAEATERLLA TVARLTDEDL RAPSLLPGWT RGHVLTHVAR NADSCVNLLT
     WARTGVRTPQ YASARAREAG IEAGAGRPAG EQLADLRDSA ERFAAALRQT PAQAWTTPVS
     GMHPPDHPAW YVPIRRLREV EVHHADLGAG YGWADWPETY VRRELYDTML WLGDESPVGE
     VVALDPGTGE VLRTWTGLGE GPAVEGTPRE LLAWFAGRTD GTGLRLAAPR GHIRHDAPDA
     RLRHDAPDAG VRRDAAGKLP SPPPWPRTSP AGLPAEPPSS WPPAGN
//
DBGET integrated database retrieval system