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Database: UniProt
Entry: D2R684_PIRSD
LinkDB: D2R684_PIRSD
Original site: D2R684_PIRSD 
ID   D2R684_PIRSD            Unreviewed;       272 AA.
AC   D2R684;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=5-carboxymethyl-2-hydroxymuconateDelta-isomerase {ECO:0000313|EMBL:ADB15462.1};
DE            EC=5.3.3.10 {ECO:0000313|EMBL:ADB15462.1};
GN   OrderedLocusNames=Psta_0777 {ECO:0000313|EMBL:ADB15462.1};
OS   Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS   staleyi).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Pirellula.
OX   NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB15462.1, ECO:0000313|Proteomes:UP000001887};
RN   [1] {ECO:0000313|EMBL:ADB15462.1, ECO:0000313|Proteomes:UP000001887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC   {ECO:0000313|Proteomes:UP000001887};
RX   PubMed=21304671; DOI=10.4056/sigs.51657;
RA   Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA   Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA   Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA   Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL   Stand. Genomic Sci. 1:308-316(2009).
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DR   EMBL; CP001848; ADB15462.1; -; Genomic_DNA.
DR   RefSeq; WP_012909727.1; NC_013720.1.
DR   AlphaFoldDB; D2R684; -.
DR   STRING; 530564.Psta_0777; -.
DR   KEGG; psl:Psta_0777; -.
DR   eggNOG; COG0179; Bacteria.
DR   HOGENOM; CLU_028458_2_1_0; -.
DR   OrthoDB; 9805307at2; -.
DR   Proteomes; UP000001887; Chromosome.
DR   GO; GO:0008704; F:5-carboxymethyl-2-hydroxymuconate delta-isomerase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.850.10; Fumarylacetoacetase-like, C-terminal domain; 1.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   InterPro; IPR018833; Rv2993c-like_N.
DR   PANTHER; PTHR11820; ACYLPYRUVASE; 1.
DR   PANTHER; PTHR11820:SF112; FUMARYLACETOACETATE HYDROLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G02370)-RELATED; 1.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   Pfam; PF10370; Rv2993c-like_N; 1.
DR   SUPFAM; SSF56529; FAH; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:ADB15462.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001887}.
FT   DOMAIN          1..49
FT                   /note="Rv2993c-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10370"
FT   DOMAIN          55..262
FT                   /note="Fumarylacetoacetase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01557"
SQ   SEQUENCE   272 AA;  29716 MW;  6D66F00E5BA66450 CRC64;
     MKIVRFVNSA GEISYGEERG DEVYVIDGDP LTGCRVTNEV AEVEKILAPI VPKAIMCIGL
     NYRKHAEEGK APIPKFPVLF MKTPSAVQNP GDPIELPRTL ESTRVDFECE LAVVIGKRCK
     NVNKAHALDY VLGYTCGNDV SARDWQKDFG GSQWCRGKTF DTFAPLGPCL VLKDAIPDPN
     ALRISTKLNG EVMQDWNTSD MIFDVPTLIE FLSGSTTLEP GTVILTGTPH GVGMARTPPV
     FLKHGDVLTI EIEKIGILEN PVIDEPTPGK HA
//
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