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Database: UniProt
Entry: A0A1C5GMN4_9ACTN
LinkDB: A0A1C5GMN4_9ACTN
Original site: A0A1C5GMN4_9ACTN 
ID   A0A1C5GMN4_9ACTN        Unreviewed;       433 AA.
AC   A0A1C5GMN4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=L-fuconate dehydratase {ECO:0000256|ARBA:ARBA00013142};
DE            EC=4.2.1.68 {ECO:0000256|ARBA:ARBA00013142};
GN   ORFNames=GA0070213_101308 {ECO:0000313|EMBL:SCG35058.1};
OS   Micromonospora humi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=745366 {ECO:0000313|EMBL:SCG35058.1, ECO:0000313|Proteomes:UP000199360};
RN   [1] {ECO:0000313|EMBL:SCG35058.1, ECO:0000313|Proteomes:UP000199360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45647 {ECO:0000313|EMBL:SCG35058.1,
RC   ECO:0000313|Proteomes:UP000199360};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-fuconate = 2-dehydro-3-deoxy-L-fuconate + H2O;
CC         Xref=Rhea:RHEA:22772, ChEBI:CHEBI:15377, ChEBI:CHEBI:21291,
CC         ChEBI:CHEBI:37448; EC=4.2.1.68;
CC         Evidence={ECO:0000256|ARBA:ARBA00001737};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; FMDM01000001; SCG35058.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5GMN4; -.
DR   STRING; 745366.GA0070213_101308; -.
DR   OrthoDB; 9796450at2; -.
DR   Proteomes; UP000199360; Unassembled WGS sequence.
DR   GO; GO:0050023; F:L-fuconate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR034610; L-fuconate_dehydratase.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   InterPro; IPR046945; RHMD-like.
DR   PANTHER; PTHR13794; ENOLASE SUPERFAMILY, MANDELATE RACEMASE; 1.
DR   PANTHER; PTHR13794:SF58; MITOCHONDRIAL ENOLASE SUPERFAMILY MEMBER 1; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDF00111; L-fuconate_dehydratase; 1.
DR   SFLD; SFLDG00179; mandelate_racemase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR   PROSITE; PS00909; MR_MLE_2; 1.
PE   4: Predicted;
FT   DOMAIN          196..292
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   433 AA;  47123 MW;  59EB78512726ADC7 CRC64;
     MTRIVDVTVH DVRFPTAASG DGSDAINRGD YSATYVELTT DGGPTGTGFT FTNGRGNEIT
     CAAVRALAHH VRGRTVAEIA AEPVAFWRSL TADVQLRWLG PEKGVIHMAT GALVNAVWDL
     RAKIAGKPMW RFLAEMPTDD LVATVDFHHI TDALTPDEAA AILDKGRDGL AERLAGLERD
     GFPSYTTSVG WLGYPDEQVR ALTRYAYAAG WRAMKMKVGG RLDDDLRRAR IIRAEIGPDA
     LLMMDANQVW DVDEAITSMA ALVEVDPYWI EEPTHADDVL GHARIARAVS ELSAGRCRVA
     TGEVAANRVV FKQLLQAEAI GVMQVDACRV GGVDEVLAEL LLAAKFGVPV CPHAGGVGLC
     EYVQHLAVFD HLRVSTGLDG RMVEYVDHLH EHFVDPVRTR GGRYLLPTAP GYSAAMRPES
     IAEFRFPDGP AWR
//
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