ID F0M4Q6_PSEPM Unreviewed; 375 AA.
AC F0M4Q6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Galactarate dehydratase L-talarate dehydratase {ECO:0000313|EMBL:ADX71251.1};
DE EC=4.2.1.- {ECO:0000313|EMBL:ADX71251.1};
DE EC=4.2.1.42 {ECO:0000313|EMBL:ADX71251.1};
DE Flags: Precursor;
GN OrderedLocusNames=Asphe3_00320 {ECO:0000313|EMBL:ADX71251.1};
OS Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG
OS 23796 / Sphe3) (Arthrobacter phenanthrenivorans).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudarthrobacter.
OX NCBI_TaxID=930171 {ECO:0000313|EMBL:ADX71251.1, ECO:0000313|Proteomes:UP000008639};
RN [1] {ECO:0000313|EMBL:ADX71251.1, ECO:0000313|Proteomes:UP000008639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18606 / JCM 16027 / LMG 23796 / Sphe3
RC {ECO:0000313|Proteomes:UP000008639};
RX PubMed=21677849; DOI=10.4056/sigs.1393494;
RA Kallimanis A., Labutti K.M., Lapidus A., Clum A., Lykidis A.,
RA Mavromatis K., Pagani I., Liolios K., Ivanova N., Goodwin L., Pitluck S.,
RA Chen A., Palaniappan K., Markowitz V., Bristow J., Velentzas A.D.,
RA Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT "Complete genome sequence of Arthrobacter phenanthrenivorans type strain
RT (Sphe3).";
RL Stand. Genomic Sci. 4:123-130(2011).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR633978-3};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR633978-3};
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DR EMBL; CP002379; ADX71251.1; -; Genomic_DNA.
DR RefSeq; WP_013599195.1; NC_015145.1.
DR AlphaFoldDB; F0M4Q6; -.
DR STRING; 930171.Asphe3_00320; -.
DR KEGG; apn:Asphe3_00320; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_3_1_11; -.
DR OrthoDB; 9796450at2; -.
DR Proteomes; UP000008639; Chromosome.
DR GO; GO:0008867; F:galactarate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:1990594; F:L-altrarate dehydratase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR CDD; cd03316; MR_like; 1.
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; IPR033978; L-talarate_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; SFLDF00134; L-talarate/galactarate_dehydra; 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;
KW Lyase {ECO:0000313|EMBL:ADX71251.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR633978-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR633978-3}.
FT DOMAIN 155..252
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-1"
FT ACT_SITE 307
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-1"
FT BINDING 25..27
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT BINDING 61..62
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT BINDING 205
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-3"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-2"
FT SITE 280
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000256|PIRSR:PIRSR633978-4"
SQ SEQUENCE 375 AA; 40954 MW; FB68D1C2F63DDA0F CRC64;
MSPVDLIRHV KLSTARLPLT VPISDAKVFT GRQKPMTEVV FLFAEITTEL GHTGVGFSYS
KRAGGPAQYA HAKEVAEGII GEDPNDIARI YTKLLWAGAS VGRSGVATQA LAAIDIALYD
LKAKRAGLSL AKFLGSYRDS VQTYNTSGGF LNATLEEVKA RATQSLEEGI GGIKIKVGLP
DSKEDLRRVA GIREHIGWDV PLMVDANQQW DRATALRMGR QLEEFNLVWI EEPLDAYDFE
GHAHLANVLD TPIATGEMLA SVAEHKGLIN ANGCDIIQPD APRVGGITQF LRLAALADER
GLGLAPHFAM EIHLHLAAAY PREPWVEHFD WLDPLFNERL ETKDGRMIVP DRPGLGVTLS
DEARAWTTES VEFGA
//
