ID A0A445AM59_ARAHY Unreviewed; 1709 AA.
AC A0A445AM59;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Mandelate racemase/muconate lactonizing enzyme C-terminal domain-containing protein {ECO:0000259|SMART:SM00922};
GN ORFNames=Ahy_B01g051462 {ECO:0000313|EMBL:RYR27430.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR27430.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR27430.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR27430.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:RYR27430.1}.
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DR EMBL; SDMP01000011; RYR27430.1; -; Genomic_DNA.
DR STRING; 3818.A0A445AM59; -.
DR Proteomes; UP000289738; Chromosome b01.
DR GO; GO:0070204; F:2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity; IEA:InterPro.
DR GO; GO:0070205; F:2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07037; TPP_PYR_MenD; 1.
DR CDD; cd02009; TPP_SHCHC_synthase; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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 Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR HAMAP; MF_01659; MenD; 1.
DR HAMAP; MF_01660; MenH; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR004433; MenaQ_synth_MenD.
DR InterPro; IPR032264; MenD_middle.
DR InterPro; IPR022485; SHCHC_synthase_MenH.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR01927; menC_gam_Gplu; 1.
DR NCBIfam; TIGR00173; menD; 1.
DR NCBIfam; TIGR03695; menH_SHCHC; 1.
DR PANTHER; PTHR42916; 2-SUCCINYL-5-ENOLPYRUVYL-6-HYDROXY-3-CYCLOHEXENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR42916:SF1; PROTEIN PHYLLO, CHLOROPLASTIC; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF16582; TPP_enzyme_M_2; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SFLD; SFLDG00180; muconate_cycloisomerase; 1.
DR SFLD; SFLDF00009; o-succinylbenzoate_synthase; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00909; MR_MLE_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1161..1257
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 1709 AA; 188672 MW; 3B45F06BDD07438B CRC64;
MISLTAARFS SVPTFFILSP SSSPFIFVGA RRRPSPPKRT VAAGARMGGG ARFDGPVPVS
GDIEENDVVF EHCVTRTLPP AVTLEEGLRK IKDSIETLKL SPPRSSTGFL RFQVAVPPSP
KALNWFCSQP ELSGVYPLIY LSKNVDNPTL KSLYVNGSRG LFGIGSAVSF SRSSSGKPSM
IKRYISSDST HIVAYGFVDI NFDSDSISMN IEDGSFYFFI PEIELDELEC ISILTVTLAW
NDFSLSTFEE ALHSLEISLN QIMCYTWSGS DTLKLKSVRS GLRKLNLVED RAIARVYMNT
ITPGRRESVV DILELKESPS SSQFCVRLSA THAVSHNMLD QSNKLSSSLI ECANINAVWA
SLIVEECSRL GLTYFCVAPG SRSSPLAVAA SSHKLITCIS CFDERSLAFH AVGYARGSHV
PAVVITSSGT AVSNLLPAVV EASQDFVPLL LLTADRPPEL LDCGANQAID QVNHFGVYVR
YFFNLPAPTD QILTNMVLTT LDSAIHRAIT SPCGPVHINC PFREPLESTP RKWRLSCLNG
LDLWISNAEP FTKYIHMRPS CIDAVGEMME VIGLMQKGKH GLILFGAIHT EDEMWAALLL
AKHLCWPVFA DILSGLRLKK ILTSFPDIER NFLFIDNLDH ALLSDSVKGL LEIDVVIQLG
SRITSKRVCQ ILEERAPFPY IVVDKHPLRH DPSHIVTHRI QTTIVDFVGF LVKAEFPHTE
RIWSTSLQLL SKMVEWEILF QINAECSLTE PYVAHMMSDA LSSESALFLG NSMPIRDVDM
YGLGWSTSNP SVASIMLNSD LPVNLMRVAG NRGASGIDGL LSTAIGFAVG SNKRVAIYVI
RIINLLILAG GNVFCLVGDI SLLHDTNSLA ILYQRKLRKP MTIFVVNNHG GAIFSLLPLA
DKVEPSILHQ YFYTSHNIFI QGLCMAHGIK HLHVKTKAEF EDALRLAQHE QVDCMVEIDS
SIDANANFHS ILRKHSLGAV KDAMRYIPNP GAIKDQHYLY KIRTMECLRY RFALSAPPTS
ASVGDNHDEF YREGFIISLI LEDGSVGFGE VAPIEIHREN LVDAEYQLRF LVHIMRQVNI
SCFLSLLKGT FSYWIWNELG IVPSSIFPSV RCGLEMAILN AIAAAKGSNL LNLLHPPISE
KDECETSSVQ VCALLDSNGS PTDVANVAAT LVEEGFSAIK LKVARRYNPT QDAMVIKEVR
KKVGCQIIIR ADANRKWTYE EAMEFSSLVK DCNLQFIEEP VQDEDDIVKF CEESGLPVAL
DETIDKIQEN PLGTLVKFTH PGIVAVVIKP SVVGGFENAA LIGRWAHQLG KMAVVSAAFE
SSLSLSAYAQ FSSYLDMLSF DTVNKLHGKK VPSVAHGLGT YRWLKEDATI NPVLIGRNPH
SGIVEASVPN ASRLLHNFQI NQNVICDIID EEQVLKYQLK LELSSLSCSF EVQETGQKTN
DNVLVFLHGF LGAGEDWSPI MKSFSGSARC ISVDLPGHGK SIIHGVNDAC EEPLLSMEII
ANIFHQLLHH ITPGKVTLVG YSMGARIALY LALRFSSKIK GAVLISGSPG LKDKLSQKIR
SAKDDSRASS IISHGLESFL NSWYAADLWK SLRSHPHFTR ITANRLQHED LQSLAKMLSG
LSIGRQPSLW KDLPNCRTPL LIIHGEKDAK FKKIAQEIMN RVRSGVGSNQ EKVNIDIHEV
VEIPNCGHAV HLENPLPVVS ALRRFLTTL
//
