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Database: UniProt
Entry: A0A0D2ND29_GOSRA
LinkDB: A0A0D2ND29_GOSRA
Original site: A0A0D2ND29_GOSRA 
ID   A0A0D2ND29_GOSRA        Unreviewed;      1403 AA.
AC   A0A0D2ND29;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Mandelate racemase/muconate lactonizing enzyme C-terminal domain-containing protein {ECO:0000259|SMART:SM00922};
GN   ORFNames=B456_005G148400 {ECO:0000313|EMBL:KJB30552.1};
OS   Gossypium raimondii (New World cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB30552.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB30552.1, ECO:0000313|Proteomes:UP000032304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23257886; DOI=10.1038/nature11798;
RA   Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA   Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA   Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA   Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA   Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA   Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA   Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA   Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA   ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA   Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA   Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA   Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA   Wang X., Schmutz J.;
RT   "Repeated polyploidization of Gossypium genomes and the evolution of
RT   spinnable cotton fibres.";
RL   Nature 492:423-427(2012).
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DR   EMBL; CM001744; KJB30552.1; -; Genomic_DNA.
DR   EnsemblPlants; KJB30552; KJB30552; B456_005G148400.
DR   Gramene; KJB30552; KJB30552; B456_005G148400.
DR   OMA; YSMEMIA; -.
DR   Proteomes; UP000032304; Chromosome 5.
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; IPR029035; DHS-like_NAD/FAD-binding_dom.
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   PANTHER; PTHR42916; 2-SUCCINYL-5-ENOLPYRUVYL-6-HYDROXY-3-CYCLOHEXENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR42916:SF1; PROTEIN PHYLLO, CHLOROPLASTIC; 1.
DR   Pfam; PF12697; Abhydrolase_6; 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; SFLDS00001; Enolase; 1.
DR   SFLD; SFLDF00009; o-succinylbenzoate_synthase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 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:UP000032304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          838..934
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   1403 AA;  156066 MW;  DDFFDB0D441037BB CRC64;
     MELRDARFFK QFCFKFSPTI GVACNMLDHA SEMAYTIQDR ANINAVWASL IVEECFRLGL
     TYFCVAPGSR SSPLALAASA HLFVTCISCF DERSLAFHAI GYARGSQKAA VIITTSGTAV
     SNLFPAVVEA SEDFVPLLVL SADRPPELQD CGANQSINQV NHFGSFVRFF FSLPPPTDQI
     PARMVLTTLD SAVHWATSSP IGPVHINCPF REPLDDCPQN WKSSCLEGLD TWRSNTEPFT
     KYIIVQHSYL CNTATRGQME EVLEKIRRVN KGILVVGAIS AEDEVWAVLL MAKYLQWPVV
     ADILSGIRLR ELLSSSPEVE ESILFVDYLD HALLSDSVRD LVQFDVIVQI GSRITSNRIS
     QMLEKCFPCS YILVDNHPHR HDPSHFVTHR IQSSAIEFAN ILMKAQIPNR SRKWHYYLQA
     LNMMVGQEIS FHLSVEHSLS EPYIAHIISE ALSAESALFI GNSMVIRDAD MYGCNWTSDN
     HSVADMMLKT ELPCTGILVA GNRGASGIDG LLSTAIGFAV GCNKRVLCVV GDISFLHDTN
     GLAILKQRML RKPMTILVIN NRGGAIFSLL PVADRTDPRV LNQYFYTSHN ISVHGLCEAH
     GVKHLEVKTK MELHDALISS QKGDTDCVIE VESSIDSNAT FHSYIRKFAC RAAEHALGVI
     SKLSPPESMS QGCHCKIQSI SYSVYRIQLC APPTSSALYH DRSIFYREGF ILSLTLEDGS
     IGYGEVAPLE ISQENLLDVE EQLRFLFHVM KGVTINYFLP MLKSSFSSWI WKTLGIPVCS
     LFPSVRCGLE MAILNAIAMS HGSSLLNILY PLRERTEEKS ENLASIRICA LIDSSGTPEE
     VARIAVDLVE EGFTAIKIKV ARRADPVEDA AVIQEVRKKV GCHIDLRVDA NRNWTYEQAI
     KFGFLVKDYN LQYIEEPVQH ESDIIRYCEE SGLPVALDET IDNCPENPLN VLVKYNHHQI
     VALVIKPTVI GGFEKAAMIA QWAHIQGKMA IISAAFESGL ALSAYILFSC YLDLQNADTC
     KLMNNSPASS VAHGLGTYRW LEEDITTDPL GIGRNPSTGF IEASVADATH LLHKFQMNHN
     FIHRTFTGEK VLGYHLDLDS NDFSFSVNVQ EIGQRNNGST ILFLHGFLGT NEEWVPIMHA
     ISGSARCISV DLPGHGATKI KNCGDDKAAL RSLLSIEIIA DLLLKLIEHV TPDKVTLVGY
     SMGARIALYM ALKFSDKIEG AVILSGSPGL EDAVARKIRR VKDDSKARSI VTHGLQLFLN
     TWYSGGLWKS LRSHPYFNHI VVRRSVHDDL QGLARVLSGL SPGRQPSLWE DLKHCKVPLM
     LVVGENDEKF KRVAQKMWHE IGHDRDDAVS KLHQMVVVPS CGHAVHLENP LPIIRLVRQF
     VTGLRSVKLQ EKGNVRDLLI YNQ
//
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