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Database: UniProt
Entry: E6K0E1_PARDN
LinkDB: E6K0E1_PARDN
Original site: E6K0E1_PARDN 
ID   E6K0E1_PARDN            Unreviewed;       493 AA.
AC   E6K0E1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=Lyase {ECO:0000313|EMBL:EFT84214.1};
GN   ORFNames=HMPREF0620_1219 {ECO:0000313|EMBL:EFT84214.1};
OS   Parascardovia denticolens DSM 10105 = JCM 12538.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Parascardovia.
OX   NCBI_TaxID=864564 {ECO:0000313|EMBL:EFT84214.1, ECO:0000313|Proteomes:UP000004946};
RN   [1] {ECO:0000313|EMBL:EFT84214.1, ECO:0000313|Proteomes:UP000004946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10105 {ECO:0000313|EMBL:EFT84214.1,
RC   ECO:0000313|Proteomes:UP000004946};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes two reactions in de novo purine nucleotide
CC       biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-
CC       succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-
CC       D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-
CC       carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-
CC       ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate
CC       (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP)
CC       and fumarate. {ECO:0000256|ARBA:ARBA00025012}.
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:EFT84214.1}.
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DR   EMBL; AEON01000001; EFT84214.1; -; Genomic_DNA.
DR   RefSeq; WP_006289818.1; NZ_CM001148.1.
DR   AlphaFoldDB; E6K0E1; -.
DR   KEGG; pdo:PSDT_0450; -.
DR   PATRIC; fig|864564.6.peg.494; -.
DR   eggNOG; COG0015; Bacteria.
DR   HOGENOM; CLU_025566_2_0_11; -.
DR   Proteomes; UP000004946; Chromosome.
DR   GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:InterPro.
DR   GO; GO:0006188; P:IMP biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   InterPro; IPR047136; PurB_bact.
DR   InterPro; IPR013539; PurB_C.
DR   PANTHER; PTHR43411; ADENYLOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43411:SF1; ADENYLOSUCCINATE LYASE; 1.
DR   Pfam; PF08328; ASL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EFT84214.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004946}.
FT   DOMAIN          17..328
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          350..469
FT                   /note="Adenylosuccinate lyase PurB C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08328"
SQ   SEQUENCE   493 AA;  54590 MW;  403F1432E48DADBC CRC64;
     MELAEITPGL ALSPLDGRYQ AQTLPLVEYL SEAALNRERM VVEVEWMIHL ANGSHDADAD
     SRIPGVSPLT AEEIAYLHAI PEDFGAEGIE ELAEIEAVTH HDVKAVEYYI DRRLDAAAQS
     LGESSQLPRL KPLVHFSCTS EDINNLSYAL CLKQAVEKVW HPRIQELLDK LDSASQKFAS
     TPLLSLTHGQ PATPTTLGKE LAVYVYRLNR QLAKVDGQEY LGKINGATGT FGAHSVALPQ
     VDWISVSRSF VEDRLHLTWN PLTTQIESHD WQAELYSTMS HINHILHNLA VDIWMYISRG
     VFAQVPVKGA TGSSTMPHKV NPIRFENAEA NLELSCALFD SLSATLVETR WQRDLTDSTA
     QRNIGTAFGY NLLALYNLTG GLDSIHPDES TMEAELESNW EVLGEPIQTA MRAAALEGRE
     GMGNPYERVK ELMRGKRINQ ADVESFIATL NFDPETSQRL AALTPRTYVG LAADLVAFRE
     VRGKESQSTK AGQ
//
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