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Database: UniProt
Entry: A8GER6_SERP5
LinkDB: A8GER6_SERP5
Original site: A8GER6_SERP5 
ID   A8GER6_SERP5            Unreviewed;       452 AA.
AC   A8GER6;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=3-carboxy-cis,cis-muconate cycloisomerase {ECO:0000313|EMBL:ABV41606.1};
GN   OrderedLocusNames=Spro_2505 {ECO:0000313|EMBL:ABV41606.1};
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741 {ECO:0000313|EMBL:ABV41606.1};
RN   [1] {ECO:0000313|EMBL:ABV41606.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568 {ECO:0000313|EMBL:ABV41606.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       {ECO:0000256|ARBA:ARBA00034772}.
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DR   EMBL; CP000826; ABV41606.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8GER6; -.
DR   STRING; 399741.Spro_2505; -.
DR   KEGG; spe:Spro_2505; -.
DR   eggNOG; COG0015; Bacteria.
DR   HOGENOM; CLU_030949_3_3_6; -.
DR   OrthoDB; 9768878at2; -.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IEA:InterPro.
DR   CDD; cd01597; pCLME; 1.
DR   Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   InterPro; IPR019468; AdenyloSucc_lyase_C.
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; IPR012789; Protocat_PcaB-like.
DR   NCBIfam; TIGR02426; protocat_pcaB; 1.
DR   PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43172:SF2; ADENYLOSUCCINATE LYASE C-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF10397; ADSL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SMART; SM00998; ADSL_C; 1.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:ABV41606.1}.
FT   DOMAIN          361..440
FT                   /note="Adenylosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00998"
SQ   SEQUENCE   452 AA;  48395 MW;  4C0E2E6C39FE6528 CRC64;
     MELLTPLLRS SAVTPCFSDT ATLQGMLDFE AALANAQAGL GIIPVEAAQH ISEACHSHLF
     DAADLAQAAA QAGNLAIPLV KQLTRQVAQQ NAEAARFVHW GATSQDAIDT GLILQLRQAI
     ELTHSDLNRL IAALVSQMTR HQDCVLVGRT WMQHALPTTL GLKLAGTLDA LLRYRQRLDE
     MRPRVLALQL GGAAGTLASL GEQGSLLVTE LASRLQLTAA NTPWHSQRDR LLEIAGWYAG
     LCGSLGKLAR DISLLTQTEV AEVAEPVAAG RGGSSTMPHK RNPVACAVIL AAANRVPALV
     GGLYAAMVQE HERGLGGWHA EWESLPELVM LTAGALHTAG DLLDGLQVFP AQMEHNLKLT
     HGLIMAEAVT MALGDVMGRQ QAHQHIEKQC HLALAQQLTL LEVLLDDPVV MAHLSAQRLA
     ELLDPQQYLG SAKVFTQRVL EQAATSGANQ HE
//
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