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
//