ID A0A1G9VKQ0_9ACTN Unreviewed; 506 AA.
AC A0A1G9VKQ0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=3-carboxy-cis,cis-muconate cycloisomerase {ECO:0000313|EMBL:SDM72405.1};
GN ORFNames=SAMN04487981_102382 {ECO:0000313|EMBL:SDM72405.1};
OS Streptomyces sp. cf386.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1761904 {ECO:0000313|EMBL:SDM72405.1, ECO:0000313|Proteomes:UP000198720};
RN [1] {ECO:0000313|Proteomes:UP000198720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF386 {ECO:0000313|Proteomes:UP000198720};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FNHV01000002; SDM72405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9VKQ0; -.
DR STRING; 1761904.SAMN04487981_102382; -.
DR OrthoDB; 9768878at2; -.
DR Proteomes; UP000198720; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProt.
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 Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR InterPro; IPR019468; AdenyloSucc_lyase_C.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
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; 2.
DR PRINTS; PR00149; FUMRATELYASE.
DR SMART; SM00998; ADSL_C; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:SDM72405.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198720}.
FT DOMAIN 393..472
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
FT REGION 485..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 506 AA; 51521 MW; 50900B8CACA32EFE CRC64;
MNALSVGTDA GLLAPTWADT PAAAEVTDEA WLQAMLDAEV ALARAQYAVG RTPAAAVAAI
ASAARADRLD LVALARAARA TANPVVALVT AFTELVAAKD PAAAEYVHRG STSQDILDSA
AMLVARRVLG LIAADLDRVR AALAALADTH RHTVLAGRTL AQHAVPTTLG LKAAGWLQLV
ADALVRVRAV ASTLPAQLGG AAGTLAAYGE YAVLDGGQGE GDARKGEGNG MRGAGGTELL
RPFAQALGLA EPVLPWHTAR TPVADLGAVL QLVTGALGKF ALDVQTLSRT EIGEVSEPAA
TGRGASSAMP QKRNPVLATL IVSAARQVPA HALVLAQCML AEDERPAGAW HAEWQPLREA
LRLAGGAAHT AVELAEGLVV HPERMLANLE LTGGAVVAER LTVALAPALG KARAKTLLTA
ATAEASDTGR PLAEVLSEHP ELSARFTPAR LAELLDPAGY TGAADALVDR ALRAYGGLGA
IPDLGGRGGT PDLGGPVGTP DEEGMR
//
