ID M6ZZU7_9ACTN Unreviewed; 408 AA.
AC M6ZZU7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 2.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=3-carboxy-cis,cis-muconate cycloisomerase {ECO:0000313|EMBL:EMP11561.2};
GN ORFNames=ISGA_4623 {ECO:0000313|EMBL:EMP11561.2};
OS Gordonia sp. NB41Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=875808 {ECO:0000313|EMBL:EMP11561.2, ECO:0000313|Proteomes:UP000011989};
RN [1] {ECO:0000313|EMBL:EMP11561.2, ECO:0000313|Proteomes:UP000011989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB4-1Y {ECO:0000313|EMBL:EMP11561.2,
RC ECO:0000313|Proteomes:UP000011989};
RX PubMed=23744905; DOI=10.1099/mic.0.068932-0;
RA Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.;
RT "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in relation
RT to 6 : 2 fluorotelomer sulfonate biodegradation.";
RL Microbiology 159:1618-1628(2013).
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC {ECO:0000256|ARBA:ARBA00034772}.
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:EMP11561.2}.
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DR EMBL; APHK02000027; EMP11561.2; -; Genomic_DNA.
DR RefSeq; WP_053776285.1; NZ_CP132196.1.
DR AlphaFoldDB; M6ZZU7; -.
DR STRING; 1241906.ISGA_4623; -.
DR OrthoDB; 9768878at2; -.
DR Proteomes; UP000011989; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProt.
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; 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; ADSL_C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:EMP11561.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000011989}.
FT DOMAIN 18..293
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
SQ SEQUENCE 408 AA; 42864 MW; 1BC7B5FFB6A041CE CRC64;
MTDLLWPGDH HAGDVLTDAA VADAMIRVEA AWSTALTEAG VAPADALVDP AALRALIGDG
DLDRIAIEAE SGGNPVIPLV KLLRSGLGES ATAQWLHRGL TSQDVVDTAL MCCSATAFAE
IGGELTAQIR ILSRYADRFR ATPMVARTLT QYAVPMTFGL KAAQWLSGVL DASELLAGVR
FPLQIGGAAG TSAALLELAG PGHDPARLYR AATEVAAREL GLEAVPPWHS VRTAICRVGD
ASVACTDAWG HIANDVLTLS RPEIAEVGEG AGGSSSTMPH KSNPVLSVLI RRAALTGPPL
ASTLHLAAAD AVDERTPGAW HAEWDTLRQL VRRTLVAARQ TTRLLDKLQI HEDRMASRLQ
AAGQAVTSEQ KSMAGIAGLP PAADYLGATQ HLIDAQLERA RKVIGDRS
//