ID A0A0T5ZEV7_9ARCH Unreviewed; 453 AA.
AC A0A0T5ZEV7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Fumarate lyase, aspartate ammonia-lyase {ECO:0000313|EMBL:KRT61281.1};
DE EC=4.3.1.1 {ECO:0000313|EMBL:KRT61281.1};
GN ORFNames=XU09_C0006G0204 {ECO:0000313|EMBL:KRT61281.1};
OS Thaumarchaeota archaeon CSP1-1.
OC Archaea; Nitrososphaerota.
OX NCBI_TaxID=1640512 {ECO:0000313|EMBL:KRT61281.1, ECO:0000313|Proteomes:UP000051388};
RN [1] {ECO:0000313|EMBL:KRT61281.1, ECO:0000313|Proteomes:UP000051388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-1 {ECO:0000313|EMBL:KRT61281.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRT61281.1}.
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DR EMBL; LDXL01000006; KRT61281.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZEV7; -.
DR STRING; 1640512.XU09_C0006G0204; -.
DR PATRIC; fig|1640512.3.peg.984; -.
DR Proteomes; UP000051388; Unassembled WGS sequence.
DR GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; 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; IPR018951; Fumarase_C_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 PANTHER; PTHR42696; ASPARTATE AMMONIA-LYASE; 1.
DR PANTHER; PTHR42696:SF2; ASPARTATE AMMONIA-LYASE; 1.
DR Pfam; PF10415; FumaraseC_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:0000313|EMBL:KRT61281.1}.
FT DOMAIN 11..340
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 406..452
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 453 AA; 48916 MW; DFBBFA1109FD6CCC CRC64;
MKFRIDRDSL GNVKIPSDAY YGPFTGRALM QYHVTGNRSH PNLINAFVMV KRSAALANLK
VSAIDKKLGM AIINACDKIL AGKFLDQFVV DAINSGAGTA FNMNTNEVIA NIALIGLGKK
KGQYEYLHPN DHVNMSQSSN DTFPTAMHVA ILMNLKKTIP AIDGLIKSLS RKAKEFSNFK
KIGRTHLMDA LPVTLGSEFG AYATSITKAK NFLVGASKEL EYVALGGTAV GTGANAPRGY
RKFAITQLAN ISKLPVKPEK DMQYSLQSKF AVATVSSALR NLALEINKLA NDIRLMASGP
VAGMSEIGIP AVHAGSSIMP GKVNPSLAEC MNMICFNILG NDTAVSYAAQ SGQFELNVML
PGMLKCILES TDMLNNFLPI FSVNLIDGLT ANKEKLLKNI ENNPVIVTLL APKIGYLKSA
ELFKESLKTG KTIRELVISK KLLTVKEINS LLG
//
