ID A0A0F5JLH7_9BACT Unreviewed; 477 AA.
AC A0A0F5JLH7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:KKB58656.1};
GN ORFNames=HMPREF1536_01534 {ECO:0000313|EMBL:KKB58656.1};
OS Parabacteroides gordonii MS-1 = DSM 23371.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=1203610 {ECO:0000313|EMBL:KKB58656.1, ECO:0000313|Proteomes:UP000033035};
RN [1] {ECO:0000313|EMBL:KKB58656.1, ECO:0000313|Proteomes:UP000033035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS-1 {ECO:0000313|EMBL:KKB58656.1,
RC ECO:0000313|Proteomes:UP000033035};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Martens E., Sakamoto M.,
RA Benno Y., Suzuki N., Matsunaga N., Koshihara K., Seki M., Komiya H.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Parabacteroides gordonii DSM 23371.";
RL Submitted (APR-2013) 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:KKB58656.1}.
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DR EMBL; AQHW01000009; KKB58656.1; -; Genomic_DNA.
DR RefSeq; WP_028726431.1; NZ_KQ033919.1.
DR AlphaFoldDB; A0A0F5JLH7; -.
DR STRING; 1203610.HMPREF1536_01534; -.
DR PATRIC; fig|1203610.3.peg.1570; -.
DR HOGENOM; CLU_021594_4_1_10; -.
DR Proteomes; UP000033035; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd01357; Aspartase; 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; 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:KKB58656.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033035}.
FT DOMAIN 18..348
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 415..467
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 477 AA; 51933 MW; BE1063A5CD9F2500 CRC64;
MKTEFTGKTR TESDLIGARE IPAEALYGVQ TLRGIENFSI SKFHLNEYPL FINGLAITKM
AAAEANFALG LLTDEQYRAI TQACHEILDG QHHEQFPVDM IQGGAGTTSN MNANEVIANR
ALEIMGHQRG EYTYCSPNDH VNRSQSTNDA YPTAIHLGMY ATHLRLIPYL EALISSFRKK
GEEFAHIIKM GRTQLEDAVP MTLGQTFNGF ASILQDEIAH LDHAANDFLT VNMGATAIGT
GICAEPGYAE KCIEALRKIT GWNIKLSADL VGATSDTSCL VGYAAAMKRV AVKINKICND
LRLLASGPRC GLGEFNLPAM QPGSSIMPGK VNPVIPEVMN QIAYKVIGNE LCVTMAGEAA
QMELNAMEPV MAQCCFESAE LLMNGFETLR TLCVEGIIAN AEHCIEEVHH SIGVVTALNP
VIGYKNSTKI AKEALETGKS VYQLVLDHGI LTKEQLDTIL SPENMIHPVK LDIHPAK
//
