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Database: UniProt
Entry: C7RF84_ANAPD
LinkDB: C7RF84_ANAPD
Original site: C7RF84_ANAPD 
ID   C7RF84_ANAPD            Unreviewed;       472 AA.
AC   C7RF84;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Fumarate lyase {ECO:0000313|EMBL:ACV28145.1};
GN   OrderedLocusNames=Apre_0092 {ECO:0000313|EMBL:ACV28145.1};
OS   Anaerococcus prevotii (strain ATCC 9321 / DSM 20548 / JCM 6508 / NCTC 11806
OS   / PC1) (Peptostreptococcus prevotii) (Peptococcus prevotii).
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Anaerococcus.
OX   NCBI_TaxID=525919 {ECO:0000313|EMBL:ACV28145.1, ECO:0000313|Proteomes:UP000002294};
RN   [1] {ECO:0000313|EMBL:ACV28145.1, ECO:0000313|Proteomes:UP000002294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9321 / DSM 20548 / JCM 6508 / NCTC 11806 / PC1
RC   {ECO:0000313|Proteomes:UP000002294};
RX   PubMed=21304652; DOI=10.4056/sigs.24194;
RA   Labutti K., Pukall R., Steenblock K., Glavina Del Rio T., Tice H.,
RA   Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L.,
RA   Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Saunders E., Brettin T., Detter J.C., Han C., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Anaerococcus prevotii type strain (PC1).";
RL   Stand. Genomic Sci. 1:159-165(2009).
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DR   EMBL; CP001708; ACV28145.1; -; Genomic_DNA.
DR   RefSeq; WP_012803564.1; NC_013171.1.
DR   AlphaFoldDB; C7RF84; -.
DR   STRING; 525919.Apre_0092; -.
DR   KEGG; apr:Apre_0092; -.
DR   eggNOG; COG1027; Bacteria.
DR   HOGENOM; CLU_021594_4_1_9; -.
DR   OrthoDB; 9802809at2; -.
DR   Proteomes; UP000002294; Chromosome.
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:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ACV28145.1}.
FT   DOMAIN          12..341
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          407..460
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   472 AA;  51914 MW;  FFA546751FE7E14A CRC64;
     MQNFRIESDS LGEIKIDKEA YYGANSKRAL DNFPITRRPM DPFLVRAIVE VKKACAIENN
     KVGILSDRKK DAIVSACEKV LAGEFLDNFV VDPIQGGAGT SFNMNVNEVI ANIANEIMGG
     GIGTYEFIHP NDHVNKGQST NDVIPSAGKI ALIRYIEELK EEVNNLIKSL ENKACEFDSY
     IKMGRTQLQD AVPITLGQEF RAYARAIRRD YERLGAAIRQ LSYLNLGGTA IGTGLNADDS
     YIKEVVPSLA KICDIDLYQA EDLVDATQNL DCFLFTSSVL KALASNLSKI SNDLRLLSSG
     PTTGISDYNL PAKQAGSSIM PGKVNPVIPE VVNQVAFLVI GNDMTVTMAV EGGQLELNAF
     EPIIFYSLFE SLKTLKAAIH TLYTNCIDGI TSDKKKLEKR VENSVAIITP FAPHIGYDRA
     SKVAKESLRT GVSVREILIR DKIMTSDEID KILDYENMTK PGILDEDHIS KD
//
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