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
//