ID S3BE53_9MICO Unreviewed; 485 AA.
AC S3BE53;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:EPD86919.1};
GN ORFNames=HMPREF1529_00095 {ECO:0000313|EMBL:EPD86919.1};
OS Microbacterium sp. oral taxon 186 str. F0373.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1203549 {ECO:0000313|EMBL:EPD86919.1, ECO:0000313|Proteomes:UP000014414};
RN [1] {ECO:0000313|EMBL:EPD86919.1, ECO:0000313|Proteomes:UP000014414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0373 {ECO:0000313|EMBL:EPD86919.1,
RC ECO:0000313|Proteomes:UP000014414};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Kirega A., Dewhirst F.D.,
RA Izard J., 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 Microbacterium sp. oral taxon 186 F0373.";
RL Submitted (MAY-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:EPD86919.1}.
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DR EMBL; ATCC01000001; EPD86919.1; -; Genomic_DNA.
DR RefSeq; WP_016463278.1; NZ_KE150457.1.
DR AlphaFoldDB; S3BE53; -.
DR PATRIC; fig|1203549.3.peg.94; -.
DR HOGENOM; CLU_021594_4_1_11; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000014414; 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:EPD86919.1}.
FT DOMAIN 15..346
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 413..463
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 485 AA; 52030 MW; FAB26EE3A8140650 CRC64;
MAFDATMRTE TDSLGSMEIP ADAYWGIHTA RALENFPISM RPISVYKDLV TALAMVKQAS
ARANLEIGVL DAERADLIDR ASQRVIDGEF HDQFVVGVVQ GGAGTSTNMN ANEVITNIAL
ELAGRPKGDY AYLSPIDHTN RSQSTNDVYP TAVKVGLSLD LKTLLEELDL LRQSFLAKAV
EFHDILKIGR TQLQDAVPMT LGQEFHGFAT TLGYDHQRLT ENAYLLFEIN MGATAIGTGI
TTHPGYAPAV LRHLREITGL DLATADDLVE ATSDTGSFMS FSSTLKRNAI KLSKIANDLR
LLSSGPQAGL GEINLPARQA GSSIMPGKVN PVIPEVVNQV AFSVAGADLT VTMAVEGGQL
QLNAFEPIIA HSIFQSITWM RRAMRTFRIN CVDGITANRE RLGAMVGSSV GVVTALTPFI
GYAASAALAK TALLTHRNVG DLVVEAGLMT RDEVDKQLSP ARLSGLEAIT QAIPVVQPAE
NLVES
//
