ID A0A2M9H8T4_9BIFI Unreviewed; 503 AA.
AC A0A2M9H8T4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:PJM73213.1};
DE EC=4.3.1.1 {ECO:0000313|EMBL:PJM73213.1};
GN Name=aspA {ECO:0000313|EMBL:PJM73213.1};
GN ORFNames=CS006_03915 {ECO:0000313|EMBL:PJM73213.1};
OS Bifidobacterium primatium.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=2045438 {ECO:0000313|EMBL:PJM73213.1, ECO:0000313|Proteomes:UP000229095};
RN [1] {ECO:0000313|EMBL:PJM73213.1, ECO:0000313|Proteomes:UP000229095}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRE1 {ECO:0000313|Proteomes:UP000229095};
RA Mattarelli P., Modesto M., Puglisi E., Morelli L., Spezio C., Bonetti A.,
RA Sandri C.;
RT "Draft genome sequences of strains TRE 1, TRE 9, TRE H and TRI 7, isolated
RT from tamarins, belonging to four potential novel Bifidobacterium species.";
RL Submitted (OCT-2017) 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:PJM73213.1}.
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DR EMBL; PEBI01000002; PJM73213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9H8T4; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000229095; 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 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:PJM73213.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000229095}.
FT DOMAIN 26..357
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 424..474
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT REGION 481..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 54463 MW; 77DE5F67CCD0FCBC CRC64;
MARHATQVTR KTHRDTATRL EHDCIGSLEV PAKAYWGIHT ARALENFQVS NIPDSTHPQL
IKAYATIKRA CATANEELGL IPGVQAGAIR QACMEIEGGR WMDQFPVDVF QGGAGTSTNM
NMNEVIANRA LELAGHKKGD YEFIHPNDDV NKSQSTNDTY PAACKLALID ALGPLAQSTD
RLGRAFHRLA DRHANDVTVG RTQLQDAVPM TYGQQFHAFA SFLKSDIAAF ERLVPRLAVL
NLGATAIGTG ICANVEFRAS VTRHLAKMTG LPITAAPDPV AAVTDMSVYV AVSSAVKNLA
IHLKKAADDL RLLNSGPNSG FNDINVPARQ AGSSIMPGKV NPVIPECVNQ CVFSVFGMDT
TVQWAASEGQ LQLNAFDPVI IHSLLSGMEL ITRVMDVFRE ECVNGITVNV EVGRRYAETT
PSIAASLNEA IGYEDAVEIA KEAEASGRTV REVAGEKTNL PAKTLDELLA PITLSRRLGQ
TCRERVDRSG RERGNTRGDR ARR
//