ID A0A261ETB9_9BIFI Unreviewed; 466 AA.
AC A0A261ETB9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Adenylosuccinate lyase {ECO:0000313|EMBL:OZG50122.1};
GN ORFNames=BOCO_0639 {ECO:0000313|EMBL:OZG50122.1};
OS Bombiscardovia coagulans.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bombiscardovia.
OX NCBI_TaxID=686666 {ECO:0000313|EMBL:OZG50122.1, ECO:0000313|Proteomes:UP000216004};
RN [1] {ECO:0000313|EMBL:OZG50122.1, ECO:0000313|Proteomes:UP000216004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22924 {ECO:0000313|EMBL:OZG50122.1,
RC ECO:0000313|Proteomes:UP000216004};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
CC -!- FUNCTION: Catalyzes two reactions in de novo purine nucleotide
CC biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-
CC succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-
CC D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-
CC carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate
CC (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP)
CC and fumarate. {ECO:0000256|ARBA:ARBA00025012}.
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:OZG50122.1}.
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DR EMBL; MWWS01000004; OZG50122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261ETB9; -.
DR Proteomes; UP000216004; Unassembled WGS sequence.
DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:InterPro.
DR GO; GO:0006188; P:IMP biosynthetic process; IEA:InterPro.
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; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR047136; PurB_bact.
DR InterPro; IPR013539; PurB_C.
DR PANTHER; PTHR43411; ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43411:SF1; ADENYLOSUCCINATE LYASE; 1.
DR Pfam; PF08328; ASL_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:OZG50122.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216004}.
FT DOMAIN 9..315
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 336..456
FT /note="Adenylosuccinate lyase PurB C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08328"
SQ SEQUENCE 466 AA; 52337 MW; 6392FCF9A46E6F23 CRC64;
MITLSPLDGR YRTQTAPLVE FLSEAALNKE RVEVEVEWMI LLSNGYNGNG SKPVLEGLQP
LSRTQISYLR SLVSDFNRSS MDELASFEAQ THHDVKAVEY FIDSRLDQSR DPQLSAIKPL
VHFGCTSEDV NNIAYARAIK TAITQVWLPS MQSLLEQLED MSQTYRSLPL LSMTHGQPAT
PTTLGKELAV YVYRLRRQLQ HLEQQEYLGK WNGATGTFGA SFVAVPHVDW IALSQHFVRE
RMGLDWNPLT TQIESHDWQA EVYSTISHSN RILHNLAVDI WMYISRGVFA QEPVQGATGS
STMPHKVNPI RFENAEANLE LSCSVLESLA STLVESRWQR DLTDSTTQRN VGVGLGHSLL
AIANLRSGLQ GIHPNTTVME TELDSNWEVL GEPIQTAMRA AALQGQSGMD HPYERVKELM
RGKDINQTDV EHFIHSLNFT AQDQDRLASL TPAQYTGLAD QLVDFE
//
