ID A9WLL8_RENSM Unreviewed; 471 AA.
AC A9WLL8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Adenylosuccinate lyase {ECO:0000313|EMBL:ABY22376.1};
DE EC=4.3.2.2 {ECO:0000313|EMBL:ABY22376.1};
GN OrderedLocusNames=RSal33209_0629 {ECO:0000313|EMBL:ABY22376.1};
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Renibacterium.
OX NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY22376.1, ECO:0000313|Proteomes:UP000002007};
RN [1] {ECO:0000313|Proteomes:UP000002007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC {ECO:0000313|Proteomes:UP000002007};
RX PubMed=18723615; DOI=10.1128/JB.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
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}.
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DR EMBL; CP000910; ABY22376.1; -; Genomic_DNA.
DR RefSeq; WP_012244077.1; NC_010168.1.
DR AlphaFoldDB; A9WLL8; -.
DR STRING; 288705.RSal33209_0629; -.
DR KEGG; rsa:RSal33209_0629; -.
DR eggNOG; COG0015; Bacteria.
DR HOGENOM; CLU_025566_2_0_11; -.
DR Proteomes; UP000002007; Chromosome.
DR GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
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:ABY22376.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002007}.
FT DOMAIN 23..318
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 339..459
FT /note="Adenylosuccinate lyase PurB C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08328"
SQ SEQUENCE 471 AA; 51435 MW; 4CDC6B0DA29AEE3C CRC64;
MPSASSSRYS LAETTIALGP LDGRYRSAVA PLVDYLSEAA LNRDRIAVEV EWLIHLTDQA
VLPGAGQLSG EQKDQLRSIV NEFDVESVTE LAEIERVTVH DVKAVEYYIG RRLAGIGIEQ
LKPLVHFACT SEDMNNLSYA LGIKGAVENV WLPAARGLSG KLHEMAEANR AVPMLSRTHG
QPATPTTLGK ELAVLAHRLD RQLRRIEKAE YLGKINGATG TYAAHYAAAP QTDWQAISQS
FVEGLGLDWN PLTTQIESHD WQAELYADIA RFNRILHNLC TDVWSYISIG YFTQIPVAGA
TGSSTMPHKV NPIRFENAEA NLEISSALLD NLAATLITSR WQRDLTDSSS QRNIGVAIGH
SVLAIGNVLG GLGRLNTAEA VLADDLDHNW EILGEAVQTV MRAEAIAGVP GMEDPYERLK
DLTRGQRVDA TRMREFVSGL GLSAEAEARL KDLTPGRYIG IAEQLVDHLG E
//
