ID A0A345UJG7_9BACT Unreviewed; 430 AA.
AC A0A345UJG7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338};
DE EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338};
GN ORFNames=CYPRO_1363 {ECO:0000313|EMBL:AXJ00619.1};
OS Cyclonatronum proteinivorum.
OC Bacteria; Balneolota; Balneolia; Balneolales; Cyclonatronaceae;
OC Cyclonatronum.
OX NCBI_TaxID=1457365 {ECO:0000313|EMBL:AXJ00619.1, ECO:0000313|Proteomes:UP000254808};
RN [1] {ECO:0000313|EMBL:AXJ00619.1, ECO:0000313|Proteomes:UP000254808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Omega {ECO:0000313|EMBL:AXJ00619.1,
RC ECO:0000313|Proteomes:UP000254808};
RA Toshchakov S.V., Korzhenkov A., Samarov N.I., Kublanov I.V., Muntyan M.S.,
RA Sorokin D.Y.;
RT "Phenotypic and genomic properties of Cyclonatronum proteinivorum gen.
RT nov., sp. nov., a haloalkaliphilic bacteroidete from soda lakes possessing
RT Na+-translocating rhodopsin.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(N(omega)-L-arginino)succinate = fumarate + L-arginine;
CC Xref=Rhea:RHEA:24020, ChEBI:CHEBI:29806, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:57472; EC=4.3.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000985};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00004941}.
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DR EMBL; CP027806; AXJ00619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345UJG7; -.
DR KEGG; cprv:CYPRO_1363; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000254808; Chromosome.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; 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; IPR009049; Argininosuccinate_lyase.
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 PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Lyase {ECO:0000313|EMBL:AXJ00619.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000254808}.
FT DOMAIN 34..306
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
SQ SEQUENCE 430 AA; 46467 MW; 66911FE4FA706B96 CRC64;
MSLWKPSSSQ TPDSVRDKIH AFTAGEDYLL DRELLPWDVR ASMAHAKGLV KAGLLSAEEG
DALLEGLTEI LSLCQAGKFT VLPDQEDCHT AIEAKLSEML GETGKKIHTG RSRNDQVLAA
MRLFELHALA EIRNNAQKLG GQFLVLAARG ENLPMPGYTH TQPAMLSSAG MWAAAFAELL
YFDLIQLETV ERLLDHSPLG TAAGYGVNLP LQRDFVAQEA GFGQLLINPI AAQNSRAKME
IALVNALESL AGTLGQFATD CVTYASNSFG FFALDDALCT GSSIMPQKKN PDSAELLRAS
AGELTGLGAS LRAVSRNLGS GYHRDMQLTK KYAMQALRLT SQLLEVAHLI AEGLHFKADN
MAAACGPELF AADHANELVR RGMSFREAYF EIKSKLDSLE VPDLQAALQA KSHRGGTGNL
DVEALRERLG
//
