ID U5N7J2_9BURK Unreviewed; 487 AA.
AC U5N7J2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000256|HAMAP-Rule:MF_00006};
GN Name=argH {ECO:0000256|HAMAP-Rule:MF_00006,
GN ECO:0000313|EMBL:AGX86263.1};
GN ORFNames=Cenrod_0129 {ECO:0000313|EMBL:AGX86263.1};
OS Candidatus Symbiobacter mobilis CR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX86263.1, ECO:0000313|Proteomes:UP000017184};
RN [1] {ECO:0000313|EMBL:AGX86263.1, ECO:0000313|Proteomes:UP000017184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:AGX86263.1};
RX PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., Rohde M.,
RA Overmann J., Bryant D.A.;
RT "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT phototrophic consortium "Chlorochromatium aggregatum".";
RL Genome Biol. 14:R127-R127(2013).
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, ECO:0000256|HAMAP-
CC Rule:MF_00006};
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, ECO:0000256|HAMAP-Rule:MF_00006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00006}.
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DR EMBL; CP004885; AGX86263.1; -; Genomic_DNA.
DR RefSeq; WP_022771086.1; NC_022576.1.
DR AlphaFoldDB; U5N7J2; -.
DR STRING; 946483.Cenrod_0129; -.
DR KEGG; cbx:Cenrod_0129; -.
DR PATRIC; fig|946483.4.peg.127; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_4; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000017184; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR CDD; cd01359; Argininosuccinate_lyase; 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 HAMAP; MF_00006; Arg_succ_lyase; 1.
DR InterPro; IPR029419; Arg_succ_lyase_C.
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 NCBIfam; TIGR00838; argH; 1.
DR PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR Pfam; PF14698; ASL_C2; 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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_00006}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:AGX86263.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017184}.
FT DOMAIN 18..315
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 390..457
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 487 AA; 54421 MW; 864973A399659C90 CRC64;
MPSNQFDHKQ QAWSALFSEP MHECVQRYTA SVSFDQRLWK VDIAASLAHA EMLCHQGILC
PQDYADICRG METITQEIES GSFVWKWELE DVHLNLEARL TALVGDAGKR LHTGRSRNDQ
VATDVRLWLR AEIDKLILAL AALQRALVEV AAEHVDVILP GFTHLQVAQP VSFAHHLLAY
VEMFDRDTQR LREVRRRTNH LPLGAAALAG TSYPLDRERV ACTLGMVDEQ GCPQLCQNSI
DAVSDRDFAI EFTASASLCM VHLSRFSEEL VLWTSQQFGF VRIADRFTTG SSIMPQKKNP
DVAELARGKT GRVVGHLMGL LMLMKGQPLA YNKDNQEDKE PLFDTVDTLW NTLRIFAEMI
GGQIDPQTGH KEGGLQLCSA AMASAARVGF STATDLADYL VRKGLPFRDA HEIVARAVRE
AIATNTDLCE WPLERLQSLH PHIQEDVYTA ISLRGALESR HTVGGTAPNR VREQLARHAQ
RLACLLK
//
