ID I4VNQ6_9GAMM Unreviewed; 431 AA.
AC I4VNQ6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338};
DE EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338};
GN ORFNames=UU9_11405 {ECO:0000313|EMBL:EIL88847.1};
OS Rhodanobacter fulvus Jip2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163408 {ECO:0000313|EMBL:EIL88847.1, ECO:0000313|Proteomes:UP000004210};
RN [1] {ECO:0000313|EMBL:EIL88847.1, ECO:0000313|Proteomes:UP000004210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jip2T {ECO:0000313|Proteomes:UP000004210};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
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}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the lyase 1 family.
CC Argininosuccinate lyase subfamily. {ECO:0000256|ARBA:ARBA00005552}.
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:EIL88847.1}.
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DR EMBL; AJXU01000044; EIL88847.1; -; Genomic_DNA.
DR RefSeq; WP_007081914.1; NZ_AJXU01000044.1.
DR AlphaFoldDB; I4VNQ6; -.
DR STRING; 1163408.UU9_11405; -.
DR PATRIC; fig|1163408.3.peg.2332; -.
DR eggNOG; COG0165; Bacteria.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000004210; Unassembled WGS sequence.
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 NCBIfam; TIGR00838; argH; 1.
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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Lyase {ECO:0000313|EMBL:EIL88847.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004210}.
FT DOMAIN 34..299
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
SQ SEQUENCE 431 AA; 46845 MW; EB55D2DD6591EC88 CRC64;
MTQPLWQKDG IKIDAKIMQF LAGNDVLLDR EFFLHDITAS KAHVEGLANI GVIGADEAAA
LKRELDALAE DFRSGAFVLD ERHEDGHSAI EARLTERLGD AGRRVHTGRS RNDQILVATR
LWLKEKLATL QTLCHDIAQV CLDRAAEAAL PLPGYTHLQR AVVSSTAMWF AGFAEGFTDN
ALRAQQTAVW IDANPLGTAA GYGVNLPLDR AHTTQALGFA RMQVSPVYAQ LSRGKFEMAV
LEAIASALLD LRRMAWDLSL FTTAEFNFVK LPAEYTTGSS IMPNKRNPDV IELLRASYAS
VAAARCEIEQ LLSLPSGYQR DLQFSKGSLF HGVTHGLSAL ELVPDLLARF QWNEPAMRAA
IEPSMYATDV AIEQAAAGVP FRDAYRAAAE AASAAGAGRT PEASLEARVS PGAGHDLKLD
QVQQRLDAIR G
//
