ID K0HW69_9BURK Unreviewed; 489 AA.
AC K0HW69;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 62.
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 ORFNames=C380_06960 {ECO:0000313|EMBL:AFU45102.1};
OS Acidovorax sp. KKS102.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU45102.1, ECO:0000313|Proteomes:UP000006306};
RN [1] {ECO:0000313|EMBL:AFU45102.1, ECO:0000313|Proteomes:UP000006306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KKS102 {ECO:0000313|EMBL:AFU45102.1,
RC ECO:0000313|Proteomes:UP000006306};
RX PubMed=23209225; DOI=10.1128/JB.01848-12;
RA Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT Polychlorinated-Biphenyl Degrader.";
RL J. Bacteriol. 194:6970-6971(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, 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; CP003872; AFU45102.1; -; Genomic_DNA.
DR RefSeq; WP_015013143.1; NC_018708.1.
DR AlphaFoldDB; K0HW69; -.
DR STRING; 358220.C380_06960; -.
DR KEGG; ack:C380_06960; -.
DR PATRIC; fig|358220.3.peg.1411; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_4; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000006306; 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:AFU45102.1}.
FT DOMAIN 29..321
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 396..464
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 489 AA; 53574 MW; D34598884D6CDFA8 CRC64;
MSKAQATSAD SAPSHNQLDT KAQAWSALFS EPMSDLVKRY TSSVFFDKRL WQADIAGSLA
HAEMLAAQGI ISPEDHASIQ RGMAQIKEEI ESGAFEWKLD LEDVHLNIEA RLTQLVGDAG
KRLHTGRSRN DQVATDVRLW LRGEIDLIGD LLKELQVSLV DVAEQNVEVI LPGFTHLQVA
QPVSFGHHML AYVEMFKRDA ERMADVRRRT NVLPLGSAAL AGTTYPLDRE RVAKTLGMDG
VCQNSLDAVS DRDFAIEFTA AASLCMVHVS RLSEELIIWM SQNFGFIKIA DRFTTGSSIM
PQKKNPDVPE LARGKTGRVV GHLMGLITLM KGQPLAYNKD NQEDKEPLFD TVDTLKDTLR
IFAEMVGGQL NPATGKKEGG ITVNAQAMEQ AALKGYATAT DLADYLVKKG LPFRDAHETV
AHAVKAATSH ACDLSELPLN VLQGFHPAIE KDVYECLSLR GSLNARNTLG GTAPAQVRAQ
LARHRARLA
//
