ID ARLY_BURM1 Reviewed; 469 AA.
AC P59615; A9AHK6; B3D2M5;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006};
GN Name=argH {ECO:0000255|HAMAP-Rule:MF_00006};
GN OrderedLocusNames=Bmul_0865, BMULJ_02393;
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12754231; DOI=10.1128/jb.185.11.3333-3343.2003;
RA Komatsu H., Imura Y., Ohori A., Nagata Y., Tsuda M.;
RT "Distribution and organization of auxotrophic genes on the multichromosomal
RT genome of Burkholderia multivorans ATCC 17616.";
RL J. Bacteriol. 185:3333-3343(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT 17616.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) 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; Evidence={ECO:0000255|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. {ECO:0000255|HAMAP-
CC Rule:MF_00006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABX14559.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB091437; BAC65282.1; -; Genomic_DNA.
DR EMBL; CP000868; ABX14559.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP009385; BAG44287.1; -; Genomic_DNA.
DR RefSeq; WP_006415883.1; NC_010804.1.
DR AlphaFoldDB; P59615; -.
DR SMR; P59615; -.
DR STRING; 395019.BMULJ_02393; -.
DR KEGG; bmj:BMULJ_02393; -.
DR KEGG; bmu:Bmul_0865; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_4; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000008815; Chromosome 1.
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; Arginine biosynthesis; Cytoplasm; Lyase;
KW Reference proteome.
FT CHAIN 1..469
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137752"
SQ SEQUENCE 469 AA; 51328 MW; 3BB758C89B16E3F1 CRC64;
MTSQLHKKGE AWSARFSEPM SELVKRYTSS VFFDKRLALV DIAGSLAHAN MLAAQKIISA
DDLAAIERGM AQIKGEIERG EFEWQLDLED VHLNIEARLT ALIGDAGKRL HTGRSRNDQV
ATDIRLWLRG EIDRIGGLLN DLRGALIDLA EQNADTIMPG FTHLQVAQPV TFGHHLLAYV
EMFSRDAERM RDCRTRVNRL PLGAAALAGT SYPIDRHAVA KSLGFDGICA NSLDAVSDRD
FAIEFTAAAA LVMTHVSRFS EELVLWMSPR VGFIDIADRF CTGSSIMPQK KNPDVPELAR
GKTGRVNGHL MALLTLMKGQ PLAYNKDNQE DKEPLFDTVD TVADTLRIFA EMVAGITVKP
DAMRAAALQG FSTATDLADY LVKRGLPFRD AHEAVAHAVK ICDDRGIDLA DLTLDEMKRE
LPNVAQLIGD DVFDYLTLEG SVASRNHPGG TAPDQVRAAA QAARAALGK
//
