ID Q2SX49_BURTA Unreviewed; 891 AA.
AC Q2SX49;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338};
DE EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338};
GN OrderedLocusNames=BTH_I1971 {ECO:0000313|EMBL:ABC38268.1};
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS CIP 106301 / E264).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC38268.1, ECO:0000313|Proteomes:UP000001930};
RN [1] {ECO:0000313|EMBL:ABC38268.1, ECO:0000313|Proteomes:UP000001930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC {ECO:0000313|Proteomes:UP000001930};
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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; CP000086; ABC38268.1; -; Genomic_DNA.
DR RefSeq; WP_009890338.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2SX49; -.
DR KEGG; bte:BTH_I1971; -.
DR HOGENOM; CLU_332539_0_0_4; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001930; Chromosome I.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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 InterPro; IPR009049; Argininosuccinate_lyase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR040570; LAL_C2.
DR PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR Pfam; PF13535; ATP-grasp_4; 1.
DR Pfam; PF18603; LAL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Lyase {ECO:0000313|EMBL:ABC38268.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 112..309
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 891 AA; 94939 MW; 076E41D560BE52BC CRC64;
MTGIFVFIES NTTGTGELLV RKALQRGLTP YFLTANRGKY PFLDAIRVVT VSLDTSDADR
VHGFVASLDG VAGVMSSSEY FIEVASEVAR RLGLPTANTE ATRICRDKKR LADVLAEHGI
DAPRTHALSL DAEADADADV APALAGLAYP VVVKPRMGSG SVGVRLCANA DEAGAHCAVL
RRAGTRAALV QTYVEGDEYS VETLTIARNT QIVGIVRKRL GRAPHFVEIG HDYPAPLSSP
QRERIERTVL RALDAVGYTF GPAHTELRVR GETVTIIEIN PRLAGGLIPV LLGEVFDVDL
LDHVLDMWLG AAGFADLTAK RYGAIRFALP AREGVLGSAL AIPAEIAAMP ELRHFHPIAQ
PGDALRLEGS FRDRIAAVVC AGDDRESVEA LADRAVAELC ADIDGDAPAP AAAPNPATPG
LPPRLQEIVY GDGAGDAPLA ELDYLFDLNE AHLVMLGATR LVALDRIRPL LDAHRRLRRA
GYAPLLARPK PRGLYMLVEG YLIETLGEGV GGVLQTGRSR NDINATTTKL HLRDGTSRAF
DALWRLRRSL IFKASANVDR AFPIYSQYQP ALPGTLAHQL LAYDDALANE IHALFALFQH
IDVCPLGAGA GGGTTLPIDP EFVCRLLGFE QPASNSLDAV ANRSGVVHFL SAMNATGLVL
SRLAQDLQIW TTAEFALVSL PAALTGGSSM LPQKKNPFLV EFVKSRAGVP FGALASCSAA
LGKTPYTNSF EAGSPMNGLI AQACAAIEEA AAVAALLIDG LEAADARIDA HLKDTGVVAM
AVAEALVVRR SLDFRSAHTQ VAQAVRDSVA RGRSSHDALV ALDPDFASRA PLDWARSHRF
GGGPGAADLN QGVARACRAL ADDEAAFRRK QDVWREAEQM RRLAAQQLAG D
//
