UniProt: A0A0B6WZU1

Database: UniProt
Entry: A0A0B6WZU1_9BACT

LinkDB:  A0A0B6WZU1_9BACT 
Original site:  A0A0B6WZU1_9BACT

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (6)   
   Pfam (2)   
All databases (14)   

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ID   A0A0B6WZU1_9BACT        Unreviewed;       506 AA.
AC   A0A0B6WZU1;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=PYK22_02841 {ECO:0000313|EMBL:CDM66803.1};
OS   Pyrinomonas methylaliphatogenes.
OC   Bacteria; Acidobacteriota; Blastocatellia; Blastocatellales;
OC   Pyrinomonadaceae; Pyrinomonas.
OX   NCBI_TaxID=454194 {ECO:0000313|EMBL:CDM66803.1, ECO:0000313|Proteomes:UP000031518};
RN   [1] {ECO:0000313|EMBL:CDM66803.1, ECO:0000313|Proteomes:UP000031518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K22 {ECO:0000313|EMBL:CDM66803.1,
RC   ECO:0000313|Proteomes:UP000031518};
RA   Stott M.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDM66803.1, ECO:0000313|Proteomes:UP000031518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K22 {ECO:0000313|EMBL:CDM66803.1,
RC   ECO:0000313|Proteomes:UP000031518};
RA   Lee K.C.Y., Power J.F., Dunfield P.F., Morgan X.C., Huttenhower C.,
RA   Stott M.B.;
RT   "Complete genome sequence of Pyrinomonas methylaliphatogenes type strain
RT   K22T.";
RL   Submitted (JAN-2015) 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;
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; CBXV010000008; CDM66803.1; -; Genomic_DNA.
DR   RefSeq; WP_060635699.1; NZ_CBXV010000008.1.
DR   AlphaFoldDB; A0A0B6WZU1; -.
DR   STRING; 454194.PYK22_02841; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000031518; Unassembled WGS sequence.
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; 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.
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:CDM66803.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031518}.
FT   DOMAIN          43..294
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          363..427
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   506 AA;  56386 MW;  773B83B403D7AE78 CRC64;
     MEQKERFPAP AYAENVLAEI FEDAKRLFLD ALIEVDIAHA VMLAERGIIS REDACQILRA
     LEGMNRDEIL AARYDGSCED LFFYLQQRLS EKCGEETAGR LHTARSRNDI DVTIYRMRLR
     RDLLALIRAV MDLRCALLDQ AALHHETTIP AYTHTQPAQP TTLAHYLLAM AEVLSRDVAR
     LQRAFENANL SPLGACAITT TGFDIDRART AELLGFEGVA ENSYAAISAV DYLTEAMGAV
     AVAMVNVGRF AQDFLLMATR EFGFLRLSDG YVQISSIMPQ KRNPVALEHV RALASCALAE
     AQGAFTVVHN TPFGDVNDAE DDLQPLIWRA LHDARRATAV FAAAISHAQF DIERLRERAA
     EDFITVTELA DAIVRREGLP FRVAHQIVAS FVRRTQGVIA TIQTSGESLH ADLLAQAAHK
     LLQETAREIL GRTLSLSPEE TRRALDPLNF VRVRGVMGGP SPEETRRILQ ASRARAELDE
     GWYRKRTELM TTYPEKLREA TRALGC
//

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