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Database: UniProt
Entry: W0L8H3_9GAMM
LinkDB: W0L8H3_9GAMM
Original site: W0L8H3_9GAMM 
ID   W0L8H3_9GAMM            Unreviewed;       457 AA.
AC   W0L8H3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=Z042_11160 {ECO:0000313|EMBL:AHG20118.1};
OS   Chania multitudinisentens RB-25.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Chania.
OX   NCBI_TaxID=1441930 {ECO:0000313|EMBL:AHG20118.1, ECO:0000313|Proteomes:UP000019030};
RN   [1] {ECO:0000313|EMBL:AHG20118.1, ECO:0000313|Proteomes:UP000019030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RB-25 {ECO:0000313|EMBL:AHG20118.1,
RC   ECO:0000313|Proteomes:UP000019030};
RA   Robson E.H.J.;
RT   "Isolation of Serratia multitudinisentens RB-25 from Ex-Landfill site.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AHG20118.1, ECO:0000313|Proteomes:UP000019030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RB-25 {ECO:0000313|EMBL:AHG20118.1,
RC   ECO:0000313|Proteomes:UP000019030};
RA   Chan K.-G.;
RL   Submitted (MAR-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}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the lyase 1 family.
CC       Argininosuccinate lyase subfamily. {ECO:0000256|ARBA:ARBA00005552}.
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DR   EMBL; CP007044; AHG20118.1; -; Genomic_DNA.
DR   RefSeq; WP_024913962.1; NZ_JAJC01000034.1.
DR   AlphaFoldDB; W0L8H3; -.
DR   STRING; 1441930.Z042_11160; -.
DR   KEGG; sfo:Z042_11160; -.
DR   PATRIC; fig|1441930.4.peg.2218; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_6; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000019030; 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:AHG20118.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019030}.
FT   DOMAIN          6..301
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          364..431
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   457 AA;  50111 MW;  F0CE2A37C77F8860 CRC64;
     MALWGGRFSQ AADQRFKQLN DSLRFDYRLA EQDIIGSVAW SKALVTVNVL TAMEQQQLEQ
     ALNALLAEVQ ADPQGIVNSD AEDIHSWVEQ KLIDKVGDLG KKLHTGRSRN DQVATDLKLW
     CKQQVGELHQ AIIQLQQALV ETAEANQDAV MPGYTHLQRA QPVTFAHWCL AYVEMLARDE
     SRLQDTLKRL DVSPLGCGAL AGTAYPIDRE QLAGWLGFAS ATRNSLDSVS DRDHVLELLS
     NAAISMVHLS RFAEDLIFFN SGEAAFVELS DRVTSGSSLM PQKKNPDALE LIRGKCGRVQ
     GALTGMMMTL KGLPLAYNKD MQEDKEGLFD ALDTWMDCLQ MAALVLDGIQ VKRPRCQEAA
     QQGYANSTEL ADYLVAKGVP FREAHHIVGE AVVEAIRQGK PLEDLPLADL QKFSSVIGSD
     VYPVLALQSC LDKRAAKGGV APQQVASAIS DAKQRLG
//
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